TY  - DATA
AU  - Szwej, Emilia
AU  - Devocelle, Marc
AU  - Kenny, Shane T.
AU  - Guzik, Maciej
AU  - O'Connor, Stephen
AU  - Nikodinović-Runić, Jasmina
AU  - Radivojević, Jelena
AU  - Maslak, Veselin
AU  - Byrne, Annete T.
AU  - Gallagher, William M.
AU  - Zulian, Qun Ren
AU  - Zinn, Manfred
AU  - O'Connor, Kevin E.
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3451
PB  - Elsevier Science Bv, Amsterdam
T2  - Journal of Biotechnology
T1  - Supplementary data for article: Szwej, E.; Devocelle, M.; Kenny, S.; Guzik, M.; O’Connor, S.; Nikodinović-Runić, J.; Radivojevic, J.; Maslak, V.; Byrne, A. T.; Gallagher, W. M.; et al. The Chain Length of Biologically Produced (R)-3-Hydroxyalkanoic Acid Affects Biological Activity and Structure of Anti-Cancer Peptides. Journal of Biotechnology 2015, 204, 7–12. https://doi.org/10.1016/j.jbiotec.2015.02.036
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3451
ER  - 

@misc{
author = "Szwej, Emilia and Devocelle, Marc and Kenny, Shane T. and Guzik, Maciej and O'Connor, Stephen and Nikodinović-Runić, Jasmina and Radivojević, Jelena and Maslak, Veselin and Byrne, Annete T. and Gallagher, William M. and Zulian, Qun Ren and Zinn, Manfred and O'Connor, Kevin E.",
year = "2015",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Journal of Biotechnology",
title = "Supplementary data for article: Szwej, E.; Devocelle, M.; Kenny, S.; Guzik, M.; O’Connor, S.; Nikodinović-Runić, J.; Radivojevic, J.; Maslak, V.; Byrne, A. T.; Gallagher, W. M.; et al. The Chain Length of Biologically Produced (R)-3-Hydroxyalkanoic Acid Affects Biological Activity and Structure of Anti-Cancer Peptides. Journal of Biotechnology 2015, 204, 7–12. https://doi.org/10.1016/j.jbiotec.2015.02.036",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3451"
}

Szwej, E., Devocelle, M., Kenny, S. T., Guzik, M., O'Connor, S., Nikodinović-Runić, J., Radivojević, J., Maslak, V., Byrne, A. T., Gallagher, W. M., Zulian, Q. R., Zinn, M.,& O'Connor, K. E.. (2015). Supplementary data for article: Szwej, E.; Devocelle, M.; Kenny, S.; Guzik, M.; O’Connor, S.; Nikodinović-Runić, J.; Radivojevic, J.; Maslak, V.; Byrne, A. T.; Gallagher, W. M.; et al. The Chain Length of Biologically Produced (R)-3-Hydroxyalkanoic Acid Affects Biological Activity and Structure of Anti-Cancer Peptides. Journal of Biotechnology 2015, 204, 7–12. https://doi.org/10.1016/j.jbiotec.2015.02.036. in Journal of Biotechnology
Elsevier Science Bv, Amsterdam..
https://hdl.handle.net/21.15107/rcub_cherry_3451

Szwej E, Devocelle M, Kenny ST, Guzik M, O'Connor S, Nikodinović-Runić J, Radivojević J, Maslak V, Byrne AT, Gallagher WM, Zulian QR, Zinn M, O'Connor KE. Supplementary data for article: Szwej, E.; Devocelle, M.; Kenny, S.; Guzik, M.; O’Connor, S.; Nikodinović-Runić, J.; Radivojevic, J.; Maslak, V.; Byrne, A. T.; Gallagher, W. M.; et al. The Chain Length of Biologically Produced (R)-3-Hydroxyalkanoic Acid Affects Biological Activity and Structure of Anti-Cancer Peptides. Journal of Biotechnology 2015, 204, 7–12. https://doi.org/10.1016/j.jbiotec.2015.02.036. in Journal of Biotechnology. 2015;.
https://hdl.handle.net/21.15107/rcub_cherry_3451 .

Szwej, Emilia, Devocelle, Marc, Kenny, Shane T., Guzik, Maciej, O'Connor, Stephen, Nikodinović-Runić, Jasmina, Radivojević, Jelena, Maslak, Veselin, Byrne, Annete T., Gallagher, William M., Zulian, Qun Ren, Zinn, Manfred, O'Connor, Kevin E., "Supplementary data for article: Szwej, E.; Devocelle, M.; Kenny, S.; Guzik, M.; O’Connor, S.; Nikodinović-Runić, J.; Radivojevic, J.; Maslak, V.; Byrne, A. T.; Gallagher, W. M.; et al. The Chain Length of Biologically Produced (R)-3-Hydroxyalkanoic Acid Affects Biological Activity and Structure of Anti-Cancer Peptides. Journal of Biotechnology 2015, 204, 7–12. https://doi.org/10.1016/j.jbiotec.2015.02.036" in Journal of Biotechnology (2015),
https://hdl.handle.net/21.15107/rcub_cherry_3451 .

TY  - JOUR
AU  - Szwej, Emilia
AU  - Devocelle, Marc
AU  - Kenny, Shane T.
AU  - Guzik, Maciej
AU  - O'Connor, Stephen
AU  - Nikodinović-Runić, Jasmina
AU  - Radivojević, Jelena
AU  - Maslak, Veselin
AU  - Byrne, Annete T.
AU  - Gallagher, William M.
AU  - Zulian, Qun Ren
AU  - Zinn, Manfred
AU  - O'Connor, Kevin E.
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1712
AB  - Conjugation of DP18L peptide with (R)-3-hydroxydecanoic acid, derived from the biopolymer polyhydroxyalkanoate, enhances its anti-cancer activity (O'Connor et al., 2013. Biomaterials 34, 2710-2718). However, it is unknown if other (R)-3-hydroxyalkanoic acids (R3HA5) can enhance peptide activity, if chain length affects enhancement, and what effect R3HA5 have on peptide structure. Here we show that the degree of enhancement of peptide (DP18L) anti-cancer activity by R3HA5 is carbon chain length dependent. In all but one example the R3HA conjugated peptides were more active against cancer cells than the unconjugated peptides. However, R3HA5 with 9 and 10 carbons were most effective at improving DPI 8L activity. DPI 8L peptide variant DPI 7L, missing a hydrophobic amino acid (leucine residue 4) exhibited lower efficacy against MiaPaCa cells. Circular dichroism analysis showed DP17L had a lower alpha helix content and the conjugation of any R3HA ((R)-3-hydroxyhexanoic acid to (R)-3-hydroxydodecanoic acid) to DPI 7L returned the helix content back to levels of DPI 8L. However (R)-3-hydroxyhexanoic did not enhance the anti-cancer activity of DPI 7L and at least 7 carbons were needed in the R3HA to enhance activity of D17L. DP17L needs a longer chain R3HA to achieve the same activity as DP18L conjugated to an R3HA. As a first step to assess the synthetic potential of polyhydroxyalkanoate derived R3HA5, (R)-3-hydroxydecanoic acid was synthetically converted to (+/-)3-chlorodecanoic acid, which when conjugated to DP18L improved its antiproliferative activity against MiaPaCa cells.
PB  - Elsevier Science Bv, Amsterdam
T2  - Journal of Biotechnology
T1  - The chain length of biologically produced (R)-3-hydroxyalkanoic acid affects biological activity and structure of anti-cancer peptides
VL  - 204
SP  - 7
EP  - 12
DO  - 10.1016/j.jbiotec.2015.02.036
ER  - 

@article{
author = "Szwej, Emilia and Devocelle, Marc and Kenny, Shane T. and Guzik, Maciej and O'Connor, Stephen and Nikodinović-Runić, Jasmina and Radivojević, Jelena and Maslak, Veselin and Byrne, Annete T. and Gallagher, William M. and Zulian, Qun Ren and Zinn, Manfred and O'Connor, Kevin E.",
year = "2015",
abstract = "Conjugation of DP18L peptide with (R)-3-hydroxydecanoic acid, derived from the biopolymer polyhydroxyalkanoate, enhances its anti-cancer activity (O'Connor et al., 2013. Biomaterials 34, 2710-2718). However, it is unknown if other (R)-3-hydroxyalkanoic acids (R3HA5) can enhance peptide activity, if chain length affects enhancement, and what effect R3HA5 have on peptide structure. Here we show that the degree of enhancement of peptide (DP18L) anti-cancer activity by R3HA5 is carbon chain length dependent. In all but one example the R3HA conjugated peptides were more active against cancer cells than the unconjugated peptides. However, R3HA5 with 9 and 10 carbons were most effective at improving DPI 8L activity. DPI 8L peptide variant DPI 7L, missing a hydrophobic amino acid (leucine residue 4) exhibited lower efficacy against MiaPaCa cells. Circular dichroism analysis showed DP17L had a lower alpha helix content and the conjugation of any R3HA ((R)-3-hydroxyhexanoic acid to (R)-3-hydroxydodecanoic acid) to DPI 7L returned the helix content back to levels of DPI 8L. However (R)-3-hydroxyhexanoic did not enhance the anti-cancer activity of DPI 7L and at least 7 carbons were needed in the R3HA to enhance activity of D17L. DP17L needs a longer chain R3HA to achieve the same activity as DP18L conjugated to an R3HA. As a first step to assess the synthetic potential of polyhydroxyalkanoate derived R3HA5, (R)-3-hydroxydecanoic acid was synthetically converted to (+/-)3-chlorodecanoic acid, which when conjugated to DP18L improved its antiproliferative activity against MiaPaCa cells.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Journal of Biotechnology",
title = "The chain length of biologically produced (R)-3-hydroxyalkanoic acid affects biological activity and structure of anti-cancer peptides",
volume = "204",
pages = "7-12",
doi = "10.1016/j.jbiotec.2015.02.036"
}

Szwej, E., Devocelle, M., Kenny, S. T., Guzik, M., O'Connor, S., Nikodinović-Runić, J., Radivojević, J., Maslak, V., Byrne, A. T., Gallagher, W. M., Zulian, Q. R., Zinn, M.,& O'Connor, K. E.. (2015). The chain length of biologically produced (R)-3-hydroxyalkanoic acid affects biological activity and structure of anti-cancer peptides. in Journal of Biotechnology
Elsevier Science Bv, Amsterdam., 204, 7-12.
https://doi.org/10.1016/j.jbiotec.2015.02.036

Szwej E, Devocelle M, Kenny ST, Guzik M, O'Connor S, Nikodinović-Runić J, Radivojević J, Maslak V, Byrne AT, Gallagher WM, Zulian QR, Zinn M, O'Connor KE. The chain length of biologically produced (R)-3-hydroxyalkanoic acid affects biological activity and structure of anti-cancer peptides. in Journal of Biotechnology. 2015;204:7-12.
doi:10.1016/j.jbiotec.2015.02.036 .

Szwej, Emilia, Devocelle, Marc, Kenny, Shane T., Guzik, Maciej, O'Connor, Stephen, Nikodinović-Runić, Jasmina, Radivojević, Jelena, Maslak, Veselin, Byrne, Annete T., Gallagher, William M., Zulian, Qun Ren, Zinn, Manfred, O'Connor, Kevin E., "The chain length of biologically produced (R)-3-hydroxyalkanoic acid affects biological activity and structure of anti-cancer peptides" in Journal of Biotechnology, 204 (2015):7-12,
https://doi.org/10.1016/j.jbiotec.2015.02.036 . .

TY  - JOUR
AU  - Narančić, Tanja
AU  - Davis, Reeta
AU  - Nikodinović-Runić, Jasmina
AU  - O'Connor, Kevin E.
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1690
AB  - Recent developments in biocatalysis, where implementation beyond the laboratory has been demonstrated, are explored: the use of transglutaminases to modify foods, reduce allergenicity and produce advanced materials, lipases for biodiesel production, and transaminases for biochemical production. The availability and application of enzymes at pilot and larger scale opens up possibilities for further improvements of biocatalyst-based processes and the development of new processes. Enzyme production, stability, activity, re-use, and product retrieval are common challenges for biocatalytic processes. We explore recent advances in biocatalysis within the process chain, such as protein engineering, enzyme expression, and biocatalyst immobilization, in the context of these challenges.
PB  - Springer, Dordrecht
T2  - Biotechnology Letters
T1  - Recent developments in biocatalysis beyond the laboratory
VL  - 37
IS  - 5
SP  - 943
EP  - 954
DO  - 10.1007/s10529-014-1762-4
ER  - 

@article{
author = "Narančić, Tanja and Davis, Reeta and Nikodinović-Runić, Jasmina and O'Connor, Kevin E.",
year = "2015",
abstract = "Recent developments in biocatalysis, where implementation beyond the laboratory has been demonstrated, are explored: the use of transglutaminases to modify foods, reduce allergenicity and produce advanced materials, lipases for biodiesel production, and transaminases for biochemical production. The availability and application of enzymes at pilot and larger scale opens up possibilities for further improvements of biocatalyst-based processes and the development of new processes. Enzyme production, stability, activity, re-use, and product retrieval are common challenges for biocatalytic processes. We explore recent advances in biocatalysis within the process chain, such as protein engineering, enzyme expression, and biocatalyst immobilization, in the context of these challenges.",
publisher = "Springer, Dordrecht",
journal = "Biotechnology Letters",
title = "Recent developments in biocatalysis beyond the laboratory",
volume = "37",
number = "5",
pages = "943-954",
doi = "10.1007/s10529-014-1762-4"
}

Narančić, T., Davis, R., Nikodinović-Runić, J.,& O'Connor, K. E.. (2015). Recent developments in biocatalysis beyond the laboratory. in Biotechnology Letters
Springer, Dordrecht., 37(5), 943-954.
https://doi.org/10.1007/s10529-014-1762-4

Narančić T, Davis R, Nikodinović-Runić J, O'Connor KE. Recent developments in biocatalysis beyond the laboratory. in Biotechnology Letters. 2015;37(5):943-954.
doi:10.1007/s10529-014-1762-4 .

Narančić, Tanja, Davis, Reeta, Nikodinović-Runić, Jasmina, O'Connor, Kevin E., "Recent developments in biocatalysis beyond the laboratory" in Biotechnology Letters, 37, no. 5 (2015):943-954,
https://doi.org/10.1007/s10529-014-1762-4 . .

TY  - JOUR
AU  - Guzik, Maciej
AU  - Kenny, Shane T.
AU  - Duane, Gearoid F.
AU  - Casey, Eoin
AU  - Woods, Trevor
AU  - Babu, Ramesh P.
AU  - Nikodinović-Runić, Jasmina
AU  - Murray, Michael
AU  - O'Connor, Kevin E.
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1764
AB  - A process for the conversion of post consumer (agricultural) polyethylene (PE) waste to the biodegradable polymer medium chain length polyhydroxyalkanoate (mcl-PHA) is reported here. The thermal treatment of PE in the absence of air (pyrolysis) generated a complex mixture of low molecular weight paraffins with carbon chain lengths from C8 to C32 (PE pyrolysis wax). Several bacterial strains were able to grow and produce PHA from this PE pyrolysis wax. The addition of biosurfactant (rhamnolipids) allowed for greater bacterial growth and PHA accumulation of the tested strains. Some strains were only capable of growth and PHA accumulation in the presence of the biosurfactant. Pseudomonas aeruginosa PAO-1 accumulated the highest level of PHA with almost 25 % of the cell dry weight as PHA when supplied with the PE pyrolysis wax in the presence of rhamnolipids. The change of nitrogen source from ammonium chloride to ammonium nitrate resulted in faster bacterial growth and the earlier onset of PHA accumulation. To our knowledge, this is the first report where PE is used as a starting material for production of a biodegradable polymer.
PB  - Springer, New York
T2  - Applied Microbiology and Biotechnology
T1  - Conversion of post consumer polyethylene to the biodegradable polymer polyhydroxyalkanoate
VL  - 98
IS  - 9
SP  - 4223
EP  - 4232
DO  - 10.1007/s00253-013-5489-2
ER  - 

@article{
author = "Guzik, Maciej and Kenny, Shane T. and Duane, Gearoid F. and Casey, Eoin and Woods, Trevor and Babu, Ramesh P. and Nikodinović-Runić, Jasmina and Murray, Michael and O'Connor, Kevin E.",
year = "2014",
abstract = "A process for the conversion of post consumer (agricultural) polyethylene (PE) waste to the biodegradable polymer medium chain length polyhydroxyalkanoate (mcl-PHA) is reported here. The thermal treatment of PE in the absence of air (pyrolysis) generated a complex mixture of low molecular weight paraffins with carbon chain lengths from C8 to C32 (PE pyrolysis wax). Several bacterial strains were able to grow and produce PHA from this PE pyrolysis wax. The addition of biosurfactant (rhamnolipids) allowed for greater bacterial growth and PHA accumulation of the tested strains. Some strains were only capable of growth and PHA accumulation in the presence of the biosurfactant. Pseudomonas aeruginosa PAO-1 accumulated the highest level of PHA with almost 25 % of the cell dry weight as PHA when supplied with the PE pyrolysis wax in the presence of rhamnolipids. The change of nitrogen source from ammonium chloride to ammonium nitrate resulted in faster bacterial growth and the earlier onset of PHA accumulation. To our knowledge, this is the first report where PE is used as a starting material for production of a biodegradable polymer.",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "Conversion of post consumer polyethylene to the biodegradable polymer polyhydroxyalkanoate",
volume = "98",
number = "9",
pages = "4223-4232",
doi = "10.1007/s00253-013-5489-2"
}

Guzik, M., Kenny, S. T., Duane, G. F., Casey, E., Woods, T., Babu, R. P., Nikodinović-Runić, J., Murray, M.,& O'Connor, K. E.. (2014). Conversion of post consumer polyethylene to the biodegradable polymer polyhydroxyalkanoate. in Applied Microbiology and Biotechnology
Springer, New York., 98(9), 4223-4232.
https://doi.org/10.1007/s00253-013-5489-2

Guzik M, Kenny ST, Duane GF, Casey E, Woods T, Babu RP, Nikodinović-Runić J, Murray M, O'Connor KE. Conversion of post consumer polyethylene to the biodegradable polymer polyhydroxyalkanoate. in Applied Microbiology and Biotechnology. 2014;98(9):4223-4232.
doi:10.1007/s00253-013-5489-2 .

Guzik, Maciej, Kenny, Shane T., Duane, Gearoid F., Casey, Eoin, Woods, Trevor, Babu, Ramesh P., Nikodinović-Runić, Jasmina, Murray, Michael, O'Connor, Kevin E., "Conversion of post consumer polyethylene to the biodegradable polymer polyhydroxyalkanoate" in Applied Microbiology and Biotechnology, 98, no. 9 (2014):4223-4232,
https://doi.org/10.1007/s00253-013-5489-2 . .

TY  - JOUR
AU  - Guzik, Maciej
AU  - Narančić, Tanja
AU  - Ilić-Tomić, Tatjana
AU  - Vojnović, Sandra
AU  - Kenny, Shane T.
AU  - Casey, William T.
AU  - Duane, Gearoid F.
AU  - Casey, Eoin
AU  - Woods, Trevor
AU  - Babu, Ramesh P.
AU  - Nikodinović-Runić, Jasmina
AU  - O'Connor, Kevin E.
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1846
AB  - Diverse and elaborate pathways for nutrient utilization, as well as mechanisms to combat unfavourable nutrient conditions make Pseudomonas putida KT2440 a versatile micro-organism able to occupy a range of ecological niches. The fatty acid degradation pathway of P. putida is complex and correlated with biopolymer medium chain length polyhydroxyalkanoate (mcl-PHA) biosynthesis. Little is known about the second step of fatty acid degradation (beta-oxidation) in this strain. In silico analysis of its genome sequence revealed 21 putative acyl-CoA dehydrogenases (ACADs), four of which were functionally characterized through mutagenesis studies. Four mutants with insertionally inactivated ACADs (PP_1893, PP_2039, PP_2048 and PP_2437) grew and accumulated mcl-PHA on a range of fatty acids as the sole source of carbon and energy. Their ability to grow and accumulate biopolymer was differentially negatively affected on various fatty acids, in comparison to the wild-type strain. Inactive PP_2437 exhibited a pattern of reduced growth and PHA accumulation when fatty acids with lengths of 10 to 14 carbon chains were used as substrates. Recombinant expression and biochemical characterization of the purified protein allowed functional annotation in P. putida KT2440 as an ACAD showing clear preference for dodecanoyl-CoA ester as a substrate and optimum activity at 30 degrees C and pH 6.5-7.
PB  - Soc General Microbiology, Reading
T2  - Microbiology, SGM / Society for General Microbiology
T1  - Identification and characterization of an acyl-CoA dehydrogenase from Pseudomonas putida KT2440 that shows preference towards medium to long chain length fatty acids
VL  - 160
SP  - 1760
EP  - 1771
DO  - 10.1099/mic.0.078758-0
ER  - 

@article{
author = "Guzik, Maciej and Narančić, Tanja and Ilić-Tomić, Tatjana and Vojnović, Sandra and Kenny, Shane T. and Casey, William T. and Duane, Gearoid F. and Casey, Eoin and Woods, Trevor and Babu, Ramesh P. and Nikodinović-Runić, Jasmina and O'Connor, Kevin E.",
year = "2014",
abstract = "Diverse and elaborate pathways for nutrient utilization, as well as mechanisms to combat unfavourable nutrient conditions make Pseudomonas putida KT2440 a versatile micro-organism able to occupy a range of ecological niches. The fatty acid degradation pathway of P. putida is complex and correlated with biopolymer medium chain length polyhydroxyalkanoate (mcl-PHA) biosynthesis. Little is known about the second step of fatty acid degradation (beta-oxidation) in this strain. In silico analysis of its genome sequence revealed 21 putative acyl-CoA dehydrogenases (ACADs), four of which were functionally characterized through mutagenesis studies. Four mutants with insertionally inactivated ACADs (PP_1893, PP_2039, PP_2048 and PP_2437) grew and accumulated mcl-PHA on a range of fatty acids as the sole source of carbon and energy. Their ability to grow and accumulate biopolymer was differentially negatively affected on various fatty acids, in comparison to the wild-type strain. Inactive PP_2437 exhibited a pattern of reduced growth and PHA accumulation when fatty acids with lengths of 10 to 14 carbon chains were used as substrates. Recombinant expression and biochemical characterization of the purified protein allowed functional annotation in P. putida KT2440 as an ACAD showing clear preference for dodecanoyl-CoA ester as a substrate and optimum activity at 30 degrees C and pH 6.5-7.",
publisher = "Soc General Microbiology, Reading",
journal = "Microbiology, SGM / Society for General Microbiology",
title = "Identification and characterization of an acyl-CoA dehydrogenase from Pseudomonas putida KT2440 that shows preference towards medium to long chain length fatty acids",
volume = "160",
pages = "1760-1771",
doi = "10.1099/mic.0.078758-0"
}

Guzik, M., Narančić, T., Ilić-Tomić, T., Vojnović, S., Kenny, S. T., Casey, W. T., Duane, G. F., Casey, E., Woods, T., Babu, R. P., Nikodinović-Runić, J.,& O'Connor, K. E.. (2014). Identification and characterization of an acyl-CoA dehydrogenase from Pseudomonas putida KT2440 that shows preference towards medium to long chain length fatty acids. in Microbiology, SGM / Society for General Microbiology
Soc General Microbiology, Reading., 160, 1760-1771.
https://doi.org/10.1099/mic.0.078758-0

Guzik M, Narančić T, Ilić-Tomić T, Vojnović S, Kenny ST, Casey WT, Duane GF, Casey E, Woods T, Babu RP, Nikodinović-Runić J, O'Connor KE. Identification and characterization of an acyl-CoA dehydrogenase from Pseudomonas putida KT2440 that shows preference towards medium to long chain length fatty acids. in Microbiology, SGM / Society for General Microbiology. 2014;160:1760-1771.
doi:10.1099/mic.0.078758-0 .

Guzik, Maciej, Narančić, Tanja, Ilić-Tomić, Tatjana, Vojnović, Sandra, Kenny, Shane T., Casey, William T., Duane, Gearoid F., Casey, Eoin, Woods, Trevor, Babu, Ramesh P., Nikodinović-Runić, Jasmina, O'Connor, Kevin E., "Identification and characterization of an acyl-CoA dehydrogenase from Pseudomonas putida KT2440 that shows preference towards medium to long chain length fatty acids" in Microbiology, SGM / Society for General Microbiology, 160 (2014):1760-1771,
https://doi.org/10.1099/mic.0.078758-0 . .

TY  - JOUR
AU  - Radivojević, Jelena
AU  - Minovska, Gordana
AU  - Šenerović, Lidija
AU  - O'Connor, Kevin E.
AU  - Jovanović, Predrag M.
AU  - Savić, Vladimir
AU  - Tokić-Vujošević, Zorana
AU  - Nikodinović-Runić, Jasmina
AU  - Maslak, Veselin
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1883
AB  - Synthesis of gamma-nitroaldehydes from branched chain aldehydes and a range of alpha,beta-unsaturated nitroalkenes was achieved by a whole-cell biocatalytic reaction using 4-oxalocrotonate tautomerase as catalyst. Under mild conditions, cyclic and acyclic branched aldehydes were converted into synthetically valuable quaternary carbon containing gamma-nitroaldehydes. The yields of the desired products were influenced by reaction condition parameters such as organic solvent, temperature and pH. The whole-cell biocatalytic approach to the generation of alpha,alpha-substituted gamma-nitroaldehydes was compared to the organocatalytic approach involving the lithium salt of phenylalanine as a catalyst. As the resulting gamma-nitroaldehydes exhibited moderate antifungal activity and mild in vitro cytotoxicity against human fibroblasts (0.2-0.4 mM) they could further be examined as potentially useful pharmaceutical synthons.
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - Synthesis of gamma-nitroaldehydes containing quaternary carbon in the alpha-position using a 4-oxalocrotonate tautomerase whole-cell biocatalyst
VL  - 4
IS  - 105
SP  - 60502
EP  - 60510
DO  - 10.1039/c4ra05517a
ER  - 

@article{
author = "Radivojević, Jelena and Minovska, Gordana and Šenerović, Lidija and O'Connor, Kevin E. and Jovanović, Predrag M. and Savić, Vladimir and Tokić-Vujošević, Zorana and Nikodinović-Runić, Jasmina and Maslak, Veselin",
year = "2014",
abstract = "Synthesis of gamma-nitroaldehydes from branched chain aldehydes and a range of alpha,beta-unsaturated nitroalkenes was achieved by a whole-cell biocatalytic reaction using 4-oxalocrotonate tautomerase as catalyst. Under mild conditions, cyclic and acyclic branched aldehydes were converted into synthetically valuable quaternary carbon containing gamma-nitroaldehydes. The yields of the desired products were influenced by reaction condition parameters such as organic solvent, temperature and pH. The whole-cell biocatalytic approach to the generation of alpha,alpha-substituted gamma-nitroaldehydes was compared to the organocatalytic approach involving the lithium salt of phenylalanine as a catalyst. As the resulting gamma-nitroaldehydes exhibited moderate antifungal activity and mild in vitro cytotoxicity against human fibroblasts (0.2-0.4 mM) they could further be examined as potentially useful pharmaceutical synthons.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "Synthesis of gamma-nitroaldehydes containing quaternary carbon in the alpha-position using a 4-oxalocrotonate tautomerase whole-cell biocatalyst",
volume = "4",
number = "105",
pages = "60502-60510",
doi = "10.1039/c4ra05517a"
}

Radivojević, J., Minovska, G., Šenerović, L., O'Connor, K. E., Jovanović, P. M., Savić, V., Tokić-Vujošević, Z., Nikodinović-Runić, J.,& Maslak, V.. (2014). Synthesis of gamma-nitroaldehydes containing quaternary carbon in the alpha-position using a 4-oxalocrotonate tautomerase whole-cell biocatalyst. in RSC Advances
Royal Soc Chemistry, Cambridge., 4(105), 60502-60510.
https://doi.org/10.1039/c4ra05517a

Radivojević J, Minovska G, Šenerović L, O'Connor KE, Jovanović PM, Savić V, Tokić-Vujošević Z, Nikodinović-Runić J, Maslak V. Synthesis of gamma-nitroaldehydes containing quaternary carbon in the alpha-position using a 4-oxalocrotonate tautomerase whole-cell biocatalyst. in RSC Advances. 2014;4(105):60502-60510.
doi:10.1039/c4ra05517a .

Radivojević, Jelena, Minovska, Gordana, Šenerović, Lidija, O'Connor, Kevin E., Jovanović, Predrag M., Savić, Vladimir, Tokić-Vujošević, Zorana, Nikodinović-Runić, Jasmina, Maslak, Veselin, "Synthesis of gamma-nitroaldehydes containing quaternary carbon in the alpha-position using a 4-oxalocrotonate tautomerase whole-cell biocatalyst" in RSC Advances, 4, no. 105 (2014):60502-60510,
https://doi.org/10.1039/c4ra05517a . .

TY  - DATA
AU  - Narančić, Tanja
AU  - Kadivojević, Jelena
AU  - Jovanović, Predrag M.
AU  - Francuski, Đorđe
AU  - Bigović, Miljan
AU  - Maslak, Veselin
AU  - Savić, Vladimir
AU  - Vasiljević, Branka
AU  - O'Connor, Kevin E.
AU  - Nikodinović-Runić, Jasmina
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3499
PB  - Elsevier Sci Ltd, Oxford
T2  - Bioresource Technology
T1  - Supplementary data for article: Narančić, T.; Kadivojevic, J.; Jovanovic, P.; Francuski, D.; Bigović, M.; Maslak, V.; Savić, V.; Vasiljević, B.; O’Connor, K. E.; Nikodinović-Runić, J. Highly Efficient Michael-Type Addition of Acetaldehyde to Beta-Nitrostyrenes by Whole Resting Cells of Escherichia Coli Expressing 4-Oxalocrotonate Tautomerase. Bioresource Technology 2013, 142, 462–468. https://doi.org/10.1016/j.biortech.2013.05.074
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3499
ER  - 

@misc{
author = "Narančić, Tanja and Kadivojević, Jelena and Jovanović, Predrag M. and Francuski, Đorđe and Bigović, Miljan and Maslak, Veselin and Savić, Vladimir and Vasiljević, Branka and O'Connor, Kevin E. and Nikodinović-Runić, Jasmina",
year = "2013",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Bioresource Technology",
title = "Supplementary data for article: Narančić, T.; Kadivojevic, J.; Jovanovic, P.; Francuski, D.; Bigović, M.; Maslak, V.; Savić, V.; Vasiljević, B.; O’Connor, K. E.; Nikodinović-Runić, J. Highly Efficient Michael-Type Addition of Acetaldehyde to Beta-Nitrostyrenes by Whole Resting Cells of Escherichia Coli Expressing 4-Oxalocrotonate Tautomerase. Bioresource Technology 2013, 142, 462–468. https://doi.org/10.1016/j.biortech.2013.05.074",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3499"
}

Narančić, T., Kadivojević, J., Jovanović, P. M., Francuski, Đ., Bigović, M., Maslak, V., Savić, V., Vasiljević, B., O'Connor, K. E.,& Nikodinović-Runić, J.. (2013). Supplementary data for article: Narančić, T.; Kadivojevic, J.; Jovanovic, P.; Francuski, D.; Bigović, M.; Maslak, V.; Savić, V.; Vasiljević, B.; O’Connor, K. E.; Nikodinović-Runić, J. Highly Efficient Michael-Type Addition of Acetaldehyde to Beta-Nitrostyrenes by Whole Resting Cells of Escherichia Coli Expressing 4-Oxalocrotonate Tautomerase. Bioresource Technology 2013, 142, 462–468. https://doi.org/10.1016/j.biortech.2013.05.074. in Bioresource Technology
Elsevier Sci Ltd, Oxford..
https://hdl.handle.net/21.15107/rcub_cherry_3499

Narančić T, Kadivojević J, Jovanović PM, Francuski Đ, Bigović M, Maslak V, Savić V, Vasiljević B, O'Connor KE, Nikodinović-Runić J. Supplementary data for article: Narančić, T.; Kadivojevic, J.; Jovanovic, P.; Francuski, D.; Bigović, M.; Maslak, V.; Savić, V.; Vasiljević, B.; O’Connor, K. E.; Nikodinović-Runić, J. Highly Efficient Michael-Type Addition of Acetaldehyde to Beta-Nitrostyrenes by Whole Resting Cells of Escherichia Coli Expressing 4-Oxalocrotonate Tautomerase. Bioresource Technology 2013, 142, 462–468. https://doi.org/10.1016/j.biortech.2013.05.074. in Bioresource Technology. 2013;.
https://hdl.handle.net/21.15107/rcub_cherry_3499 .

Narančić, Tanja, Kadivojević, Jelena, Jovanović, Predrag M., Francuski, Đorđe, Bigović, Miljan, Maslak, Veselin, Savić, Vladimir, Vasiljević, Branka, O'Connor, Kevin E., Nikodinović-Runić, Jasmina, "Supplementary data for article: Narančić, T.; Kadivojevic, J.; Jovanovic, P.; Francuski, D.; Bigović, M.; Maslak, V.; Savić, V.; Vasiljević, B.; O’Connor, K. E.; Nikodinović-Runić, J. Highly Efficient Michael-Type Addition of Acetaldehyde to Beta-Nitrostyrenes by Whole Resting Cells of Escherichia Coli Expressing 4-Oxalocrotonate Tautomerase. Bioresource Technology 2013, 142, 462–468. https://doi.org/10.1016/j.biortech.2013.05.074" in Bioresource Technology (2013),
https://hdl.handle.net/21.15107/rcub_cherry_3499 .

TY  - JOUR
AU  - O'Connor, Stephen
AU  - Szwej, Emilia
AU  - Nikodinović-Runić, Jasmina
AU  - O'Connor, Aisling
AU  - Byrne, Annette T.
AU  - Devocelle, Marc
AU  - O'Donovan, Norma
AU  - Gallagher, William M.
AU  - Babu, Ramesh P.
AU  - Kenny, Shane T.
AU  - Zinn, Manfred
AU  - Zulian, Qun Ren
AU  - O'Connor, Kevin E.
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1609
AB  - The biodegradable polymer medium chain length polyhydroxyalkanoate (mclPHA), produced by Pseudomonas putida CA-3, was depolymerised and the predominant monomer (R)-3-hydroxydecanoic acid (R10) purified. R10 was conjugated to a D-peptide DP18 and its derivatives. All peptides conjugated with R10 exhibited greater anti-cancer activity compared to the unconjugated peptides. Unconjugated and conjugated peptides were cytocidal for cancer cells. Conjugation of R10 to peptides was essential for enhanced anti-proliferation activity, as unconjugated mixes did not result in enhancement of anti-cancer activity. The conjugation of R10 resulted in more rapid uptake of peptides into HeLa and MiaPaCa cells compared to unconjugated peptide. Both unconjugated and R10 conjugated peptides localized to the mitochondria of HeLa and MiaPaCa cells and induced apoptosis. Peptide conjugated with a terminally hydroxylated decanoic acid (omega-hydroxydecanoic acid) exhibited 3.3 and 6.3 fold higher IC50 values compared to R10 conjugated peptide indicating a role for the position of the hydroxyl moiety in enhancement of anti-cancer activity. Conjugation of decanoic acid (C10) to peptides resulted in similar or higher IC50 values compared to R10 conjugates but C10 conjugates did not exhibit any cancer selectivity. Combination studies showed that R10DP18L exhibited synergy with cisplatin, gemcitabine, and taxotere with IC50 values in the nanomolar range.
PB  - Elsevier Sci Ltd, Oxford
T2  - Biomaterials
T1  - The anti-cancer activity of a cationic anti-microbial peptide derived from monomers of polyhydroxyalkanoate
VL  - 34
IS  - 11
SP  - 2710
EP  - 2718
DO  - 10.1016/j.biomaterials.2012.12.032
ER  - 

@article{
author = "O'Connor, Stephen and Szwej, Emilia and Nikodinović-Runić, Jasmina and O'Connor, Aisling and Byrne, Annette T. and Devocelle, Marc and O'Donovan, Norma and Gallagher, William M. and Babu, Ramesh P. and Kenny, Shane T. and Zinn, Manfred and Zulian, Qun Ren and O'Connor, Kevin E.",
year = "2013",
abstract = "The biodegradable polymer medium chain length polyhydroxyalkanoate (mclPHA), produced by Pseudomonas putida CA-3, was depolymerised and the predominant monomer (R)-3-hydroxydecanoic acid (R10) purified. R10 was conjugated to a D-peptide DP18 and its derivatives. All peptides conjugated with R10 exhibited greater anti-cancer activity compared to the unconjugated peptides. Unconjugated and conjugated peptides were cytocidal for cancer cells. Conjugation of R10 to peptides was essential for enhanced anti-proliferation activity, as unconjugated mixes did not result in enhancement of anti-cancer activity. The conjugation of R10 resulted in more rapid uptake of peptides into HeLa and MiaPaCa cells compared to unconjugated peptide. Both unconjugated and R10 conjugated peptides localized to the mitochondria of HeLa and MiaPaCa cells and induced apoptosis. Peptide conjugated with a terminally hydroxylated decanoic acid (omega-hydroxydecanoic acid) exhibited 3.3 and 6.3 fold higher IC50 values compared to R10 conjugated peptide indicating a role for the position of the hydroxyl moiety in enhancement of anti-cancer activity. Conjugation of decanoic acid (C10) to peptides resulted in similar or higher IC50 values compared to R10 conjugates but C10 conjugates did not exhibit any cancer selectivity. Combination studies showed that R10DP18L exhibited synergy with cisplatin, gemcitabine, and taxotere with IC50 values in the nanomolar range.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Biomaterials",
title = "The anti-cancer activity of a cationic anti-microbial peptide derived from monomers of polyhydroxyalkanoate",
volume = "34",
number = "11",
pages = "2710-2718",
doi = "10.1016/j.biomaterials.2012.12.032"
}

O'Connor, S., Szwej, E., Nikodinović-Runić, J., O'Connor, A., Byrne, A. T., Devocelle, M., O'Donovan, N., Gallagher, W. M., Babu, R. P., Kenny, S. T., Zinn, M., Zulian, Q. R.,& O'Connor, K. E.. (2013). The anti-cancer activity of a cationic anti-microbial peptide derived from monomers of polyhydroxyalkanoate. in Biomaterials
Elsevier Sci Ltd, Oxford., 34(11), 2710-2718.
https://doi.org/10.1016/j.biomaterials.2012.12.032

O'Connor S, Szwej E, Nikodinović-Runić J, O'Connor A, Byrne AT, Devocelle M, O'Donovan N, Gallagher WM, Babu RP, Kenny ST, Zinn M, Zulian QR, O'Connor KE. The anti-cancer activity of a cationic anti-microbial peptide derived from monomers of polyhydroxyalkanoate. in Biomaterials. 2013;34(11):2710-2718.
doi:10.1016/j.biomaterials.2012.12.032 .

O'Connor, Stephen, Szwej, Emilia, Nikodinović-Runić, Jasmina, O'Connor, Aisling, Byrne, Annette T., Devocelle, Marc, O'Donovan, Norma, Gallagher, William M., Babu, Ramesh P., Kenny, Shane T., Zinn, Manfred, Zulian, Qun Ren, O'Connor, Kevin E., "The anti-cancer activity of a cationic anti-microbial peptide derived from monomers of polyhydroxyalkanoate" in Biomaterials, 34, no. 11 (2013):2710-2718,
https://doi.org/10.1016/j.biomaterials.2012.12.032 . .

TY  - DATA
AU  - O'Connor, Stephen
AU  - Szwej, Emilia
AU  - Nikodinović-Runić, Jasmina
AU  - O'Connor, Aisling
AU  - Byrne, Annette T.
AU  - Devocelle, Marc
AU  - O'Donovan, Norma
AU  - Gallagher, William M.
AU  - Babu, Ramesh P.
AU  - Kenny, Shane T.
AU  - Zinn, Manfred
AU  - Zulian, Qun Ren
AU  - O'Connor, Kevin E.
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3550
PB  - Elsevier Sci Ltd, Oxford
T2  - Biomaterials
T1  - Supplementary data for article: O’Connor, S.; Szwej, E.; Nikodinović-Runić, J.; O’Connor, A.; Byrne, A. T.; Devocelle, M.; O’Donovan, N.; Gallagher, W. M.; Babu, R. P.; Kenny, S. T.; et al. The Anti-Cancer Activity of a Cationic Anti-Microbial Peptide Derived from Monomers of Polyhydroxyalkanoate. Biomaterials 2013, 34 (11), 2710–2718. https://doi.org/10.1016/j.biomaterials.2012.12.032
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3550
ER  - 

@misc{
author = "O'Connor, Stephen and Szwej, Emilia and Nikodinović-Runić, Jasmina and O'Connor, Aisling and Byrne, Annette T. and Devocelle, Marc and O'Donovan, Norma and Gallagher, William M. and Babu, Ramesh P. and Kenny, Shane T. and Zinn, Manfred and Zulian, Qun Ren and O'Connor, Kevin E.",
year = "2013",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Biomaterials",
title = "Supplementary data for article: O’Connor, S.; Szwej, E.; Nikodinović-Runić, J.; O’Connor, A.; Byrne, A. T.; Devocelle, M.; O’Donovan, N.; Gallagher, W. M.; Babu, R. P.; Kenny, S. T.; et al. The Anti-Cancer Activity of a Cationic Anti-Microbial Peptide Derived from Monomers of Polyhydroxyalkanoate. Biomaterials 2013, 34 (11), 2710–2718. https://doi.org/10.1016/j.biomaterials.2012.12.032",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3550"
}

O'Connor, S., Szwej, E., Nikodinović-Runić, J., O'Connor, A., Byrne, A. T., Devocelle, M., O'Donovan, N., Gallagher, W. M., Babu, R. P., Kenny, S. T., Zinn, M., Zulian, Q. R.,& O'Connor, K. E.. (2013). Supplementary data for article: O’Connor, S.; Szwej, E.; Nikodinović-Runić, J.; O’Connor, A.; Byrne, A. T.; Devocelle, M.; O’Donovan, N.; Gallagher, W. M.; Babu, R. P.; Kenny, S. T.; et al. The Anti-Cancer Activity of a Cationic Anti-Microbial Peptide Derived from Monomers of Polyhydroxyalkanoate. Biomaterials 2013, 34 (11), 2710–2718. https://doi.org/10.1016/j.biomaterials.2012.12.032. in Biomaterials
Elsevier Sci Ltd, Oxford..
https://hdl.handle.net/21.15107/rcub_cherry_3550

O'Connor S, Szwej E, Nikodinović-Runić J, O'Connor A, Byrne AT, Devocelle M, O'Donovan N, Gallagher WM, Babu RP, Kenny ST, Zinn M, Zulian QR, O'Connor KE. Supplementary data for article: O’Connor, S.; Szwej, E.; Nikodinović-Runić, J.; O’Connor, A.; Byrne, A. T.; Devocelle, M.; O’Donovan, N.; Gallagher, W. M.; Babu, R. P.; Kenny, S. T.; et al. The Anti-Cancer Activity of a Cationic Anti-Microbial Peptide Derived from Monomers of Polyhydroxyalkanoate. Biomaterials 2013, 34 (11), 2710–2718. https://doi.org/10.1016/j.biomaterials.2012.12.032. in Biomaterials. 2013;.
https://hdl.handle.net/21.15107/rcub_cherry_3550 .

O'Connor, Stephen, Szwej, Emilia, Nikodinović-Runić, Jasmina, O'Connor, Aisling, Byrne, Annette T., Devocelle, Marc, O'Donovan, Norma, Gallagher, William M., Babu, Ramesh P., Kenny, Shane T., Zinn, Manfred, Zulian, Qun Ren, O'Connor, Kevin E., "Supplementary data for article: O’Connor, S.; Szwej, E.; Nikodinović-Runić, J.; O’Connor, A.; Byrne, A. T.; Devocelle, M.; O’Donovan, N.; Gallagher, W. M.; Babu, R. P.; Kenny, S. T.; et al. The Anti-Cancer Activity of a Cationic Anti-Microbial Peptide Derived from Monomers of Polyhydroxyalkanoate. Biomaterials 2013, 34 (11), 2710–2718. https://doi.org/10.1016/j.biomaterials.2012.12.032" in Biomaterials (2013),
https://hdl.handle.net/21.15107/rcub_cherry_3550 .

TY  - JOUR
AU  - Narančić, Tanja
AU  - Kadivojević, Jelena
AU  - Jovanović, Predrag M.
AU  - Francuski, Đorđe
AU  - Bigović, Miljan
AU  - Maslak, Veselin
AU  - Savić, Vladimir
AU  - Vasiljević, Branka
AU  - O'Connor, Kevin E.
AU  - Nikodinović-Runić, Jasmina
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1377
AB  - A novel whole cell system based on recombinantly expressed 4-oxalocrotonate tautomerase (4-OT) was developed and shown to be an effective biocatalyst for the asymmetric Michael addition of acetaldehyde to beta-nitrostyrenes. Optimal ratio of substrates (2 mM beta-nitrostyrenes and 20 mM acetaldehyde) and biocatalyst of 5 g of cell dry weight of biocatalyst per liter was determined. Through further bioprocess improvement by sequential addition of substrate 10 mM nitrostyrene biotransformation was achieved within 150 min. Excellent enantioselectivity ( gt 99% ee) and product yields of up to 60% were obtained with beta-nitrostyrene substrate. The biotransformation product, 4-nitro-3-phenyl-butanal, was isolated from aqueous media and further transformed into the corresponding amino alcohol. The biocatalyst exhibited lower reaction rates with p-Cl-, o-Cl- and p-F-beta-nitrostyrenes with product yields of 38%, 51%, 31% and ee values of 84%, 88% and 94% respectively. The importance of the terminal,proline of 4-UT was confirmed by two proline enriched variants and homology modeling.
PB  - Elsevier Sci Ltd, Oxford
T2  - Bioresource Technology
T1  - Highly efficient Michael-type addition of acetaldehyde to beta-nitrostyrenes by whole resting cells of Escherichia coli expressing 4-oxalocrotonate tautomerase
VL  - 142
SP  - 462
EP  - 468
DO  - 10.1016/j.biortech.2013.05.074
ER  - 

@article{
author = "Narančić, Tanja and Kadivojević, Jelena and Jovanović, Predrag M. and Francuski, Đorđe and Bigović, Miljan and Maslak, Veselin and Savić, Vladimir and Vasiljević, Branka and O'Connor, Kevin E. and Nikodinović-Runić, Jasmina",
year = "2013",
abstract = "A novel whole cell system based on recombinantly expressed 4-oxalocrotonate tautomerase (4-OT) was developed and shown to be an effective biocatalyst for the asymmetric Michael addition of acetaldehyde to beta-nitrostyrenes. Optimal ratio of substrates (2 mM beta-nitrostyrenes and 20 mM acetaldehyde) and biocatalyst of 5 g of cell dry weight of biocatalyst per liter was determined. Through further bioprocess improvement by sequential addition of substrate 10 mM nitrostyrene biotransformation was achieved within 150 min. Excellent enantioselectivity ( gt 99% ee) and product yields of up to 60% were obtained with beta-nitrostyrene substrate. The biotransformation product, 4-nitro-3-phenyl-butanal, was isolated from aqueous media and further transformed into the corresponding amino alcohol. The biocatalyst exhibited lower reaction rates with p-Cl-, o-Cl- and p-F-beta-nitrostyrenes with product yields of 38%, 51%, 31% and ee values of 84%, 88% and 94% respectively. The importance of the terminal,proline of 4-UT was confirmed by two proline enriched variants and homology modeling.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Bioresource Technology",
title = "Highly efficient Michael-type addition of acetaldehyde to beta-nitrostyrenes by whole resting cells of Escherichia coli expressing 4-oxalocrotonate tautomerase",
volume = "142",
pages = "462-468",
doi = "10.1016/j.biortech.2013.05.074"
}

Narančić, T., Kadivojević, J., Jovanović, P. M., Francuski, Đ., Bigović, M., Maslak, V., Savić, V., Vasiljević, B., O'Connor, K. E.,& Nikodinović-Runić, J.. (2013). Highly efficient Michael-type addition of acetaldehyde to beta-nitrostyrenes by whole resting cells of Escherichia coli expressing 4-oxalocrotonate tautomerase. in Bioresource Technology
Elsevier Sci Ltd, Oxford., 142, 462-468.
https://doi.org/10.1016/j.biortech.2013.05.074

Narančić T, Kadivojević J, Jovanović PM, Francuski Đ, Bigović M, Maslak V, Savić V, Vasiljević B, O'Connor KE, Nikodinović-Runić J. Highly efficient Michael-type addition of acetaldehyde to beta-nitrostyrenes by whole resting cells of Escherichia coli expressing 4-oxalocrotonate tautomerase. in Bioresource Technology. 2013;142:462-468.
doi:10.1016/j.biortech.2013.05.074 .

Narančić, Tanja, Kadivojević, Jelena, Jovanović, Predrag M., Francuski, Đorđe, Bigović, Miljan, Maslak, Veselin, Savić, Vladimir, Vasiljević, Branka, O'Connor, Kevin E., Nikodinović-Runić, Jasmina, "Highly efficient Michael-type addition of acetaldehyde to beta-nitrostyrenes by whole resting cells of Escherichia coli expressing 4-oxalocrotonate tautomerase" in Bioresource Technology, 142 (2013):462-468,
https://doi.org/10.1016/j.biortech.2013.05.074 . .

TY  - JOUR
AU  - Molloy, Susan
AU  - Nikodinović-Runić, Jasmina
AU  - Martin, Leona B.
AU  - Hartmann, Hermann
AU  - Solano, Francisco
AU  - Decker, Heinz
AU  - O'Connor, Kevin E.
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3491
AB  - The tyrosinase gene from Ralstonia solanacearum (GenBank NP518458) was subjected to random mutagenesis resulting in tyrosinase variants (RVC10 and RV145) with up to 3.2-fold improvement in kcat, 5.2-fold lower Km and 16-fold improvement in catalytic efficiency for D-tyrosine. Based on RVC10 and RV145 mutated sequences, single mutation variants were generated with all variants showing increased kcat for D-tyrosine compared to the wild type (WT). All single mutation variants based on RV145 had a higher kcat and Km value compared to the RV145 and thus the combination of four mutations in RV145 was antagonistic for turnover, but synergistic for affinity of the enzyme for D-tyrosine. Single mutation variant 145_V153A exhibited the highest (6.9-fold) improvement in kcat and a 2.4-fold increase in Km compared to the WT. Two single mutation variants, C10_N322S and C10_T183I reduced the Km up to 2.6-fold for D-tyrosine but one variant 145_V153A increased the Km 2.4-fold compared to the WT. Homology based modeling of R. solanacearum tyrosinase showed that mutation V153A disrupts the van der Waals interactions with an -helix providing one of the conserved histidine residues of the active site. The kcat and Km values for L-tyrosine decreased for RV145 and RVC10 compared to the WT. RV145 exhibited a 2.1-fold high catalytic efficiency compared to the WT which is a 7.6-fold lower improvement compared to D-tyrosine. RV145 exhibited a threefold higher monophenolase:diphenolase activity ratio for D-tyrosine:D-DOPA and a 1.4-fold higher L-tyrosine:L-DOPA activity ratio compared to the WT. Biotechnol. Bioeng. 2013; 110: 1849-1857.
PB  - Wiley-Blackwell, Hoboken
T2  - Biotechnology and Bioengineering
T1  - Engineering of a bacterial tyrosinase for improved catalytic efficiency towards D-tyrosine using random and site directed mutagenesis approaches
VL  - 110
IS  - 7
SP  - 1849
EP  - 1857
DO  - 10.1002/bit.24859
ER  - 

@article{
author = "Molloy, Susan and Nikodinović-Runić, Jasmina and Martin, Leona B. and Hartmann, Hermann and Solano, Francisco and Decker, Heinz and O'Connor, Kevin E.",
year = "2013",
abstract = "The tyrosinase gene from Ralstonia solanacearum (GenBank NP518458) was subjected to random mutagenesis resulting in tyrosinase variants (RVC10 and RV145) with up to 3.2-fold improvement in kcat, 5.2-fold lower Km and 16-fold improvement in catalytic efficiency for D-tyrosine. Based on RVC10 and RV145 mutated sequences, single mutation variants were generated with all variants showing increased kcat for D-tyrosine compared to the wild type (WT). All single mutation variants based on RV145 had a higher kcat and Km value compared to the RV145 and thus the combination of four mutations in RV145 was antagonistic for turnover, but synergistic for affinity of the enzyme for D-tyrosine. Single mutation variant 145_V153A exhibited the highest (6.9-fold) improvement in kcat and a 2.4-fold increase in Km compared to the WT. Two single mutation variants, C10_N322S and C10_T183I reduced the Km up to 2.6-fold for D-tyrosine but one variant 145_V153A increased the Km 2.4-fold compared to the WT. Homology based modeling of R. solanacearum tyrosinase showed that mutation V153A disrupts the van der Waals interactions with an -helix providing one of the conserved histidine residues of the active site. The kcat and Km values for L-tyrosine decreased for RV145 and RVC10 compared to the WT. RV145 exhibited a 2.1-fold high catalytic efficiency compared to the WT which is a 7.6-fold lower improvement compared to D-tyrosine. RV145 exhibited a threefold higher monophenolase:diphenolase activity ratio for D-tyrosine:D-DOPA and a 1.4-fold higher L-tyrosine:L-DOPA activity ratio compared to the WT. Biotechnol. Bioeng. 2013; 110: 1849-1857.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Biotechnology and Bioengineering",
title = "Engineering of a bacterial tyrosinase for improved catalytic efficiency towards D-tyrosine using random and site directed mutagenesis approaches",
volume = "110",
number = "7",
pages = "1849-1857",
doi = "10.1002/bit.24859"
}

Molloy, S., Nikodinović-Runić, J., Martin, L. B., Hartmann, H., Solano, F., Decker, H.,& O'Connor, K. E.. (2013). Engineering of a bacterial tyrosinase for improved catalytic efficiency towards D-tyrosine using random and site directed mutagenesis approaches. in Biotechnology and Bioengineering
Wiley-Blackwell, Hoboken., 110(7), 1849-1857.
https://doi.org/10.1002/bit.24859

Molloy S, Nikodinović-Runić J, Martin LB, Hartmann H, Solano F, Decker H, O'Connor KE. Engineering of a bacterial tyrosinase for improved catalytic efficiency towards D-tyrosine using random and site directed mutagenesis approaches. in Biotechnology and Bioengineering. 2013;110(7):1849-1857.
doi:10.1002/bit.24859 .

Molloy, Susan, Nikodinović-Runić, Jasmina, Martin, Leona B., Hartmann, Hermann, Solano, Francisco, Decker, Heinz, O'Connor, Kevin E., "Engineering of a bacterial tyrosinase for improved catalytic efficiency towards D-tyrosine using random and site directed mutagenesis approaches" in Biotechnology and Bioengineering, 110, no. 7 (2013):1849-1857,
https://doi.org/10.1002/bit.24859 . .

TY  - DATA
AU  - Molloy, Susan
AU  - Nikodinović-Runić, Jasmina
AU  - Martin, Leona B.
AU  - Hartmann, Hermann
AU  - Solano, Francisco
AU  - Decker, Heinz
AU  - O'Connor, Kevin E.
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3492
PB  - Wiley-Blackwell, Hoboken
T2  - Biotechnology and Bioengineering
T1  - Supplementary data for article: Molloy, S.; Nikodinović-Runić, J.; Martin, L. B.; Hartmann, H.; Solano, F.; Decker, H.; O’Connor, K. E. Engineering of a Bacterial Tyrosinase for Improved Catalytic Efficiency towards D-Tyrosine Using Random and Site Directed Mutagenesis Approaches. Biotechnology and Bioengineering 2013, 110 (7), 1849–1857. https://doi.org/10.1002/bit.24859
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3492
ER  - 

@misc{
author = "Molloy, Susan and Nikodinović-Runić, Jasmina and Martin, Leona B. and Hartmann, Hermann and Solano, Francisco and Decker, Heinz and O'Connor, Kevin E.",
year = "2013",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Biotechnology and Bioengineering",
title = "Supplementary data for article: Molloy, S.; Nikodinović-Runić, J.; Martin, L. B.; Hartmann, H.; Solano, F.; Decker, H.; O’Connor, K. E. Engineering of a Bacterial Tyrosinase for Improved Catalytic Efficiency towards D-Tyrosine Using Random and Site Directed Mutagenesis Approaches. Biotechnology and Bioengineering 2013, 110 (7), 1849–1857. https://doi.org/10.1002/bit.24859",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3492"
}

Molloy, S., Nikodinović-Runić, J., Martin, L. B., Hartmann, H., Solano, F., Decker, H.,& O'Connor, K. E.. (2013). Supplementary data for article: Molloy, S.; Nikodinović-Runić, J.; Martin, L. B.; Hartmann, H.; Solano, F.; Decker, H.; O’Connor, K. E. Engineering of a Bacterial Tyrosinase for Improved Catalytic Efficiency towards D-Tyrosine Using Random and Site Directed Mutagenesis Approaches. Biotechnology and Bioengineering 2013, 110 (7), 1849–1857. https://doi.org/10.1002/bit.24859. in Biotechnology and Bioengineering
Wiley-Blackwell, Hoboken..
https://hdl.handle.net/21.15107/rcub_cherry_3492

Molloy S, Nikodinović-Runić J, Martin LB, Hartmann H, Solano F, Decker H, O'Connor KE. Supplementary data for article: Molloy, S.; Nikodinović-Runić, J.; Martin, L. B.; Hartmann, H.; Solano, F.; Decker, H.; O’Connor, K. E. Engineering of a Bacterial Tyrosinase for Improved Catalytic Efficiency towards D-Tyrosine Using Random and Site Directed Mutagenesis Approaches. Biotechnology and Bioengineering 2013, 110 (7), 1849–1857. https://doi.org/10.1002/bit.24859. in Biotechnology and Bioengineering. 2013;.
https://hdl.handle.net/21.15107/rcub_cherry_3492 .

Molloy, Susan, Nikodinović-Runić, Jasmina, Martin, Leona B., Hartmann, Hermann, Solano, Francisco, Decker, Heinz, O'Connor, Kevin E., "Supplementary data for article: Molloy, S.; Nikodinović-Runić, J.; Martin, L. B.; Hartmann, H.; Solano, F.; Decker, H.; O’Connor, K. E. Engineering of a Bacterial Tyrosinase for Improved Catalytic Efficiency towards D-Tyrosine Using Random and Site Directed Mutagenesis Approaches. Biotechnology and Bioengineering 2013, 110 (7), 1849–1857. https://doi.org/10.1002/bit.24859" in Biotechnology and Bioengineering (2013),
https://hdl.handle.net/21.15107/rcub_cherry_3492 .

TY  - JOUR
AU  - Casey, William T.
AU  - Nikodinović-Runić, Jasmina
AU  - Fonseca Garcia, Pilar
AU  - Guzik, Maciej
AU  - McGrath, John W.
AU  - Quinn, John P.
AU  - Cagney, Gerard
AU  - Auxiliadora Prieto, Maria
AU  - O'Connor, Kevin E.
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3553
AB  - The primary enzyme involved in polyphosphate (polyP) synthesis, polyP kinase (ppk), has been deleted in Pseudomonas putidaKT2440. This has resulted in a threefold to sixfold reduction in polyhydroxyalkanoate (PHA) accumulation compared with the wild type under conditions of nitrogen limitation, with either temperature or oxidative (H2O2) stress, when grown on glucose. The accumulation of PHA by ppk mutant was the same as the wild type under nitrogen-limiting growth conditions. There was no difference in polyP levels between wild-type and ppk strains under all growth conditions tested. In the ppk mutant proteome, polyP kinase (PPK) was undetectable, but up-regulation of the polyp-associated proteins polyP adenosine triphosphate (ATP)/nicotinamide adenine dinucleotide (NAD) kinase (PpnK), a putative polyP adenosine monophosphate (AMP) phosphotransferase (PP_1752), and exopolyphosphatase was observed. ppk strain exhibited significantly retarded growth with glycerol as carbon and energy source (42h of lag period compared with 24h in wild-type strain) but similar growth to the wild-type strain with glucose. Analysis of gene transcription revealed downregulation of glycerol kinase and the glycerol facilitator respectively. Glycerol kinase protein expression was also downregulated in the ppk mutant. The deletion of ppk did not affect motility but reduced biofilm formation. Thus, the knockout of the ppk gene has resulted in a number of phenotypic changes to the mutant without affecting polyP accumulation.
PB  - Wiley-Blackwell, Hoboken
T2  - Environmental Microbiology Reports
T1  - The effect of polyphosphate kinase gene deletion on polyhydroxyalkanoate accumulation and carbon metabolism in Pseudomonas putida KT2440
VL  - 5
IS  - 5
SP  - 740
EP  - 746
DO  - 10.1111/1758-2229.12076
ER  - 

@article{
author = "Casey, William T. and Nikodinović-Runić, Jasmina and Fonseca Garcia, Pilar and Guzik, Maciej and McGrath, John W. and Quinn, John P. and Cagney, Gerard and Auxiliadora Prieto, Maria and O'Connor, Kevin E.",
year = "2013",
abstract = "The primary enzyme involved in polyphosphate (polyP) synthesis, polyP kinase (ppk), has been deleted in Pseudomonas putidaKT2440. This has resulted in a threefold to sixfold reduction in polyhydroxyalkanoate (PHA) accumulation compared with the wild type under conditions of nitrogen limitation, with either temperature or oxidative (H2O2) stress, when grown on glucose. The accumulation of PHA by ppk mutant was the same as the wild type under nitrogen-limiting growth conditions. There was no difference in polyP levels between wild-type and ppk strains under all growth conditions tested. In the ppk mutant proteome, polyP kinase (PPK) was undetectable, but up-regulation of the polyp-associated proteins polyP adenosine triphosphate (ATP)/nicotinamide adenine dinucleotide (NAD) kinase (PpnK), a putative polyP adenosine monophosphate (AMP) phosphotransferase (PP_1752), and exopolyphosphatase was observed. ppk strain exhibited significantly retarded growth with glycerol as carbon and energy source (42h of lag period compared with 24h in wild-type strain) but similar growth to the wild-type strain with glucose. Analysis of gene transcription revealed downregulation of glycerol kinase and the glycerol facilitator respectively. Glycerol kinase protein expression was also downregulated in the ppk mutant. The deletion of ppk did not affect motility but reduced biofilm formation. Thus, the knockout of the ppk gene has resulted in a number of phenotypic changes to the mutant without affecting polyP accumulation.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Environmental Microbiology Reports",
title = "The effect of polyphosphate kinase gene deletion on polyhydroxyalkanoate accumulation and carbon metabolism in Pseudomonas putida KT2440",
volume = "5",
number = "5",
pages = "740-746",
doi = "10.1111/1758-2229.12076"
}

Casey, W. T., Nikodinović-Runić, J., Fonseca Garcia, P., Guzik, M., McGrath, J. W., Quinn, J. P., Cagney, G., Auxiliadora Prieto, M.,& O'Connor, K. E.. (2013). The effect of polyphosphate kinase gene deletion on polyhydroxyalkanoate accumulation and carbon metabolism in Pseudomonas putida KT2440. in Environmental Microbiology Reports
Wiley-Blackwell, Hoboken., 5(5), 740-746.
https://doi.org/10.1111/1758-2229.12076

Casey WT, Nikodinović-Runić J, Fonseca Garcia P, Guzik M, McGrath JW, Quinn JP, Cagney G, Auxiliadora Prieto M, O'Connor KE. The effect of polyphosphate kinase gene deletion on polyhydroxyalkanoate accumulation and carbon metabolism in Pseudomonas putida KT2440. in Environmental Microbiology Reports. 2013;5(5):740-746.
doi:10.1111/1758-2229.12076 .

Casey, William T., Nikodinović-Runić, Jasmina, Fonseca Garcia, Pilar, Guzik, Maciej, McGrath, John W., Quinn, John P., Cagney, Gerard, Auxiliadora Prieto, Maria, O'Connor, Kevin E., "The effect of polyphosphate kinase gene deletion on polyhydroxyalkanoate accumulation and carbon metabolism in Pseudomonas putida KT2440" in Environmental Microbiology Reports, 5, no. 5 (2013):740-746,
https://doi.org/10.1111/1758-2229.12076 . .

TY  - DATA
AU  - Casey, William T.
AU  - Nikodinović-Runić, Jasmina
AU  - Fonseca Garcia, Pilar
AU  - Guzik, Maciej
AU  - McGrath, John W.
AU  - Quinn, John P.
AU  - Cagney, Gerard
AU  - Auxiliadora Prieto, Maria
AU  - O'Connor, Kevin E.
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3554
PB  - Wiley-Blackwell, Hoboken
T2  - Environmental Microbiology Reports
T1  - Supplementary data for article: Casey, W. T.; Nikodinović-Runić, J.; Fonseca Garcia, P.; Guzik, M. W.; McGrath, J. W.; Quinn, J. P.; Cagney, G.; Auxiliadora Prieto, M.; O’Connor, K. E. The Effect of Polyphosphate Kinase Gene Deletion on Polyhydroxyalkanoate Accumulation and Carbon Metabolism in Pseudomonas Putida KT2440. Environmental Microbiology Reports 2013, 5 (5), 740–746. https://doi.org/10.1111/1758-2229.12076
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3554
ER  - 

@misc{
author = "Casey, William T. and Nikodinović-Runić, Jasmina and Fonseca Garcia, Pilar and Guzik, Maciej and McGrath, John W. and Quinn, John P. and Cagney, Gerard and Auxiliadora Prieto, Maria and O'Connor, Kevin E.",
year = "2013",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Environmental Microbiology Reports",
title = "Supplementary data for article: Casey, W. T.; Nikodinović-Runić, J.; Fonseca Garcia, P.; Guzik, M. W.; McGrath, J. W.; Quinn, J. P.; Cagney, G.; Auxiliadora Prieto, M.; O’Connor, K. E. The Effect of Polyphosphate Kinase Gene Deletion on Polyhydroxyalkanoate Accumulation and Carbon Metabolism in Pseudomonas Putida KT2440. Environmental Microbiology Reports 2013, 5 (5), 740–746. https://doi.org/10.1111/1758-2229.12076",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3554"
}

Casey, W. T., Nikodinović-Runić, J., Fonseca Garcia, P., Guzik, M., McGrath, J. W., Quinn, J. P., Cagney, G., Auxiliadora Prieto, M.,& O'Connor, K. E.. (2013). Supplementary data for article: Casey, W. T.; Nikodinović-Runić, J.; Fonseca Garcia, P.; Guzik, M. W.; McGrath, J. W.; Quinn, J. P.; Cagney, G.; Auxiliadora Prieto, M.; O’Connor, K. E. The Effect of Polyphosphate Kinase Gene Deletion on Polyhydroxyalkanoate Accumulation and Carbon Metabolism in Pseudomonas Putida KT2440. Environmental Microbiology Reports 2013, 5 (5), 740–746. https://doi.org/10.1111/1758-2229.12076. in Environmental Microbiology Reports
Wiley-Blackwell, Hoboken..
https://hdl.handle.net/21.15107/rcub_cherry_3554

Casey WT, Nikodinović-Runić J, Fonseca Garcia P, Guzik M, McGrath JW, Quinn JP, Cagney G, Auxiliadora Prieto M, O'Connor KE. Supplementary data for article: Casey, W. T.; Nikodinović-Runić, J.; Fonseca Garcia, P.; Guzik, M. W.; McGrath, J. W.; Quinn, J. P.; Cagney, G.; Auxiliadora Prieto, M.; O’Connor, K. E. The Effect of Polyphosphate Kinase Gene Deletion on Polyhydroxyalkanoate Accumulation and Carbon Metabolism in Pseudomonas Putida KT2440. Environmental Microbiology Reports 2013, 5 (5), 740–746. https://doi.org/10.1111/1758-2229.12076. in Environmental Microbiology Reports. 2013;.
https://hdl.handle.net/21.15107/rcub_cherry_3554 .

Casey, William T., Nikodinović-Runić, Jasmina, Fonseca Garcia, Pilar, Guzik, Maciej, McGrath, John W., Quinn, John P., Cagney, Gerard, Auxiliadora Prieto, Maria, O'Connor, Kevin E., "Supplementary data for article: Casey, W. T.; Nikodinović-Runić, J.; Fonseca Garcia, P.; Guzik, M. W.; McGrath, J. W.; Quinn, J. P.; Cagney, G.; Auxiliadora Prieto, M.; O’Connor, K. E. The Effect of Polyphosphate Kinase Gene Deletion on Polyhydroxyalkanoate Accumulation and Carbon Metabolism in Pseudomonas Putida KT2440. Environmental Microbiology Reports 2013, 5 (5), 740–746. https://doi.org/10.1111/1758-2229.12076" in Environmental Microbiology Reports (2013),
https://hdl.handle.net/21.15107/rcub_cherry_3554 .

TY  - JOUR
AU  - Nikodinović-Runić, Jasmina
AU  - Coulombel, Lydie
AU  - Francuski, Đorđe
AU  - Sharma, Narain D.
AU  - Boyd, Derek R.
AU  - Ferrall, Rory Moore O.
AU  - O'Connor, Kevin E.
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1355
AB  - Nine different sulfur-containing compounds were biotransformed to the corresponding sulfoxides by Escherichia coli Bl21(DE3) cells expressing styrene monooxygenase (SMO) from Pseudomonas putida CA-3. Thioanisole was consumed at 83.3 mu moles min(-1) g cell dry weight(-1) resulting mainly in the formation of R-thioanisole sulfoxide with an enantiomeric excess (ee) value of 45 %. The rate of 2-methyl-, 2-chloro- and 2-bromo-thioanisole consumption was 2-fold lower than that of thioanisole. Surprisingly, the 2-methylthioanisole sulfoxide product had the opposite (S) configuration to that of the other 2-substituted thioanisole derivatives and had a higher ee value (84 %). The rate of oxidation of 4-substituted thioanisoles was higher than the corresponding 2-substituted substrates but the ee values of the products were consistently lower (10-23 %). The rate of benzo[b]thiophene and 2-methylbenzo[b]thiophene sulfoxidation was approximately 10-fold lower than that of thioanisole. The ee value of the benzo[b]thiophene sulfoxide could not be determined as the product racemized rapidly. E. coli cells expressing an engineered SMO (SMOeng R3-11) oxidised 2-substituted thioanisoles between 1.8- and 2.8-fold faster compared to cells expressing the wild-type enzyme. SMOeng R3-11 oxidised benzo[b]thiophene and 2-methylbenzo[b]thiophene 10.1 and 5.6 times faster that the wild-type enzyme. The stereospecificity of the reaction catalysed by SMOeng was unchanged from that of the wild type. Using the X-ray crystal structure of the P. putida S12 SMO, it was evident that the entrance of substrates into the SMO active site is limited by the binding pocket bottleneck formed by the side chains of Val-211 and Asn-46 carboxyamide group.
PB  - Springer, New York
T2  - Applied Microbiology and Biotechnology
T1  - The oxidation of alkylaryl sulfides and benzo[b]thiophenes by Escherichia coli cells expressing wild-type and engineered styrene monooxygenase from Pseudomonas putida CA-3
VL  - 97
IS  - 11
SP  - 4849
EP  - 4858
DO  - 10.1007/s00253-012-4332-5
ER  - 

@article{
author = "Nikodinović-Runić, Jasmina and Coulombel, Lydie and Francuski, Đorđe and Sharma, Narain D. and Boyd, Derek R. and Ferrall, Rory Moore O. and O'Connor, Kevin E.",
year = "2013",
abstract = "Nine different sulfur-containing compounds were biotransformed to the corresponding sulfoxides by Escherichia coli Bl21(DE3) cells expressing styrene monooxygenase (SMO) from Pseudomonas putida CA-3. Thioanisole was consumed at 83.3 mu moles min(-1) g cell dry weight(-1) resulting mainly in the formation of R-thioanisole sulfoxide with an enantiomeric excess (ee) value of 45 %. The rate of 2-methyl-, 2-chloro- and 2-bromo-thioanisole consumption was 2-fold lower than that of thioanisole. Surprisingly, the 2-methylthioanisole sulfoxide product had the opposite (S) configuration to that of the other 2-substituted thioanisole derivatives and had a higher ee value (84 %). The rate of oxidation of 4-substituted thioanisoles was higher than the corresponding 2-substituted substrates but the ee values of the products were consistently lower (10-23 %). The rate of benzo[b]thiophene and 2-methylbenzo[b]thiophene sulfoxidation was approximately 10-fold lower than that of thioanisole. The ee value of the benzo[b]thiophene sulfoxide could not be determined as the product racemized rapidly. E. coli cells expressing an engineered SMO (SMOeng R3-11) oxidised 2-substituted thioanisoles between 1.8- and 2.8-fold faster compared to cells expressing the wild-type enzyme. SMOeng R3-11 oxidised benzo[b]thiophene and 2-methylbenzo[b]thiophene 10.1 and 5.6 times faster that the wild-type enzyme. The stereospecificity of the reaction catalysed by SMOeng was unchanged from that of the wild type. Using the X-ray crystal structure of the P. putida S12 SMO, it was evident that the entrance of substrates into the SMO active site is limited by the binding pocket bottleneck formed by the side chains of Val-211 and Asn-46 carboxyamide group.",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "The oxidation of alkylaryl sulfides and benzo[b]thiophenes by Escherichia coli cells expressing wild-type and engineered styrene monooxygenase from Pseudomonas putida CA-3",
volume = "97",
number = "11",
pages = "4849-4858",
doi = "10.1007/s00253-012-4332-5"
}

Nikodinović-Runić, J., Coulombel, L., Francuski, Đ., Sharma, N. D., Boyd, D. R., Ferrall, R. M. O.,& O'Connor, K. E.. (2013). The oxidation of alkylaryl sulfides and benzo[b]thiophenes by Escherichia coli cells expressing wild-type and engineered styrene monooxygenase from Pseudomonas putida CA-3. in Applied Microbiology and Biotechnology
Springer, New York., 97(11), 4849-4858.
https://doi.org/10.1007/s00253-012-4332-5

Nikodinović-Runić J, Coulombel L, Francuski Đ, Sharma ND, Boyd DR, Ferrall RMO, O'Connor KE. The oxidation of alkylaryl sulfides and benzo[b]thiophenes by Escherichia coli cells expressing wild-type and engineered styrene monooxygenase from Pseudomonas putida CA-3. in Applied Microbiology and Biotechnology. 2013;97(11):4849-4858.
doi:10.1007/s00253-012-4332-5 .

Nikodinović-Runić, Jasmina, Coulombel, Lydie, Francuski, Đorđe, Sharma, Narain D., Boyd, Derek R., Ferrall, Rory Moore O., O'Connor, Kevin E., "The oxidation of alkylaryl sulfides and benzo[b]thiophenes by Escherichia coli cells expressing wild-type and engineered styrene monooxygenase from Pseudomonas putida CA-3" in Applied Microbiology and Biotechnology, 97, no. 11 (2013):4849-4858,
https://doi.org/10.1007/s00253-012-4332-5 . .

TY  - JOUR
AU  - Brooks, Sarah J.
AU  - Nikodinović-Runić, Jasmina
AU  - Martin, Leona
AU  - Doyle, Evelyn M.
AU  - O'Sullivan, Timothy
AU  - Guiry, Patrick J.
AU  - Coulombel, Lydie
AU  - Li, Zhi
AU  - O'Connor, Kevin E.
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1352
AB  - 1-(3,4-Dihydroxyphenyl) ethanol was produced biocatalytically for the first time using mushroom tyrosinase. 4-Ethylphenol at 1 mM was consumed over 12 min giving 0.23 mM 4-ethylcatechol and 0.36 mM (R/S)-1-(3,4-dihydroxyphenyl) ethanol (ee 0.5 %). Mushroom tyrosinase consumed 4-ethylphenol at 6.7 mu mol min(-1) mg protein(-1) while the rates of formation of 4-ethylcatechol and 1-(3,4-dihydroxyphenyl) ethanol were 1.1 and 1.9 mu mol min(-1) mg protein(-1). Addition of the ascorbic acid, as a reducing agent to biotransformation reactions, increased 4-ethylcatechol formation by 340 %. However, accumulation of 1-(3,4-dihydroxyphenyl) ethanol was not observed in the presence of ascorbic acid. While the 1-(3,4-dihydroxyphenyl) ethanol was racemic, it is the first chiral product produced by tyrosinase starting from a non-chiral substrate.
PB  - Springer, Dordrecht
T2  - Biotechnology Letters
T1  - Production of a chiral alcohol, 1-(3,4-dihydroxyphenyl) ethanol, by mushroom tyrosinase
VL  - 35
IS  - 5
SP  - 779
EP  - 783
DO  - 10.1007/s10529-013-1148-z
ER  - 

@article{
author = "Brooks, Sarah J. and Nikodinović-Runić, Jasmina and Martin, Leona and Doyle, Evelyn M. and O'Sullivan, Timothy and Guiry, Patrick J. and Coulombel, Lydie and Li, Zhi and O'Connor, Kevin E.",
year = "2013",
abstract = "1-(3,4-Dihydroxyphenyl) ethanol was produced biocatalytically for the first time using mushroom tyrosinase. 4-Ethylphenol at 1 mM was consumed over 12 min giving 0.23 mM 4-ethylcatechol and 0.36 mM (R/S)-1-(3,4-dihydroxyphenyl) ethanol (ee 0.5 %). Mushroom tyrosinase consumed 4-ethylphenol at 6.7 mu mol min(-1) mg protein(-1) while the rates of formation of 4-ethylcatechol and 1-(3,4-dihydroxyphenyl) ethanol were 1.1 and 1.9 mu mol min(-1) mg protein(-1). Addition of the ascorbic acid, as a reducing agent to biotransformation reactions, increased 4-ethylcatechol formation by 340 %. However, accumulation of 1-(3,4-dihydroxyphenyl) ethanol was not observed in the presence of ascorbic acid. While the 1-(3,4-dihydroxyphenyl) ethanol was racemic, it is the first chiral product produced by tyrosinase starting from a non-chiral substrate.",
publisher = "Springer, Dordrecht",
journal = "Biotechnology Letters",
title = "Production of a chiral alcohol, 1-(3,4-dihydroxyphenyl) ethanol, by mushroom tyrosinase",
volume = "35",
number = "5",
pages = "779-783",
doi = "10.1007/s10529-013-1148-z"
}

Brooks, S. J., Nikodinović-Runić, J., Martin, L., Doyle, E. M., O'Sullivan, T., Guiry, P. J., Coulombel, L., Li, Z.,& O'Connor, K. E.. (2013). Production of a chiral alcohol, 1-(3,4-dihydroxyphenyl) ethanol, by mushroom tyrosinase. in Biotechnology Letters
Springer, Dordrecht., 35(5), 779-783.
https://doi.org/10.1007/s10529-013-1148-z

Brooks SJ, Nikodinović-Runić J, Martin L, Doyle EM, O'Sullivan T, Guiry PJ, Coulombel L, Li Z, O'Connor KE. Production of a chiral alcohol, 1-(3,4-dihydroxyphenyl) ethanol, by mushroom tyrosinase. in Biotechnology Letters. 2013;35(5):779-783.
doi:10.1007/s10529-013-1148-z .

Brooks, Sarah J., Nikodinović-Runić, Jasmina, Martin, Leona, Doyle, Evelyn M., O'Sullivan, Timothy, Guiry, Patrick J., Coulombel, Lydie, Li, Zhi, O'Connor, Kevin E., "Production of a chiral alcohol, 1-(3,4-dihydroxyphenyl) ethanol, by mushroom tyrosinase" in Biotechnology Letters, 35, no. 5 (2013):779-783,
https://doi.org/10.1007/s10529-013-1148-z . .

TY  - JOUR
AU  - Molloy, Susan
AU  - Nikodinović-Runić, Jasmina
AU  - Martin, Leona B.
AU  - Hartmann, Hermann
AU  - Solano, Francisco
AU  - Decker, Heinz
AU  - O'Connor, Kevin E.
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1359
AB  - The tyrosinase gene from Ralstonia solanacearum (GenBank NP518458) was subjected to random mutagenesis resulting in tyrosinase variants (RVC10 and RV145) with up to 3.2-fold improvement in kcat, 5.2-fold lower Km and 16-fold improvement in catalytic efficiency for D-tyrosine. Based on RVC10 and RV145 mutated sequences, single mutation variants were generated with all variants showing increased kcat for D-tyrosine compared to the wild type (WT). All single mutation variants based on RV145 had a higher kcat and Km value compared to the RV145 and thus the combination of four mutations in RV145 was antagonistic for turnover, but synergistic for affinity of the enzyme for D-tyrosine. Single mutation variant 145_V153A exhibited the highest (6.9-fold) improvement in kcat and a 2.4-fold increase in Km compared to the WT. Two single mutation variants, C10_N322S and C10_T183I reduced the Km up to 2.6-fold for D-tyrosine but one variant 145_V153A increased the Km 2.4-fold compared to the WT. Homology based modeling of R. solanacearum tyrosinase showed that mutation V153A disrupts the van der Waals interactions with an -helix providing one of the conserved histidine residues of the active site. The kcat and Km values for L-tyrosine decreased for RV145 and RVC10 compared to the WT. RV145 exhibited a 2.1-fold high catalytic efficiency compared to the WT which is a 7.6-fold lower improvement compared to D-tyrosine. RV145 exhibited a threefold higher monophenolase:diphenolase activity ratio for D-tyrosine:D-DOPA and a 1.4-fold higher L-tyrosine:L-DOPA activity ratio compared to the WT. Biotechnol. Bioeng. 2013; 110: 1849-1857.
PB  - Wiley-Blackwell, Hoboken
T2  - Biotechnology and Bioengineering
T1  - Engineering of a bacterial tyrosinase for improved catalytic efficiency towards D-tyrosine using random and site directed mutagenesis approaches
VL  - 110
IS  - 7
SP  - 1849
EP  - 1857
DO  - 10.1002/bit.24859
ER  - 

@article{
author = "Molloy, Susan and Nikodinović-Runić, Jasmina and Martin, Leona B. and Hartmann, Hermann and Solano, Francisco and Decker, Heinz and O'Connor, Kevin E.",
year = "2013",
abstract = "The tyrosinase gene from Ralstonia solanacearum (GenBank NP518458) was subjected to random mutagenesis resulting in tyrosinase variants (RVC10 and RV145) with up to 3.2-fold improvement in kcat, 5.2-fold lower Km and 16-fold improvement in catalytic efficiency for D-tyrosine. Based on RVC10 and RV145 mutated sequences, single mutation variants were generated with all variants showing increased kcat for D-tyrosine compared to the wild type (WT). All single mutation variants based on RV145 had a higher kcat and Km value compared to the RV145 and thus the combination of four mutations in RV145 was antagonistic for turnover, but synergistic for affinity of the enzyme for D-tyrosine. Single mutation variant 145_V153A exhibited the highest (6.9-fold) improvement in kcat and a 2.4-fold increase in Km compared to the WT. Two single mutation variants, C10_N322S and C10_T183I reduced the Km up to 2.6-fold for D-tyrosine but one variant 145_V153A increased the Km 2.4-fold compared to the WT. Homology based modeling of R. solanacearum tyrosinase showed that mutation V153A disrupts the van der Waals interactions with an -helix providing one of the conserved histidine residues of the active site. The kcat and Km values for L-tyrosine decreased for RV145 and RVC10 compared to the WT. RV145 exhibited a 2.1-fold high catalytic efficiency compared to the WT which is a 7.6-fold lower improvement compared to D-tyrosine. RV145 exhibited a threefold higher monophenolase:diphenolase activity ratio for D-tyrosine:D-DOPA and a 1.4-fold higher L-tyrosine:L-DOPA activity ratio compared to the WT. Biotechnol. Bioeng. 2013; 110: 1849-1857.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Biotechnology and Bioengineering",
title = "Engineering of a bacterial tyrosinase for improved catalytic efficiency towards D-tyrosine using random and site directed mutagenesis approaches",
volume = "110",
number = "7",
pages = "1849-1857",
doi = "10.1002/bit.24859"
}

Molloy, S., Nikodinović-Runić, J., Martin, L. B., Hartmann, H., Solano, F., Decker, H.,& O'Connor, K. E.. (2013). Engineering of a bacterial tyrosinase for improved catalytic efficiency towards D-tyrosine using random and site directed mutagenesis approaches. in Biotechnology and Bioengineering
Wiley-Blackwell, Hoboken., 110(7), 1849-1857.
https://doi.org/10.1002/bit.24859

Molloy S, Nikodinović-Runić J, Martin LB, Hartmann H, Solano F, Decker H, O'Connor KE. Engineering of a bacterial tyrosinase for improved catalytic efficiency towards D-tyrosine using random and site directed mutagenesis approaches. in Biotechnology and Bioengineering. 2013;110(7):1849-1857.
doi:10.1002/bit.24859 .

Molloy, Susan, Nikodinović-Runić, Jasmina, Martin, Leona B., Hartmann, Hermann, Solano, Francisco, Decker, Heinz, O'Connor, Kevin E., "Engineering of a bacterial tyrosinase for improved catalytic efficiency towards D-tyrosine using random and site directed mutagenesis approaches" in Biotechnology and Bioengineering, 110, no. 7 (2013):1849-1857,
https://doi.org/10.1002/bit.24859 . .

TY  - JOUR
AU  - Casey, William T.
AU  - Nikodinović-Runić, Jasmina
AU  - Fonseca Garcia, Pilar
AU  - Guzik, Maciej
AU  - McGrath, John W.
AU  - Quinn, John P.
AU  - Cagney, Gerard
AU  - Auxiliadora Prieto, Maria
AU  - O'Connor, Kevin E.
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1408
AB  - The primary enzyme involved in polyphosphate (polyP) synthesis, polyP kinase (ppk), has been deleted in Pseudomonas putidaKT2440. This has resulted in a threefold to sixfold reduction in polyhydroxyalkanoate (PHA) accumulation compared with the wild type under conditions of nitrogen limitation, with either temperature or oxidative (H2O2) stress, when grown on glucose. The accumulation of PHA by ppk mutant was the same as the wild type under nitrogen-limiting growth conditions. There was no difference in polyP levels between wild-type and ppk strains under all growth conditions tested. In the ppk mutant proteome, polyP kinase (PPK) was undetectable, but up-regulation of the polyp-associated proteins polyP adenosine triphosphate (ATP)/nicotinamide adenine dinucleotide (NAD) kinase (PpnK), a putative polyP adenosine monophosphate (AMP) phosphotransferase (PP_1752), and exopolyphosphatase was observed. ppk strain exhibited significantly retarded growth with glycerol as carbon and energy source (42h of lag period compared with 24h in wild-type strain) but similar growth to the wild-type strain with glucose. Analysis of gene transcription revealed downregulation of glycerol kinase and the glycerol facilitator respectively. Glycerol kinase protein expression was also downregulated in the ppk mutant. The deletion of ppk did not affect motility but reduced biofilm formation. Thus, the knockout of the ppk gene has resulted in a number of phenotypic changes to the mutant without affecting polyP accumulation.
PB  - Wiley-Blackwell, Hoboken
T2  - Environmental Microbiology Reports
T1  - The effect of polyphosphate kinase gene deletion on polyhydroxyalkanoate accumulation and carbon metabolism in Pseudomonas putida KT2440
VL  - 5
IS  - 5
SP  - 740
EP  - 746
DO  - 10.1111/1758-2229.12076
ER  - 

@article{
author = "Casey, William T. and Nikodinović-Runić, Jasmina and Fonseca Garcia, Pilar and Guzik, Maciej and McGrath, John W. and Quinn, John P. and Cagney, Gerard and Auxiliadora Prieto, Maria and O'Connor, Kevin E.",
year = "2013",
abstract = "The primary enzyme involved in polyphosphate (polyP) synthesis, polyP kinase (ppk), has been deleted in Pseudomonas putidaKT2440. This has resulted in a threefold to sixfold reduction in polyhydroxyalkanoate (PHA) accumulation compared with the wild type under conditions of nitrogen limitation, with either temperature or oxidative (H2O2) stress, when grown on glucose. The accumulation of PHA by ppk mutant was the same as the wild type under nitrogen-limiting growth conditions. There was no difference in polyP levels between wild-type and ppk strains under all growth conditions tested. In the ppk mutant proteome, polyP kinase (PPK) was undetectable, but up-regulation of the polyp-associated proteins polyP adenosine triphosphate (ATP)/nicotinamide adenine dinucleotide (NAD) kinase (PpnK), a putative polyP adenosine monophosphate (AMP) phosphotransferase (PP_1752), and exopolyphosphatase was observed. ppk strain exhibited significantly retarded growth with glycerol as carbon and energy source (42h of lag period compared with 24h in wild-type strain) but similar growth to the wild-type strain with glucose. Analysis of gene transcription revealed downregulation of glycerol kinase and the glycerol facilitator respectively. Glycerol kinase protein expression was also downregulated in the ppk mutant. The deletion of ppk did not affect motility but reduced biofilm formation. Thus, the knockout of the ppk gene has resulted in a number of phenotypic changes to the mutant without affecting polyP accumulation.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Environmental Microbiology Reports",
title = "The effect of polyphosphate kinase gene deletion on polyhydroxyalkanoate accumulation and carbon metabolism in Pseudomonas putida KT2440",
volume = "5",
number = "5",
pages = "740-746",
doi = "10.1111/1758-2229.12076"
}

Casey, W. T., Nikodinović-Runić, J., Fonseca Garcia, P., Guzik, M., McGrath, J. W., Quinn, J. P., Cagney, G., Auxiliadora Prieto, M.,& O'Connor, K. E.. (2013). The effect of polyphosphate kinase gene deletion on polyhydroxyalkanoate accumulation and carbon metabolism in Pseudomonas putida KT2440. in Environmental Microbiology Reports
Wiley-Blackwell, Hoboken., 5(5), 740-746.
https://doi.org/10.1111/1758-2229.12076

Casey WT, Nikodinović-Runić J, Fonseca Garcia P, Guzik M, McGrath JW, Quinn JP, Cagney G, Auxiliadora Prieto M, O'Connor KE. The effect of polyphosphate kinase gene deletion on polyhydroxyalkanoate accumulation and carbon metabolism in Pseudomonas putida KT2440. in Environmental Microbiology Reports. 2013;5(5):740-746.
doi:10.1111/1758-2229.12076 .

Casey, William T., Nikodinović-Runić, Jasmina, Fonseca Garcia, Pilar, Guzik, Maciej, McGrath, John W., Quinn, John P., Cagney, Gerard, Auxiliadora Prieto, Maria, O'Connor, Kevin E., "The effect of polyphosphate kinase gene deletion on polyhydroxyalkanoate accumulation and carbon metabolism in Pseudomonas putida KT2440" in Environmental Microbiology Reports, 5, no. 5 (2013):740-746,
https://doi.org/10.1111/1758-2229.12076 . .

TY  - JOUR
AU  - Narančić, Tanja
AU  - Đokić, Lidija
AU  - Kenny, Shane T.
AU  - O'Connor, Kevin E.
AU  - Radulovic, Vanja
AU  - Nikodinović-Runić, Jasmina
AU  - Vasiljević, Branka
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1064
AB  - Gram-positive bacteria from river sediments affected by the proximity of a petrochemical industrial site were isolated and characterized with respect to their ability to degrade a wide range of aromatic compounds. In this study we identified metabolically diverse Gram-positive bacteria capable of growth on wide range aromatic compounds in the presence of heavy metals and with the ability to accumulate biopolymers. Thirty-four isolates that were able to use 9 or more common aromatic pollutants, such as benzene, biphenyl, naphthalene etc. as a sole source of carbon and energy included members of Bacillus, Arthrobacter, Rhodococcus, Gordonia, Streptomyces, and Staphylococcus genus. Rhodococcus sp. TN105, Gordonia sp. TN103 and Arthrobacter sp. TN221 were identified as novel strains. Nine isolates were able to grow in the presence of one or more metals (mercury, cadmium, nickel) at high concentration (100 mM). Seven isolates could degrade 15 different aromatic compounds and could grow in the presence of one or more heavy metals. Two of these isolates were resistant to multiple antibiotics including erythromycin and nalidixic acid. One third of isolates could accumulate at least one biopolymer. Twelve isolates (mainly Bacillus sp. and Arthrobacter sp.) accumulated polyphosphate, 3 Bacillus sp. accumulated polyhydroxybutyrate, while 4 isolates could accumulate exopolysaccharides. (C) 2012 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Journal of Hazardous Materials
T1  - Metabolic versatility of Gram-positive microbial isolates from contaminated river sediments
VL  - 215
SP  - 243
EP  - 251
DO  - 10.1016/j.jhazmat.2012.02.059
ER  - 

@article{
author = "Narančić, Tanja and Đokić, Lidija and Kenny, Shane T. and O'Connor, Kevin E. and Radulovic, Vanja and Nikodinović-Runić, Jasmina and Vasiljević, Branka",
year = "2012",
abstract = "Gram-positive bacteria from river sediments affected by the proximity of a petrochemical industrial site were isolated and characterized with respect to their ability to degrade a wide range of aromatic compounds. In this study we identified metabolically diverse Gram-positive bacteria capable of growth on wide range aromatic compounds in the presence of heavy metals and with the ability to accumulate biopolymers. Thirty-four isolates that were able to use 9 or more common aromatic pollutants, such as benzene, biphenyl, naphthalene etc. as a sole source of carbon and energy included members of Bacillus, Arthrobacter, Rhodococcus, Gordonia, Streptomyces, and Staphylococcus genus. Rhodococcus sp. TN105, Gordonia sp. TN103 and Arthrobacter sp. TN221 were identified as novel strains. Nine isolates were able to grow in the presence of one or more metals (mercury, cadmium, nickel) at high concentration (100 mM). Seven isolates could degrade 15 different aromatic compounds and could grow in the presence of one or more heavy metals. Two of these isolates were resistant to multiple antibiotics including erythromycin and nalidixic acid. One third of isolates could accumulate at least one biopolymer. Twelve isolates (mainly Bacillus sp. and Arthrobacter sp.) accumulated polyphosphate, 3 Bacillus sp. accumulated polyhydroxybutyrate, while 4 isolates could accumulate exopolysaccharides. (C) 2012 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Journal of Hazardous Materials",
title = "Metabolic versatility of Gram-positive microbial isolates from contaminated river sediments",
volume = "215",
pages = "243-251",
doi = "10.1016/j.jhazmat.2012.02.059"
}

Narančić, T., Đokić, L., Kenny, S. T., O'Connor, K. E., Radulovic, V., Nikodinović-Runić, J.,& Vasiljević, B.. (2012). Metabolic versatility of Gram-positive microbial isolates from contaminated river sediments. in Journal of Hazardous Materials
Elsevier Science Bv, Amsterdam., 215, 243-251.
https://doi.org/10.1016/j.jhazmat.2012.02.059

Narančić T, Đokić L, Kenny ST, O'Connor KE, Radulovic V, Nikodinović-Runić J, Vasiljević B. Metabolic versatility of Gram-positive microbial isolates from contaminated river sediments. in Journal of Hazardous Materials. 2012;215:243-251.
doi:10.1016/j.jhazmat.2012.02.059 .

Narančić, Tanja, Đokić, Lidija, Kenny, Shane T., O'Connor, Kevin E., Radulovic, Vanja, Nikodinović-Runić, Jasmina, Vasiljević, Branka, "Metabolic versatility of Gram-positive microbial isolates from contaminated river sediments" in Journal of Hazardous Materials, 215 (2012):243-251,
https://doi.org/10.1016/j.jhazmat.2012.02.059 . .

TY  - JOUR
AU  - Kenny, Shane T.
AU  - Nikodinović-Runić, Jasmina
AU  - Kaminsky, Walter
AU  - Woods, Trevor
AU  - Babu, Ramesh P.
AU  - O'Connor, Kevin E.
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1319
AB  - Sodium terephthalate (TA) produced from a PET pyrolysis product and waste glycerol (WG) from biodiesel manufacture were supplied to Pseudomonas putida GO16 in a fed-batch bioreactor. Six feeding strategies were employed by altering the sequence of TA and WG feeding. P. putida GO16 reached 8.70 g/l cell dry weight (CDW) and 2.61 g/l PHA in 48 h when grown on TA alone. When TA and WG were supplied in combination, biomass productivity (g/l/h) was increased between 1.3- and 1.7-fold and PHA productivity (g/l/h) was increased 1.8- to 2.2-fold compared to TA supplied alone. The monomer composition of the PHA accumulated from TA or WG was predominantly composed of 3-hydroxydecanoic acid. PHA monomers 3-hydroxytetradeeanoic acid and 3-hydroxytetradecenoic acid were not present in PHA accumulated from TA alone but were present when WG was supplied to the fermentation. When WG was either the sole carbon source or the predominant carbon source supplied to the fermentation the molecular weight of PHA accumulated was lower compared to PHA accumulated when TA was supplied as the sole substrate. Despite similarities in data for the properties of the polymers, PHAs produced with WG present in the PHA accumulation phase were tacky while PHA produced where TA was the sole carbon substrate in the polymer accumulation phase exhibited little or no tackiness at room temperature. The co-feeding of WG to fermentations allows for increased utilisation of TA. The order of feeding of WG and TA has an effect on TA utilisation and polymer properties.
PB  - Springer, New York
T2  - Applied Microbiology and Biotechnology
T1  - Development of a bioprocess to convert PET derived terephthalic acid and biodiesel derived glycerol to medium chain length polyhydroxyalkanoate
VL  - 95
IS  - 3
SP  - 623
EP  - 633
DO  - 10.1007/s00253-012-4058-4
ER  - 

@article{
author = "Kenny, Shane T. and Nikodinović-Runić, Jasmina and Kaminsky, Walter and Woods, Trevor and Babu, Ramesh P. and O'Connor, Kevin E.",
year = "2012",
abstract = "Sodium terephthalate (TA) produced from a PET pyrolysis product and waste glycerol (WG) from biodiesel manufacture were supplied to Pseudomonas putida GO16 in a fed-batch bioreactor. Six feeding strategies were employed by altering the sequence of TA and WG feeding. P. putida GO16 reached 8.70 g/l cell dry weight (CDW) and 2.61 g/l PHA in 48 h when grown on TA alone. When TA and WG were supplied in combination, biomass productivity (g/l/h) was increased between 1.3- and 1.7-fold and PHA productivity (g/l/h) was increased 1.8- to 2.2-fold compared to TA supplied alone. The monomer composition of the PHA accumulated from TA or WG was predominantly composed of 3-hydroxydecanoic acid. PHA monomers 3-hydroxytetradeeanoic acid and 3-hydroxytetradecenoic acid were not present in PHA accumulated from TA alone but were present when WG was supplied to the fermentation. When WG was either the sole carbon source or the predominant carbon source supplied to the fermentation the molecular weight of PHA accumulated was lower compared to PHA accumulated when TA was supplied as the sole substrate. Despite similarities in data for the properties of the polymers, PHAs produced with WG present in the PHA accumulation phase were tacky while PHA produced where TA was the sole carbon substrate in the polymer accumulation phase exhibited little or no tackiness at room temperature. The co-feeding of WG to fermentations allows for increased utilisation of TA. The order of feeding of WG and TA has an effect on TA utilisation and polymer properties.",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "Development of a bioprocess to convert PET derived terephthalic acid and biodiesel derived glycerol to medium chain length polyhydroxyalkanoate",
volume = "95",
number = "3",
pages = "623-633",
doi = "10.1007/s00253-012-4058-4"
}

Kenny, S. T., Nikodinović-Runić, J., Kaminsky, W., Woods, T., Babu, R. P.,& O'Connor, K. E.. (2012). Development of a bioprocess to convert PET derived terephthalic acid and biodiesel derived glycerol to medium chain length polyhydroxyalkanoate. in Applied Microbiology and Biotechnology
Springer, New York., 95(3), 623-633.
https://doi.org/10.1007/s00253-012-4058-4

Kenny ST, Nikodinović-Runić J, Kaminsky W, Woods T, Babu RP, O'Connor KE. Development of a bioprocess to convert PET derived terephthalic acid and biodiesel derived glycerol to medium chain length polyhydroxyalkanoate. in Applied Microbiology and Biotechnology. 2012;95(3):623-633.
doi:10.1007/s00253-012-4058-4 .

Kenny, Shane T., Nikodinović-Runić, Jasmina, Kaminsky, Walter, Woods, Trevor, Babu, Ramesh P., O'Connor, Kevin E., "Development of a bioprocess to convert PET derived terephthalic acid and biodiesel derived glycerol to medium chain length polyhydroxyalkanoate" in Applied Microbiology and Biotechnology, 95, no. 3 (2012):623-633,
https://doi.org/10.1007/s00253-012-4058-4 . .

TY  - JOUR
AU  - Boyd, Derek R.
AU  - Sharma, Narain D.
AU  - McMurray, Brian
AU  - Haughey, Simon A.
AU  - Allen, Christopher C. R.
AU  - Hamilton, John T. G.
AU  - McRoberts, W. Colin
AU  - O'Ferrall, Rory A. More
AU  - Nikodinović-Runić, Jasmina
AU  - Coulombel, Lydie A.
AU  - O'Connor, Kevin E.
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1238
AB  - Asymmetric heteroatom oxidation of benzo[b]thiophenes to yield the corresponding sulfoxides was catalysed by toluene dioxygenase (TDO), naphthalene dioxygenase (NDO) and styrene monooxygenase (SMO) enzymes present in P. putida mutant and E. coli recombinant whole cells. TDO-catalysed oxidation yielded the relatively unstable benzo[b] thiophene sulfoxide; its dimerization, followed by dehydrogenation, resulted in the isolation of stable tetracyclic sulfoxides as minor products with cis-dihydrodiols being the dominant metabolites. SMO mainly catalysed the formation of enantioenriched benzo[b] thiophene sulfoxide and 2-methyl benzo[b] thiophene sulfoxides which racemized at ambient temperature. The barriers to pyramidal sulfur inversion of 2- and 3-methyl benzo[b] thiophene sulfoxide metabolites, obtained using TDO and NDO as biocatalysts, were found to be ca.: 25-27 kcal mol(-1). The absolute configurations of the benzo[b] thiophene sulfoxides were determined by ECD spectroscopy, X-ray crystallography and stereochemical correlation. A site-directed mutant E. coli strain containing an engineered form of NDO, was found to change the regioselectivity toward preferential oxidation of the thiophene ring rather than the benzene ring.
PB  - Royal Soc Chemistry, Cambridge
T2  - Organic and Biomolecular Chemistry
T1  - Bacterial dioxygenase- and monooxygenase-catalysed sulfoxidation of benzo[b]thiophenes
VL  - 10
IS  - 4
SP  - 782
EP  - 790
DO  - 10.1039/c1ob06678a
ER  - 

@article{
author = "Boyd, Derek R. and Sharma, Narain D. and McMurray, Brian and Haughey, Simon A. and Allen, Christopher C. R. and Hamilton, John T. G. and McRoberts, W. Colin and O'Ferrall, Rory A. More and Nikodinović-Runić, Jasmina and Coulombel, Lydie A. and O'Connor, Kevin E.",
year = "2012",
abstract = "Asymmetric heteroatom oxidation of benzo[b]thiophenes to yield the corresponding sulfoxides was catalysed by toluene dioxygenase (TDO), naphthalene dioxygenase (NDO) and styrene monooxygenase (SMO) enzymes present in P. putida mutant and E. coli recombinant whole cells. TDO-catalysed oxidation yielded the relatively unstable benzo[b] thiophene sulfoxide; its dimerization, followed by dehydrogenation, resulted in the isolation of stable tetracyclic sulfoxides as minor products with cis-dihydrodiols being the dominant metabolites. SMO mainly catalysed the formation of enantioenriched benzo[b] thiophene sulfoxide and 2-methyl benzo[b] thiophene sulfoxides which racemized at ambient temperature. The barriers to pyramidal sulfur inversion of 2- and 3-methyl benzo[b] thiophene sulfoxide metabolites, obtained using TDO and NDO as biocatalysts, were found to be ca.: 25-27 kcal mol(-1). The absolute configurations of the benzo[b] thiophene sulfoxides were determined by ECD spectroscopy, X-ray crystallography and stereochemical correlation. A site-directed mutant E. coli strain containing an engineered form of NDO, was found to change the regioselectivity toward preferential oxidation of the thiophene ring rather than the benzene ring.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "Organic and Biomolecular Chemistry",
title = "Bacterial dioxygenase- and monooxygenase-catalysed sulfoxidation of benzo[b]thiophenes",
volume = "10",
number = "4",
pages = "782-790",
doi = "10.1039/c1ob06678a"
}

Boyd, D. R., Sharma, N. D., McMurray, B., Haughey, S. A., Allen, C. C. R., Hamilton, J. T. G., McRoberts, W. C., O'Ferrall, R. A. M., Nikodinović-Runić, J., Coulombel, L. A.,& O'Connor, K. E.. (2012). Bacterial dioxygenase- and monooxygenase-catalysed sulfoxidation of benzo[b]thiophenes. in Organic and Biomolecular Chemistry
Royal Soc Chemistry, Cambridge., 10(4), 782-790.
https://doi.org/10.1039/c1ob06678a

Boyd DR, Sharma ND, McMurray B, Haughey SA, Allen CCR, Hamilton JTG, McRoberts WC, O'Ferrall RAM, Nikodinović-Runić J, Coulombel LA, O'Connor KE. Bacterial dioxygenase- and monooxygenase-catalysed sulfoxidation of benzo[b]thiophenes. in Organic and Biomolecular Chemistry. 2012;10(4):782-790.
doi:10.1039/c1ob06678a .

Boyd, Derek R., Sharma, Narain D., McMurray, Brian, Haughey, Simon A., Allen, Christopher C. R., Hamilton, John T. G., McRoberts, W. Colin, O'Ferrall, Rory A. More, Nikodinović-Runić, Jasmina, Coulombel, Lydie A., O'Connor, Kevin E., "Bacterial dioxygenase- and monooxygenase-catalysed sulfoxidation of benzo[b]thiophenes" in Organic and Biomolecular Chemistry, 10, no. 4 (2012):782-790,
https://doi.org/10.1039/c1ob06678a . .

TY  - JOUR
AU  - Nikodinović-Runić, Jasmina
AU  - Casey, Eoin
AU  - Duane, Gearoid F.
AU  - Mitić, Dragana
AU  - Hume, Aisling R.
AU  - Kenny, Shane T.
AU  - O'Connor, Kevin E.
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1193
AB  - The improvement and modeling of a process for the supply of the volatile aromatic hydrocarbon, styrene, to a fermentor for increased biomass production of the medium chain length polyhydroxyalkanoate (mcl-PHA) accumulating bacterium Pseudomonas putida CA-3 was investigated. Fed-batch experiments were undertaken using different methods to provide the styrene. Initial experiments where styrene was supplied as a liquid to the bioreactor had detrimental effects on cell growth and inhibited PHA polymer accumulation. By changing the feed of gaseous styrene to liquid styrene through the air sparger a 5.4-fold increase in cell dry-weight was achieved (total of 10.56 g L(-1)) which corresponds to a fourfold improvement in PHA production (3.36 g L(-1)) compared to previous studies performed in our laboratory (0.82 g L(-1)). In addition this final improved feeding strategy reduced the release of styrene from the fermentor 50-fold compared to initial experiments (0.12mL total styrene released per 48 h run). An unstructured kinetic model was developed to describe cell growth along with substrate and oxygen utilization. The formation of dispersed gas (air) and liquid (styrene) phases in the medium and the transfer of styrene between the aqueous and dispersed liquid droplet phases was also modeled. The model provided a detailed description of these phase transitions and helped explain how the feeding strategy led to improved process performance in terms of final biomass levels. It also highlighted the key factors to be considered during further process improvement. Biotechnol. Bioeng. 2011; 108: 2447-2455. (C) 2011 Wiley Periodicals, Inc.
PB  - Wiley-Blackwell, Malden
T2  - Biotechnology and Bioengineering
T1  - Process Analysis of the Conversion of Styrene to Biomass and Medium Chain Length Polyhydroxyalkanoate in a Two-Phase Bioreactor
VL  - 108
IS  - 10
SP  - 2447
EP  - 2455
DO  - 10.1002/bit.23187
ER  - 

@article{
author = "Nikodinović-Runić, Jasmina and Casey, Eoin and Duane, Gearoid F. and Mitić, Dragana and Hume, Aisling R. and Kenny, Shane T. and O'Connor, Kevin E.",
year = "2011",
abstract = "The improvement and modeling of a process for the supply of the volatile aromatic hydrocarbon, styrene, to a fermentor for increased biomass production of the medium chain length polyhydroxyalkanoate (mcl-PHA) accumulating bacterium Pseudomonas putida CA-3 was investigated. Fed-batch experiments were undertaken using different methods to provide the styrene. Initial experiments where styrene was supplied as a liquid to the bioreactor had detrimental effects on cell growth and inhibited PHA polymer accumulation. By changing the feed of gaseous styrene to liquid styrene through the air sparger a 5.4-fold increase in cell dry-weight was achieved (total of 10.56 g L(-1)) which corresponds to a fourfold improvement in PHA production (3.36 g L(-1)) compared to previous studies performed in our laboratory (0.82 g L(-1)). In addition this final improved feeding strategy reduced the release of styrene from the fermentor 50-fold compared to initial experiments (0.12mL total styrene released per 48 h run). An unstructured kinetic model was developed to describe cell growth along with substrate and oxygen utilization. The formation of dispersed gas (air) and liquid (styrene) phases in the medium and the transfer of styrene between the aqueous and dispersed liquid droplet phases was also modeled. The model provided a detailed description of these phase transitions and helped explain how the feeding strategy led to improved process performance in terms of final biomass levels. It also highlighted the key factors to be considered during further process improvement. Biotechnol. Bioeng. 2011; 108: 2447-2455. (C) 2011 Wiley Periodicals, Inc.",
publisher = "Wiley-Blackwell, Malden",
journal = "Biotechnology and Bioengineering",
title = "Process Analysis of the Conversion of Styrene to Biomass and Medium Chain Length Polyhydroxyalkanoate in a Two-Phase Bioreactor",
volume = "108",
number = "10",
pages = "2447-2455",
doi = "10.1002/bit.23187"
}

Nikodinović-Runić, J., Casey, E., Duane, G. F., Mitić, D., Hume, A. R., Kenny, S. T.,& O'Connor, K. E.. (2011). Process Analysis of the Conversion of Styrene to Biomass and Medium Chain Length Polyhydroxyalkanoate in a Two-Phase Bioreactor. in Biotechnology and Bioengineering
Wiley-Blackwell, Malden., 108(10), 2447-2455.
https://doi.org/10.1002/bit.23187

Nikodinović-Runić J, Casey E, Duane GF, Mitić D, Hume AR, Kenny ST, O'Connor KE. Process Analysis of the Conversion of Styrene to Biomass and Medium Chain Length Polyhydroxyalkanoate in a Two-Phase Bioreactor. in Biotechnology and Bioengineering. 2011;108(10):2447-2455.
doi:10.1002/bit.23187 .

Nikodinović-Runić, Jasmina, Casey, Eoin, Duane, Gearoid F., Mitić, Dragana, Hume, Aisling R., Kenny, Shane T., O'Connor, Kevin E., "Process Analysis of the Conversion of Styrene to Biomass and Medium Chain Length Polyhydroxyalkanoate in a Two-Phase Bioreactor" in Biotechnology and Bioengineering, 108, no. 10 (2011):2447-2455,
https://doi.org/10.1002/bit.23187 . .

TY  - JOUR
AU  - Coulombel, Lydie
AU  - Nolan, Louise C.
AU  - Nikodinović-Runić, Jasmina
AU  - Doyle, Evelyn M.
AU  - O'Connor, Kevin E.
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1161
AB  - Escherichia coli cells, expressing 4-hydroxyphenylacetate 3-hydroxylase, fully transformed 4-halogenated phenols to their equivalent catechols as single products in shaken flasks. 4-Fluorophenol was transformed at a rate 1.6, 1.8, and 3.4-fold higher than the biotransformation of 4-chloro-, 4-bromo-, and 4-iodo- phenol, respectively. A scale-up from shaken flask to a 5 L stirred tank bioreactor was undertaken to develop a bioprocess for the production of 4-substituted halocatechols at higher concentrations and scale. In a stirred tank reactor, the optimized conditions for induction of 4-HPA hydroxylase expression were at 37 C for 3 h. The rate of biotransformation of 4-fluorophenol to 4-fluorocatechol by stirred tank bioreactor grown cells was the same at 1 and 4.8 mM (5.13 mu mol/min/g CDW) once the ratio of biocatalyst (E. coli CDW) to substrate concentration (mM) was maintained at 2:1. At 10.8 mM 4-fluorophenol, the rate of 4-fluorocatechol formation decreased by 4.7-fold. However, the complete transformation of 1.3 g of 4-fluorophenol (10.8 mM) to 4-fluorocatechol was achieved within 7 h in a 1 L reaction volume. Similar to 4-fluorophenol, other 4-substituted halophenols were completely transformed to 4-halocatechols at 2 mM within a 1-2 h period. An increase in 4-halophenol concentration to 4.8 mM resulted in a 2.5-20-fold decrease in biotransformation efficiency depending on the substrate tested. Organic solvent extraction of the 4-halocatechol products followed by column chromatography resulted in the production of purified products with a final yield of between 33% and 38%.
PB  - Springer, New York
T2  - Applied Microbiology and Biotechnology
T1  - Biotransformation of 4-halophenols to 4-halocatechols using Escherichia coli expressing 4-hydroxyphenylacetate 3-hydroxylase
VL  - 89
IS  - 6
SP  - 1867
EP  - 1875
DO  - 10.1007/s00253-010-2969-5
ER  - 

@article{
author = "Coulombel, Lydie and Nolan, Louise C. and Nikodinović-Runić, Jasmina and Doyle, Evelyn M. and O'Connor, Kevin E.",
year = "2011",
abstract = "Escherichia coli cells, expressing 4-hydroxyphenylacetate 3-hydroxylase, fully transformed 4-halogenated phenols to their equivalent catechols as single products in shaken flasks. 4-Fluorophenol was transformed at a rate 1.6, 1.8, and 3.4-fold higher than the biotransformation of 4-chloro-, 4-bromo-, and 4-iodo- phenol, respectively. A scale-up from shaken flask to a 5 L stirred tank bioreactor was undertaken to develop a bioprocess for the production of 4-substituted halocatechols at higher concentrations and scale. In a stirred tank reactor, the optimized conditions for induction of 4-HPA hydroxylase expression were at 37 C for 3 h. The rate of biotransformation of 4-fluorophenol to 4-fluorocatechol by stirred tank bioreactor grown cells was the same at 1 and 4.8 mM (5.13 mu mol/min/g CDW) once the ratio of biocatalyst (E. coli CDW) to substrate concentration (mM) was maintained at 2:1. At 10.8 mM 4-fluorophenol, the rate of 4-fluorocatechol formation decreased by 4.7-fold. However, the complete transformation of 1.3 g of 4-fluorophenol (10.8 mM) to 4-fluorocatechol was achieved within 7 h in a 1 L reaction volume. Similar to 4-fluorophenol, other 4-substituted halophenols were completely transformed to 4-halocatechols at 2 mM within a 1-2 h period. An increase in 4-halophenol concentration to 4.8 mM resulted in a 2.5-20-fold decrease in biotransformation efficiency depending on the substrate tested. Organic solvent extraction of the 4-halocatechol products followed by column chromatography resulted in the production of purified products with a final yield of between 33% and 38%.",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "Biotransformation of 4-halophenols to 4-halocatechols using Escherichia coli expressing 4-hydroxyphenylacetate 3-hydroxylase",
volume = "89",
number = "6",
pages = "1867-1875",
doi = "10.1007/s00253-010-2969-5"
}

Coulombel, L., Nolan, L. C., Nikodinović-Runić, J., Doyle, E. M.,& O'Connor, K. E.. (2011). Biotransformation of 4-halophenols to 4-halocatechols using Escherichia coli expressing 4-hydroxyphenylacetate 3-hydroxylase. in Applied Microbiology and Biotechnology
Springer, New York., 89(6), 1867-1875.
https://doi.org/10.1007/s00253-010-2969-5

Coulombel L, Nolan LC, Nikodinović-Runić J, Doyle EM, O'Connor KE. Biotransformation of 4-halophenols to 4-halocatechols using Escherichia coli expressing 4-hydroxyphenylacetate 3-hydroxylase. in Applied Microbiology and Biotechnology. 2011;89(6):1867-1875.
doi:10.1007/s00253-010-2969-5 .

Coulombel, Lydie, Nolan, Louise C., Nikodinović-Runić, Jasmina, Doyle, Evelyn M., O'Connor, Kevin E., "Biotransformation of 4-halophenols to 4-halocatechols using Escherichia coli expressing 4-hydroxyphenylacetate 3-hydroxylase" in Applied Microbiology and Biotechnology, 89, no. 6 (2011):1867-1875,
https://doi.org/10.1007/s00253-010-2969-5 . .

TY  - JOUR
AU  - Gursky, Lucas J.
AU  - Nikodinović-Runić, Jasmina
AU  - Feenstra, K. Anton
AU  - O'Connor, Kevin E.
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1041
AB  - The styAB genes from Pseudomonas putida CA-3, which encode styrene monooxygenase, were subjected to three rounds of in vitro evolution using error-prone polymerase chain reaction with a view to improving the rate of styrene oxide and indene oxide formation. Improvements in styrene monooxygenase activity were monitored using an indole to indigo conversion assay. Each round of random mutagenesis generated variants improved in indigo formation with third round variants improved nine- to 12-fold over the wild type enzyme. Each round of in vitro evolution resulted in two to three amino acid substitutions in styrene monooxygenase. While the majority of mutations occurred in styA (oxygenase), mutations were also observed in styB (reductase). A mutation resulting in the substitution of valine with isoleucine at amino acid residue 303 occurred near the styrene and flavin adenine dinucleotide binding site of styrene monooxygenase. One mutation caused a shift in the reading frame in styA and resulted in a StyA variant that is 19 amino acids longer than the wild-type protein. Whole cells expressing the best styrene monooxygenase variants (round 3) exhibited eight- and 12-fold improvements in styrene and indene oxidation rates compared to the wild-type enzyme. In all cases, a single enantiomer, (S)-styrene oxide, was formed from styrene while (1S,2R)-indene oxide was the predominant enantiomer (e.e. 97%) formed from indene. The average yield of styrene oxide and indene oxide from their respective alkene substrates was 65% and 90%, respectively.
PB  - Springer, New York
T2  - Applied Microbiology and Biotechnology
T1  - In vitro evolution of styrene monooxygenase from Pseudomonas putida CA-3 for improved epoxide synthesis
VL  - 85
IS  - 4
SP  - 995
EP  - 1004
DO  - 10.1007/s00253-009-2096-3
ER  - 

@article{
author = "Gursky, Lucas J. and Nikodinović-Runić, Jasmina and Feenstra, K. Anton and O'Connor, Kevin E.",
year = "2010",
abstract = "The styAB genes from Pseudomonas putida CA-3, which encode styrene monooxygenase, were subjected to three rounds of in vitro evolution using error-prone polymerase chain reaction with a view to improving the rate of styrene oxide and indene oxide formation. Improvements in styrene monooxygenase activity were monitored using an indole to indigo conversion assay. Each round of random mutagenesis generated variants improved in indigo formation with third round variants improved nine- to 12-fold over the wild type enzyme. Each round of in vitro evolution resulted in two to three amino acid substitutions in styrene monooxygenase. While the majority of mutations occurred in styA (oxygenase), mutations were also observed in styB (reductase). A mutation resulting in the substitution of valine with isoleucine at amino acid residue 303 occurred near the styrene and flavin adenine dinucleotide binding site of styrene monooxygenase. One mutation caused a shift in the reading frame in styA and resulted in a StyA variant that is 19 amino acids longer than the wild-type protein. Whole cells expressing the best styrene monooxygenase variants (round 3) exhibited eight- and 12-fold improvements in styrene and indene oxidation rates compared to the wild-type enzyme. In all cases, a single enantiomer, (S)-styrene oxide, was formed from styrene while (1S,2R)-indene oxide was the predominant enantiomer (e.e. 97%) formed from indene. The average yield of styrene oxide and indene oxide from their respective alkene substrates was 65% and 90%, respectively.",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "In vitro evolution of styrene monooxygenase from Pseudomonas putida CA-3 for improved epoxide synthesis",
volume = "85",
number = "4",
pages = "995-1004",
doi = "10.1007/s00253-009-2096-3"
}

Gursky, L. J., Nikodinović-Runić, J., Feenstra, K. A.,& O'Connor, K. E.. (2010). In vitro evolution of styrene monooxygenase from Pseudomonas putida CA-3 for improved epoxide synthesis. in Applied Microbiology and Biotechnology
Springer, New York., 85(4), 995-1004.
https://doi.org/10.1007/s00253-009-2096-3

Gursky LJ, Nikodinović-Runić J, Feenstra KA, O'Connor KE. In vitro evolution of styrene monooxygenase from Pseudomonas putida CA-3 for improved epoxide synthesis. in Applied Microbiology and Biotechnology. 2010;85(4):995-1004.
doi:10.1007/s00253-009-2096-3 .

Gursky, Lucas J., Nikodinović-Runić, Jasmina, Feenstra, K. Anton, O'Connor, Kevin E., "In vitro evolution of styrene monooxygenase from Pseudomonas putida CA-3 for improved epoxide synthesis" in Applied Microbiology and Biotechnology, 85, no. 4 (2010):995-1004,
https://doi.org/10.1007/s00253-009-2096-3 . .

TY  - JOUR
AU  - Nikodinović-Runić, Jasmina
AU  - Flanagan, Michelle
AU  - Hume, Aisling R.
AU  - Cagney, Gerard
AU  - O'Connor, Kevin E.
PY  - 2009
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1022
AB  - Pseudomonas putida CA-3 is a styrene-degrading bacterium capable of accumulating medium-chain-length polyhydroxyalkanoate (mcIPHA) when exposed to limiting concentrations of a nitrogen source in the growth medium. Using shotgun proteomics we analysed global proteome expression in P. putida CA-3 supplied with styrene as the sole carbon and energy source under N-limiting (condition permissive for mclPHA synthesis) and non-limiting (condition non-permissive for mcIPHA accumulation) growth conditions in order to provide insight into the molecular response of P. putida CA-3 to limitation of nitrogen when grown on styrene. A total of 1761 proteins were identified with high confidence and the detected proteins could be assigned to functional groups including styrene degradation, energy, nucleotide metabolism, protein synthesis, transport, stress response and motility. Proteins involved in the upper and lower styrene degradation pathway were expressed throughout the 48 h growth period under both nitrogen limitation and excess. Proteins involved in polyhydroxyalkanoate (PHA) biosynthesis, nitrogen assimilation and amino acid transport, and outer membrane proteins were upregulated under nitrogen limitation. PHA accumulation and biosynthesis were only expressed under nitrogen limitation. Nitrogen assimilation proteins were detected on average at twofold higher amounts under nitrogen limitation. Expression of the branched-chain amino acid ABC transporter was up to 16-fold higher under nitrogen-limiting conditions. Branched chain amino acid uptake by nitrogen-limited cultures was also higher than that by non-limited cultures. Outer membrane lipoproteins were expressed at twofold higher levels under nitrogen limitation. This was confirmed by Western blotting (immunochemical detection) of cells grown under nitrogen limitation. Our study provides the first global description of protein expression changes during growth of any organism on styrene and accumulating mcIPHA (nitrogen-limited growth).
PB  - Soc General Microbiology, Reading
T2  - Microbiology, SGM / Society for General Microbiology
T1  - Analysis of the Pseudomonas putida CA-3 proteome during growth on styrene under nitrogen-limiting and non-limiting conditions
VL  - 155
SP  - 3348
EP  - 3361
DO  - 10.1099/mic.0.031153-0
ER  - 

@article{
author = "Nikodinović-Runić, Jasmina and Flanagan, Michelle and Hume, Aisling R. and Cagney, Gerard and O'Connor, Kevin E.",
year = "2009",
abstract = "Pseudomonas putida CA-3 is a styrene-degrading bacterium capable of accumulating medium-chain-length polyhydroxyalkanoate (mcIPHA) when exposed to limiting concentrations of a nitrogen source in the growth medium. Using shotgun proteomics we analysed global proteome expression in P. putida CA-3 supplied with styrene as the sole carbon and energy source under N-limiting (condition permissive for mclPHA synthesis) and non-limiting (condition non-permissive for mcIPHA accumulation) growth conditions in order to provide insight into the molecular response of P. putida CA-3 to limitation of nitrogen when grown on styrene. A total of 1761 proteins were identified with high confidence and the detected proteins could be assigned to functional groups including styrene degradation, energy, nucleotide metabolism, protein synthesis, transport, stress response and motility. Proteins involved in the upper and lower styrene degradation pathway were expressed throughout the 48 h growth period under both nitrogen limitation and excess. Proteins involved in polyhydroxyalkanoate (PHA) biosynthesis, nitrogen assimilation and amino acid transport, and outer membrane proteins were upregulated under nitrogen limitation. PHA accumulation and biosynthesis were only expressed under nitrogen limitation. Nitrogen assimilation proteins were detected on average at twofold higher amounts under nitrogen limitation. Expression of the branched-chain amino acid ABC transporter was up to 16-fold higher under nitrogen-limiting conditions. Branched chain amino acid uptake by nitrogen-limited cultures was also higher than that by non-limited cultures. Outer membrane lipoproteins were expressed at twofold higher levels under nitrogen limitation. This was confirmed by Western blotting (immunochemical detection) of cells grown under nitrogen limitation. Our study provides the first global description of protein expression changes during growth of any organism on styrene and accumulating mcIPHA (nitrogen-limited growth).",
publisher = "Soc General Microbiology, Reading",
journal = "Microbiology, SGM / Society for General Microbiology",
title = "Analysis of the Pseudomonas putida CA-3 proteome during growth on styrene under nitrogen-limiting and non-limiting conditions",
volume = "155",
pages = "3348-3361",
doi = "10.1099/mic.0.031153-0"
}

Nikodinović-Runić, J., Flanagan, M., Hume, A. R., Cagney, G.,& O'Connor, K. E.. (2009). Analysis of the Pseudomonas putida CA-3 proteome during growth on styrene under nitrogen-limiting and non-limiting conditions. in Microbiology, SGM / Society for General Microbiology
Soc General Microbiology, Reading., 155, 3348-3361.
https://doi.org/10.1099/mic.0.031153-0

Nikodinović-Runić J, Flanagan M, Hume AR, Cagney G, O'Connor KE. Analysis of the Pseudomonas putida CA-3 proteome during growth on styrene under nitrogen-limiting and non-limiting conditions. in Microbiology, SGM / Society for General Microbiology. 2009;155:3348-3361.
doi:10.1099/mic.0.031153-0 .

Nikodinović-Runić, Jasmina, Flanagan, Michelle, Hume, Aisling R., Cagney, Gerard, O'Connor, Kevin E., "Analysis of the Pseudomonas putida CA-3 proteome during growth on styrene under nitrogen-limiting and non-limiting conditions" in Microbiology, SGM / Society for General Microbiology, 155 (2009):3348-3361,
https://doi.org/10.1099/mic.0.031153-0 . .