TY  - JOUR
AU  - Šokarda-Slavić, Marinela
AU  - Pešić, Milja
AU  - Vujčić, Zoran
AU  - Božić, Nataša
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2061
AB  - alpha-Amylase from Bacillus licheniformis ATCC 9945a (BliAmy) was proven to be very efficient in hydrolysis of granular starch below the temperature of gelatinization. By applying two-stage feeding strategy to achieve high-cell-density cultivation of Escherichia coli and extracellular production of BliAmy, total of 250.5 U/mL (i.e. 0.7 g/L) of enzyme was obtained. Thermostability of amylase was exploited to simplify purification. The hydrolysis of concentrated raw starch was optimized using response surface methodology. Regardless of raw starch concentration tested (20, 25, 30 %), BliAmy was very effective, achieving the final hydrolysis degree of 91 % for the hydrolysis of 30 % starch suspension after 24 h. The major A-type crystalline structure and amorphous domains of the starch granule were degraded at the same rates, while amylose-lipid complexes were not degraded. BliAmy presents interesting performances on highly concentrated solid starch and could be of value for starch-consuming industries while response surface methodology (RSM) could be efficiently applied for the optimization of the hydrolysis.
PB  - Springer, New York
T2  - Applied Microbiology and Biotechnology
T1  - Overcoming hydrolysis of raw corn starch under industrial conditions with Bacillus licheniformis ATCC 9945a alpha-amylase
VL  - 100
IS  - 6
SP  - 2709
EP  - 2719
DO  - 10.1007/s00253-015-7101-4
ER  - 

@article{
author = "Šokarda-Slavić, Marinela and Pešić, Milja and Vujčić, Zoran and Božić, Nataša",
year = "2016",
abstract = "alpha-Amylase from Bacillus licheniformis ATCC 9945a (BliAmy) was proven to be very efficient in hydrolysis of granular starch below the temperature of gelatinization. By applying two-stage feeding strategy to achieve high-cell-density cultivation of Escherichia coli and extracellular production of BliAmy, total of 250.5 U/mL (i.e. 0.7 g/L) of enzyme was obtained. Thermostability of amylase was exploited to simplify purification. The hydrolysis of concentrated raw starch was optimized using response surface methodology. Regardless of raw starch concentration tested (20, 25, 30 %), BliAmy was very effective, achieving the final hydrolysis degree of 91 % for the hydrolysis of 30 % starch suspension after 24 h. The major A-type crystalline structure and amorphous domains of the starch granule were degraded at the same rates, while amylose-lipid complexes were not degraded. BliAmy presents interesting performances on highly concentrated solid starch and could be of value for starch-consuming industries while response surface methodology (RSM) could be efficiently applied for the optimization of the hydrolysis.",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "Overcoming hydrolysis of raw corn starch under industrial conditions with Bacillus licheniformis ATCC 9945a alpha-amylase",
volume = "100",
number = "6",
pages = "2709-2719",
doi = "10.1007/s00253-015-7101-4"
}

Šokarda-Slavić, M., Pešić, M., Vujčić, Z.,& Božić, N.. (2016). Overcoming hydrolysis of raw corn starch under industrial conditions with Bacillus licheniformis ATCC 9945a alpha-amylase. in Applied Microbiology and Biotechnology
Springer, New York., 100(6), 2709-2719.
https://doi.org/10.1007/s00253-015-7101-4

Šokarda-Slavić M, Pešić M, Vujčić Z, Božić N. Overcoming hydrolysis of raw corn starch under industrial conditions with Bacillus licheniformis ATCC 9945a alpha-amylase. in Applied Microbiology and Biotechnology. 2016;100(6):2709-2719.
doi:10.1007/s00253-015-7101-4 .

Šokarda-Slavić, Marinela, Pešić, Milja, Vujčić, Zoran, Božić, Nataša, "Overcoming hydrolysis of raw corn starch under industrial conditions with Bacillus licheniformis ATCC 9945a alpha-amylase" in Applied Microbiology and Biotechnology, 100, no. 6 (2016):2709-2719,
https://doi.org/10.1007/s00253-015-7101-4 . .

TY  - DATA
AU  - Šokarda-Slavić, Marinela
AU  - Pešić, Milja
AU  - Vujčić, Zoran
AU  - Božić, Nataša
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3588
PB  - Springer, New York
T2  - Applied Microbiology and Biotechnology
T1  - Supplementary material for the article: Šokarda Slavić, M.; Pešić, M.; Vujčić, Z.; Božić, N. Overcoming Hydrolysis of Raw Corn  Starch under Industrial Conditions with Bacillus Licheniformis ATCC 9945a α-Amylase. Applied Microbiology and Biotechnology 2016, 100 (6), 2709–2719. https://doi.org/10.1007/s00253-015-7101-4
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3588
ER  - 

@misc{
author = "Šokarda-Slavić, Marinela and Pešić, Milja and Vujčić, Zoran and Božić, Nataša",
year = "2016",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "Supplementary material for the article: Šokarda Slavić, M.; Pešić, M.; Vujčić, Z.; Božić, N. Overcoming Hydrolysis of Raw Corn  Starch under Industrial Conditions with Bacillus Licheniformis ATCC 9945a α-Amylase. Applied Microbiology and Biotechnology 2016, 100 (6), 2709–2719. https://doi.org/10.1007/s00253-015-7101-4",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3588"
}

Šokarda-Slavić, M., Pešić, M., Vujčić, Z.,& Božić, N.. (2016). Supplementary material for the article: Šokarda Slavić, M.; Pešić, M.; Vujčić, Z.; Božić, N. Overcoming Hydrolysis of Raw Corn  Starch under Industrial Conditions with Bacillus Licheniformis ATCC 9945a α-Amylase. Applied Microbiology and Biotechnology 2016, 100 (6), 2709–2719. https://doi.org/10.1007/s00253-015-7101-4. in Applied Microbiology and Biotechnology
Springer, New York..
https://hdl.handle.net/21.15107/rcub_cherry_3588

Šokarda-Slavić M, Pešić M, Vujčić Z, Božić N. Supplementary material for the article: Šokarda Slavić, M.; Pešić, M.; Vujčić, Z.; Božić, N. Overcoming Hydrolysis of Raw Corn  Starch under Industrial Conditions with Bacillus Licheniformis ATCC 9945a α-Amylase. Applied Microbiology and Biotechnology 2016, 100 (6), 2709–2719. https://doi.org/10.1007/s00253-015-7101-4. in Applied Microbiology and Biotechnology. 2016;.
https://hdl.handle.net/21.15107/rcub_cherry_3588 .

Šokarda-Slavić, Marinela, Pešić, Milja, Vujčić, Zoran, Božić, Nataša, "Supplementary material for the article: Šokarda Slavić, M.; Pešić, M.; Vujčić, Z.; Božić, N. Overcoming Hydrolysis of Raw Corn  Starch under Industrial Conditions with Bacillus Licheniformis ATCC 9945a α-Amylase. Applied Microbiology and Biotechnology 2016, 100 (6), 2709–2719. https://doi.org/10.1007/s00253-015-7101-4" in Applied Microbiology and Biotechnology (2016),
https://hdl.handle.net/21.15107/rcub_cherry_3588 .

TY  - JOUR
AU  - Pešić, Milja
AU  - Božić, Nataša
AU  - Lopez, Carmen
AU  - Lončar, Nikola L.
AU  - Alvaro, Gregorio
AU  - Vujčić, Zoran
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1844
AB  - Chloroperoxidase from Caldariomyces fumago (CPO, EC 1.11.1.10) is one of the most interesting enzymes from the group of heme peroxidases and has been extensively applied in synthetic processes. Nevertheless, the practical application of CPO is limited due to its very low operational stability, especially in the presence of peroxidative compounds. For this reason, effect of chemical modifications of CPO in the stability of the enzyme was studied. Side-chain selective modifications of amino groups of Lys residues, and carboxyl groups of Asp and Glu residues, as well as crosslinking and periodate oxidation of sugar moiety were carried out. The stability of modified CPOs was evaluated at elevated pH and temperature, and in the presence of tert-butyl hydroperoxide. Effect of modification of CPO on the performance of the reaction of Cbz-ethanolamine oxidation was studied as well. Those modifications that involved carboxyl groups via carbodiimide coupled method and the periodate oxidation of the sugar moiety produced better catalysts than native CPO in terms of stability and activity at elevated pH values and temperatures. (C) 2014 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Process Biochemistry
T1  - Chemical modification of chloroperoxidase for enhanced stability and activity
VL  - 49
IS  - 9
SP  - 1472
EP  - 1479
DO  - 10.1016/j.procbio.2014.05.025
ER  - 

@article{
author = "Pešić, Milja and Božić, Nataša and Lopez, Carmen and Lončar, Nikola L. and Alvaro, Gregorio and Vujčić, Zoran",
year = "2014",
abstract = "Chloroperoxidase from Caldariomyces fumago (CPO, EC 1.11.1.10) is one of the most interesting enzymes from the group of heme peroxidases and has been extensively applied in synthetic processes. Nevertheless, the practical application of CPO is limited due to its very low operational stability, especially in the presence of peroxidative compounds. For this reason, effect of chemical modifications of CPO in the stability of the enzyme was studied. Side-chain selective modifications of amino groups of Lys residues, and carboxyl groups of Asp and Glu residues, as well as crosslinking and periodate oxidation of sugar moiety were carried out. The stability of modified CPOs was evaluated at elevated pH and temperature, and in the presence of tert-butyl hydroperoxide. Effect of modification of CPO on the performance of the reaction of Cbz-ethanolamine oxidation was studied as well. Those modifications that involved carboxyl groups via carbodiimide coupled method and the periodate oxidation of the sugar moiety produced better catalysts than native CPO in terms of stability and activity at elevated pH values and temperatures. (C) 2014 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Process Biochemistry",
title = "Chemical modification of chloroperoxidase for enhanced stability and activity",
volume = "49",
number = "9",
pages = "1472-1479",
doi = "10.1016/j.procbio.2014.05.025"
}

Pešić, M., Božić, N., Lopez, C., Lončar, N. L., Alvaro, G.,& Vujčić, Z.. (2014). Chemical modification of chloroperoxidase for enhanced stability and activity. in Process Biochemistry
Elsevier Sci Ltd, Oxford., 49(9), 1472-1479.
https://doi.org/10.1016/j.procbio.2014.05.025

Pešić M, Božić N, Lopez C, Lončar NL, Alvaro G, Vujčić Z. Chemical modification of chloroperoxidase for enhanced stability and activity. in Process Biochemistry. 2014;49(9):1472-1479.
doi:10.1016/j.procbio.2014.05.025 .

Pešić, Milja, Božić, Nataša, Lopez, Carmen, Lončar, Nikola L., Alvaro, Gregorio, Vujčić, Zoran, "Chemical modification of chloroperoxidase for enhanced stability and activity" in Process Biochemistry, 49, no. 9 (2014):1472-1479,
https://doi.org/10.1016/j.procbio.2014.05.025 . .

TY  - JOUR
AU  - Pešić, Milja
AU  - Božić, Nataša
AU  - Lopez, Carmen
AU  - Lončar, Nikola L.
AU  - Alvaro, Gregorio
AU  - Vujčić, Zoran
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3743
AB  - Chloroperoxidase from Caldariomyces fumago (CPO, EC 1.11.1.10) is one of the most interesting enzymes from the group of heme peroxidases and has been extensively applied in synthetic processes. Nevertheless, the practical application of CPO is limited due to its very low operational stability, especially in the presence of peroxidative compounds. For this reason, effect of chemical modifications of CPO in the stability of the enzyme was studied. Side-chain selective modifications of amino groups of Lys residues, and carboxyl groups of Asp and Glu residues, as well as crosslinking and periodate oxidation of sugar moiety were carried out. The stability of modified CPOs was evaluated at elevated pH and temperature, and in the presence of tert-butyl hydroperoxide. Effect of modification of CPO on the performance of the reaction of Cbz-ethanolamine oxidation was studied as well. Those modifications that involved carboxyl groups via carbodiimide coupled method and the periodate oxidation of the sugar moiety produced better catalysts than native CPO in terms of stability and activity at elevated pH values and temperatures. (C) 2014 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Process Biochemistry
T1  - Chemical modification of chloroperoxidase for enhanced stability and activity
VL  - 49
IS  - 9
SP  - 1472
EP  - 1479
DO  - 10.1016/j.procbio.2014.05.025
ER  - 

@article{
author = "Pešić, Milja and Božić, Nataša and Lopez, Carmen and Lončar, Nikola L. and Alvaro, Gregorio and Vujčić, Zoran",
year = "2014",
abstract = "Chloroperoxidase from Caldariomyces fumago (CPO, EC 1.11.1.10) is one of the most interesting enzymes from the group of heme peroxidases and has been extensively applied in synthetic processes. Nevertheless, the practical application of CPO is limited due to its very low operational stability, especially in the presence of peroxidative compounds. For this reason, effect of chemical modifications of CPO in the stability of the enzyme was studied. Side-chain selective modifications of amino groups of Lys residues, and carboxyl groups of Asp and Glu residues, as well as crosslinking and periodate oxidation of sugar moiety were carried out. The stability of modified CPOs was evaluated at elevated pH and temperature, and in the presence of tert-butyl hydroperoxide. Effect of modification of CPO on the performance of the reaction of Cbz-ethanolamine oxidation was studied as well. Those modifications that involved carboxyl groups via carbodiimide coupled method and the periodate oxidation of the sugar moiety produced better catalysts than native CPO in terms of stability and activity at elevated pH values and temperatures. (C) 2014 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Process Biochemistry",
title = "Chemical modification of chloroperoxidase for enhanced stability and activity",
volume = "49",
number = "9",
pages = "1472-1479",
doi = "10.1016/j.procbio.2014.05.025"
}

Pešić, M., Božić, N., Lopez, C., Lončar, N. L., Alvaro, G.,& Vujčić, Z.. (2014). Chemical modification of chloroperoxidase for enhanced stability and activity. in Process Biochemistry
Elsevier Sci Ltd, Oxford., 49(9), 1472-1479.
https://doi.org/10.1016/j.procbio.2014.05.025

Pešić M, Božić N, Lopez C, Lončar NL, Alvaro G, Vujčić Z. Chemical modification of chloroperoxidase for enhanced stability and activity. in Process Biochemistry. 2014;49(9):1472-1479.
doi:10.1016/j.procbio.2014.05.025 .

Pešić, Milja, Božić, Nataša, Lopez, Carmen, Lončar, Nikola L., Alvaro, Gregorio, Vujčić, Zoran, "Chemical modification of chloroperoxidase for enhanced stability and activity" in Process Biochemistry, 49, no. 9 (2014):1472-1479,
https://doi.org/10.1016/j.procbio.2014.05.025 . .