TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Božić, Nataša
AU  - Lopez-Santin, Josep
AU  - Vujčić, Zoran
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1431
AB  - One hundred wild type strains of Bacillus sp. were isolated from industrial and agricultural soil across Serbia and screened for laccase activity. Three strains showed high laccase activity temperature optimum of 65 and 80 degrees C towards ABTS. A new laccase gene from the strain with highest temperature optimum, namely Bacillus amyloliquefaciens 12B was cloned and expressed in Escherichia coli. Recombinant laccase degraded dye Reactive blue 52 at pH 7.0 and pH 4.0 and at elevated temperature, while fungal laccases was unable to act on this substrate at pH higher than 4.0 and was quickly inactivated at temperatures higher than 45 degrees C. Degradation of dye was monitored by HPLC-DAD and resulting precipitate was analyzed by FTIR spectroscopy. Single product peak without chromophore was detected in solution, while water insoluble aggregate, presumably dye polymer is formed retaining blue color. (C) 2013 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Bioresource Technology
T1  - Bacillus amyloliquefaciens laccase - From soil bacteria to recombinant enzyme for wastewater decolorization
VL  - 147
SP  - 177
EP  - 183
DO  - 10.1016/j.biortech.2013.08.056
ER  - 

@article{
author = "Lončar, Nikola L. and Božić, Nataša and Lopez-Santin, Josep and Vujčić, Zoran",
year = "2013",
abstract = "One hundred wild type strains of Bacillus sp. were isolated from industrial and agricultural soil across Serbia and screened for laccase activity. Three strains showed high laccase activity temperature optimum of 65 and 80 degrees C towards ABTS. A new laccase gene from the strain with highest temperature optimum, namely Bacillus amyloliquefaciens 12B was cloned and expressed in Escherichia coli. Recombinant laccase degraded dye Reactive blue 52 at pH 7.0 and pH 4.0 and at elevated temperature, while fungal laccases was unable to act on this substrate at pH higher than 4.0 and was quickly inactivated at temperatures higher than 45 degrees C. Degradation of dye was monitored by HPLC-DAD and resulting precipitate was analyzed by FTIR spectroscopy. Single product peak without chromophore was detected in solution, while water insoluble aggregate, presumably dye polymer is formed retaining blue color. (C) 2013 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Bioresource Technology",
title = "Bacillus amyloliquefaciens laccase - From soil bacteria to recombinant enzyme for wastewater decolorization",
volume = "147",
pages = "177-183",
doi = "10.1016/j.biortech.2013.08.056"
}

Lončar, N. L., Božić, N., Lopez-Santin, J.,& Vujčić, Z.. (2013). Bacillus amyloliquefaciens laccase - From soil bacteria to recombinant enzyme for wastewater decolorization. in Bioresource Technology
Elsevier Sci Ltd, Oxford., 147, 177-183.
https://doi.org/10.1016/j.biortech.2013.08.056

Lončar NL, Božić N, Lopez-Santin J, Vujčić Z. Bacillus amyloliquefaciens laccase - From soil bacteria to recombinant enzyme for wastewater decolorization. in Bioresource Technology. 2013;147:177-183.
doi:10.1016/j.biortech.2013.08.056 .

Lončar, Nikola L., Božić, Nataša, Lopez-Santin, Josep, Vujčić, Zoran, "Bacillus amyloliquefaciens laccase - From soil bacteria to recombinant enzyme for wastewater decolorization" in Bioresource Technology, 147 (2013):177-183,
https://doi.org/10.1016/j.biortech.2013.08.056 . .

TY  - JOUR
AU  - Božić, Nataša
AU  - Puertas, Juan-Miguel
AU  - Lončar, Nikola L.
AU  - Sans Duran, Cristina
AU  - Lopez-Santin, Josep
AU  - Vujčić, Zoran
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1638
AB  - In this study, a new approach for extracellular production of recombinant alpha-amylase in Escherichia coli was investigated. A gene encoding a highly efficient raw-starch-digesting alpha-amylase from Bacillus licheniformis ATCC 9945a was cloned and expressed in E. coli. The gene encoding mature alpha-amylase was cloned into the pDAss expression vector, and secretion of the gene product was regulated by fusion to the signal peptide of DsbA, a well-characterized E. coli periplasmic protein. E. coli BL21 (DE3) carrying pDAss vector containing amylase gene had approximately 2.5-fold higher volumetric enzyme productivity than the natural system. The recombinant enzyme showed higher efficiency for digesting diverse raw starches when compared with the native enzyme and was similar to commercial alpha-amylase in its ability to hydrolyze raw starches. The properties of the recombinant enzyme demonstrate the potential of the DsbA signal peptide approach for the secretory production of the fully active, industrially important recombinant enzyme. (C) 2013 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Process Biochemistry
T1  - The DsbA signal peptide-mediated secretion of a highly efficient raw-starch-digesting, recombinant alpha-amylase from Bacillus licheniformis ATCC 9945a
VL  - 48
IS  - 3
SP  - 438
EP  - 442
DO  - 10.1016/j.procbio.2013.01.016
ER  - 

@article{
author = "Božić, Nataša and Puertas, Juan-Miguel and Lončar, Nikola L. and Sans Duran, Cristina and Lopez-Santin, Josep and Vujčić, Zoran",
year = "2013",
abstract = "In this study, a new approach for extracellular production of recombinant alpha-amylase in Escherichia coli was investigated. A gene encoding a highly efficient raw-starch-digesting alpha-amylase from Bacillus licheniformis ATCC 9945a was cloned and expressed in E. coli. The gene encoding mature alpha-amylase was cloned into the pDAss expression vector, and secretion of the gene product was regulated by fusion to the signal peptide of DsbA, a well-characterized E. coli periplasmic protein. E. coli BL21 (DE3) carrying pDAss vector containing amylase gene had approximately 2.5-fold higher volumetric enzyme productivity than the natural system. The recombinant enzyme showed higher efficiency for digesting diverse raw starches when compared with the native enzyme and was similar to commercial alpha-amylase in its ability to hydrolyze raw starches. The properties of the recombinant enzyme demonstrate the potential of the DsbA signal peptide approach for the secretory production of the fully active, industrially important recombinant enzyme. (C) 2013 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Process Biochemistry",
title = "The DsbA signal peptide-mediated secretion of a highly efficient raw-starch-digesting, recombinant alpha-amylase from Bacillus licheniformis ATCC 9945a",
volume = "48",
number = "3",
pages = "438-442",
doi = "10.1016/j.procbio.2013.01.016"
}

Božić, N., Puertas, J., Lončar, N. L., Sans Duran, C., Lopez-Santin, J.,& Vujčić, Z.. (2013). The DsbA signal peptide-mediated secretion of a highly efficient raw-starch-digesting, recombinant alpha-amylase from Bacillus licheniformis ATCC 9945a. in Process Biochemistry
Elsevier Sci Ltd, Oxford., 48(3), 438-442.
https://doi.org/10.1016/j.procbio.2013.01.016

Božić N, Puertas J, Lončar NL, Sans Duran C, Lopez-Santin J, Vujčić Z. The DsbA signal peptide-mediated secretion of a highly efficient raw-starch-digesting, recombinant alpha-amylase from Bacillus licheniformis ATCC 9945a. in Process Biochemistry. 2013;48(3):438-442.
doi:10.1016/j.procbio.2013.01.016 .

Božić, Nataša, Puertas, Juan-Miguel, Lončar, Nikola L., Sans Duran, Cristina, Lopez-Santin, Josep, Vujčić, Zoran, "The DsbA signal peptide-mediated secretion of a highly efficient raw-starch-digesting, recombinant alpha-amylase from Bacillus licheniformis ATCC 9945a" in Process Biochemistry, 48, no. 3 (2013):438-442,
https://doi.org/10.1016/j.procbio.2013.01.016 . .

TY  - JOUR
AU  - Božić, Nataša
AU  - Ruiz, Jordi
AU  - Lopez-Santin, Josep
AU  - Vujčić, Zoran
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1187
AB  - Cell growth and the level of alpha-amylase in response to the carbon and nitrogen sources used for the growth of the strain Bacillus subtilis IP 5832 were examined. Based on the amylase productivity level in shake flask cultures after 24 hours of growth, the growth medium containing starch and peptone was selected as the best medium. Amylase production was greatly reduced when glutamate or citrate as sources of carbon were used. Experiments performed at different initial concentrations of starch showed that although the strain grew well with all the starch concentration used, 0.5 % starch was necessary for maximum alpha-amylase production, inducing 1.55 IU mL(-1) of amylase to be secreted after 8 h of cultivation in shaking flasks. During the batch fermentation of B. subtilis IP 5832 strain in 2 L laboratory fermenter, a 60 % higher activity (2.5 IU mL(-1)) was obtained. The production of the enzyme was directly related to the growth of the strain. Maximum enzyme activity was obtained at the beginning of the stationary growth phase.
AB  - Ćelijski rast i nivoi α-amilaze nakon gajenja Bacillus subtilis IP 5832 ispitivani su u zavisnosti od različitih izvora ugljenika i azota korišćenih u podlozi. Na osnovu produktivnosti amilaze nakon dvadesetčetvoročasovnog gajenja kulture u erlenmajerima sa mešanjem pokazano je da je najbolja hranljiva podloga ona koja sadrži skrob i pepton. Kada su glutamat ili citrat korišćeni kao izvori ugljenika produkcija enzima je bila značajno redukovana. Eksperimentima u kojima je varirana inicijalna koncentracija skroba pokazano je da je, iako soj dobro raste na svim korišćenim koncentracijama, 0,5 % skrob neophodan za maksimalnu produkciju enzima, indukujući sekreciju 1,55 IU mL-1 amilaze nakon 8 sati gajenja kulture u erlenmajerima sa mešanjem. Tokom šaržne fermentacije B. subtilis IP 5832 soja u laboratorijskom fermentoru od 2 L dobijeno je 60 % više aktivnosti enzima (2,5 IU mL -1). Produkcija enzima je bila direktno vezana za rast mikroorganizma. Maksimalna enzimska aktivnost dobijena je na početku stacionarne faze rasta.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Optimization of the growth and alpha-amylase production of Bacillus subtilis IP 5832 in shake flask and laboratory fermenter batch cultures
T1  - Optimizacija rasta i produkcije α-amilaze Bacillus subtilis IP 5832 u šaržnim kulturama u erlenmajeru i laboratorijskom fermentoru
VL  - 76
IS  - 7
SP  - 965
EP  - 972
DO  - 10.2298/JSC101010098B
ER  - 

@article{
author = "Božić, Nataša and Ruiz, Jordi and Lopez-Santin, Josep and Vujčić, Zoran",
year = "2011",
abstract = "Cell growth and the level of alpha-amylase in response to the carbon and nitrogen sources used for the growth of the strain Bacillus subtilis IP 5832 were examined. Based on the amylase productivity level in shake flask cultures after 24 hours of growth, the growth medium containing starch and peptone was selected as the best medium. Amylase production was greatly reduced when glutamate or citrate as sources of carbon were used. Experiments performed at different initial concentrations of starch showed that although the strain grew well with all the starch concentration used, 0.5 % starch was necessary for maximum alpha-amylase production, inducing 1.55 IU mL(-1) of amylase to be secreted after 8 h of cultivation in shaking flasks. During the batch fermentation of B. subtilis IP 5832 strain in 2 L laboratory fermenter, a 60 % higher activity (2.5 IU mL(-1)) was obtained. The production of the enzyme was directly related to the growth of the strain. Maximum enzyme activity was obtained at the beginning of the stationary growth phase., Ćelijski rast i nivoi α-amilaze nakon gajenja Bacillus subtilis IP 5832 ispitivani su u zavisnosti od različitih izvora ugljenika i azota korišćenih u podlozi. Na osnovu produktivnosti amilaze nakon dvadesetčetvoročasovnog gajenja kulture u erlenmajerima sa mešanjem pokazano je da je najbolja hranljiva podloga ona koja sadrži skrob i pepton. Kada su glutamat ili citrat korišćeni kao izvori ugljenika produkcija enzima je bila značajno redukovana. Eksperimentima u kojima je varirana inicijalna koncentracija skroba pokazano je da je, iako soj dobro raste na svim korišćenim koncentracijama, 0,5 % skrob neophodan za maksimalnu produkciju enzima, indukujući sekreciju 1,55 IU mL-1 amilaze nakon 8 sati gajenja kulture u erlenmajerima sa mešanjem. Tokom šaržne fermentacije B. subtilis IP 5832 soja u laboratorijskom fermentoru od 2 L dobijeno je 60 % više aktivnosti enzima (2,5 IU mL -1). Produkcija enzima je bila direktno vezana za rast mikroorganizma. Maksimalna enzimska aktivnost dobijena je na početku stacionarne faze rasta.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Optimization of the growth and alpha-amylase production of Bacillus subtilis IP 5832 in shake flask and laboratory fermenter batch cultures, Optimizacija rasta i produkcije α-amilaze Bacillus subtilis IP 5832 u šaržnim kulturama u erlenmajeru i laboratorijskom fermentoru",
volume = "76",
number = "7",
pages = "965-972",
doi = "10.2298/JSC101010098B"
}

Božić, N., Ruiz, J., Lopez-Santin, J.,& Vujčić, Z.. (2011). Optimization of the growth and alpha-amylase production of Bacillus subtilis IP 5832 in shake flask and laboratory fermenter batch cultures. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 76(7), 965-972.
https://doi.org/10.2298/JSC101010098B

Božić N, Ruiz J, Lopez-Santin J, Vujčić Z. Optimization of the growth and alpha-amylase production of Bacillus subtilis IP 5832 in shake flask and laboratory fermenter batch cultures. in Journal of the Serbian Chemical Society. 2011;76(7):965-972.
doi:10.2298/JSC101010098B .

Božić, Nataša, Ruiz, Jordi, Lopez-Santin, Josep, Vujčić, Zoran, "Optimization of the growth and alpha-amylase production of Bacillus subtilis IP 5832 in shake flask and laboratory fermenter batch cultures" in Journal of the Serbian Chemical Society, 76, no. 7 (2011):965-972,
https://doi.org/10.2298/JSC101010098B . .

TY  - JOUR
AU  - Božić, Nataša
AU  - Ruiz, Jordi
AU  - Lopez-Santin, Josep
AU  - Vujčić, Zoran
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1151
AB  - Highly efficient raw starch digesting alpha-amylase was produced after 24 h of batch fermentation of Bacillus licheniformis ATCC 9945a in laboratory bioreactor at 37 degrees C. The enzyme was purified by gel filtration chromatographies with 6-fold increase of specific activity and 38% recovery and showed a molecular mass of 31 kDa by SDS-PAGE. The purified enzyme had an optimum pH of 6.5 and optimum temperature of 90 degrees C. The purified alpha-amylase in the presence of CaCl(2) retained 55% of its activity after 6 h of incubation at 70 degrees C. Co(2+), Ni(2+) and Ca(2+) slightly stimulated, while Hg(2+) completely inhibited alpha-amylase activity. Hydrolysis rates of raw triticale, wheat, potato, horseradish and corn starches, at 1% concentration were 63, 60, 59, 52 and 37%, respectively, in a period of 4 h. The properties of the purified enzyme proved its high efficacy for digesting diverse raw starches below gelatinization temperature and, hence, its potential commercial value to use as an industrial enzyme. (C) 2010 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Sa, Lausanne
T2  - Biochemical Engineering Journal
T1  - Production and properties of the highly efficient raw starch digesting alpha-amylase from a Bacillus licheniformis ATCC 9945a
VL  - 53
IS  - 2
SP  - 203
EP  - 209
DO  - 10.1016/j.bej.2010.10.014
ER  - 

@article{
author = "Božić, Nataša and Ruiz, Jordi and Lopez-Santin, Josep and Vujčić, Zoran",
year = "2011",
abstract = "Highly efficient raw starch digesting alpha-amylase was produced after 24 h of batch fermentation of Bacillus licheniformis ATCC 9945a in laboratory bioreactor at 37 degrees C. The enzyme was purified by gel filtration chromatographies with 6-fold increase of specific activity and 38% recovery and showed a molecular mass of 31 kDa by SDS-PAGE. The purified enzyme had an optimum pH of 6.5 and optimum temperature of 90 degrees C. The purified alpha-amylase in the presence of CaCl(2) retained 55% of its activity after 6 h of incubation at 70 degrees C. Co(2+), Ni(2+) and Ca(2+) slightly stimulated, while Hg(2+) completely inhibited alpha-amylase activity. Hydrolysis rates of raw triticale, wheat, potato, horseradish and corn starches, at 1% concentration were 63, 60, 59, 52 and 37%, respectively, in a period of 4 h. The properties of the purified enzyme proved its high efficacy for digesting diverse raw starches below gelatinization temperature and, hence, its potential commercial value to use as an industrial enzyme. (C) 2010 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Sa, Lausanne",
journal = "Biochemical Engineering Journal",
title = "Production and properties of the highly efficient raw starch digesting alpha-amylase from a Bacillus licheniformis ATCC 9945a",
volume = "53",
number = "2",
pages = "203-209",
doi = "10.1016/j.bej.2010.10.014"
}

Božić, N., Ruiz, J., Lopez-Santin, J.,& Vujčić, Z.. (2011). Production and properties of the highly efficient raw starch digesting alpha-amylase from a Bacillus licheniformis ATCC 9945a. in Biochemical Engineering Journal
Elsevier Science Sa, Lausanne., 53(2), 203-209.
https://doi.org/10.1016/j.bej.2010.10.014

Božić N, Ruiz J, Lopez-Santin J, Vujčić Z. Production and properties of the highly efficient raw starch digesting alpha-amylase from a Bacillus licheniformis ATCC 9945a. in Biochemical Engineering Journal. 2011;53(2):203-209.
doi:10.1016/j.bej.2010.10.014 .

Božić, Nataša, Ruiz, Jordi, Lopez-Santin, Josep, Vujčić, Zoran, "Production and properties of the highly efficient raw starch digesting alpha-amylase from a Bacillus licheniformis ATCC 9945a" in Biochemical Engineering Journal, 53, no. 2 (2011):203-209,
https://doi.org/10.1016/j.bej.2010.10.014 . .