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 . .