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The DsbA signal peptide-mediated secretion of a highly efficient raw-starch-digesting, recombinant alpha-amylase from Bacillus licheniformis ATCC 9945a

Authorized Users Only
2013
Authors
Božić, Nataša
Puertas, Juan-Miguel
Lončar, Nikola
Sans, Duran Cristina
Lopez-Santin, Josep
Vujčić, Zoran
Article (Published version)
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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.

Keywords:
alpha-Amylase / Bacillus licheniformis / Escherichia coli / DsbA signal peptide / Raw starch hydrolysis
Source:
Process Biochemistry, 2013, 48, 3, 438-442
Publisher:
  • Elsevier Sci Ltd, Oxford
Funding / projects:
  • Production, purification and characterization of enzymes and small molecules and their application as soluble or immobilized in food biotechnology, biofuels production and environmental protection (RS-172048)
  • Federation of European Biochemical Societies
  • Joint Serbian-Spanish Action
  • Spanish MICINN [CTQ2011-28398-CO2-01]

DOI: 10.1016/j.procbio.2013.01.016

ISSN: 1359-5113

WoS: 000318262900008

Scopus: 2-s2.0-84875906938
[ Google Scholar ]
11
8
URI
https://cer.ihtm.bg.ac.rs/handle/123456789/1368
Collections
  • Radovi istraživača / Researchers' publications
Institution/Community
IHTM
TY  - JOUR
AU  - Božić, Nataša
AU  - Puertas, Juan-Miguel
AU  - Lončar, Nikola
AU  - Sans, Duran Cristina
AU  - Lopez-Santin, Josep
AU  - Vujčić, Zoran
PY  - 2013
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1368
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.
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 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.",
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., Sans, D. 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 N, Sans DC, 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, 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 . .

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