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Thermostable Bacterial Endoglucanases Mined from Swiss-Prot Database

Thermostable Bacterial Endoglucanases Mined from Swiss-Prot Database As one critical enzyme in deconstructing complicated cellulose matrix, endoglucanase (EG) is needed to exhibit high activity and thermostability under severe industrial conditions. Driven by this purpose, EGtf1 (Q08166) and EGtf2 (Q7X2N2), with relatively high specific activities, were selected out of 43 putative EG genes from SWISS-PROT database. These distinguished EGs were successfully overexpressed in Escherichia coli and purified by one-step affinity chromatography. The maximal activity was shown at approximate pH 5.0 and 50 °C. It is worth noting that EGtf1 and EGtf2 displayed outstanding thermostability with a half-life of up to 1,386 h at 50 °C, which is almost 100-fold higher than other reported EGs. Furthermore, the presence of various metal ions (1 mM) or organic solvents (50%, v/v) did not cause significant effect on the activities of EGtf1 and EGtf2 and even showed 2.1- and 2.7-fold enhancement in the case of dodecanol. All these features, especially the excellent thermostability of EGtf1 and EGtf2, enable them to become a good candidate for further protein engineering to realize the ultimate practical application in biomass industry. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied Biochemistry and Biotechnology Springer Journals

Thermostable Bacterial Endoglucanases Mined from Swiss-Prot Database

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References (28)

Publisher
Springer Journals
Copyright
Copyright © 2011 by Springer Science+Business Media, LLC
Subject
Chemistry; Biochemistry, general; Biotechnology
ISSN
0273-2289
eISSN
1559-0291
DOI
10.1007/s12010-011-9368-y
pmid
21989797
Publisher site
See Article on Publisher Site

Abstract

As one critical enzyme in deconstructing complicated cellulose matrix, endoglucanase (EG) is needed to exhibit high activity and thermostability under severe industrial conditions. Driven by this purpose, EGtf1 (Q08166) and EGtf2 (Q7X2N2), with relatively high specific activities, were selected out of 43 putative EG genes from SWISS-PROT database. These distinguished EGs were successfully overexpressed in Escherichia coli and purified by one-step affinity chromatography. The maximal activity was shown at approximate pH 5.0 and 50 °C. It is worth noting that EGtf1 and EGtf2 displayed outstanding thermostability with a half-life of up to 1,386 h at 50 °C, which is almost 100-fold higher than other reported EGs. Furthermore, the presence of various metal ions (1 mM) or organic solvents (50%, v/v) did not cause significant effect on the activities of EGtf1 and EGtf2 and even showed 2.1- and 2.7-fold enhancement in the case of dodecanol. All these features, especially the excellent thermostability of EGtf1 and EGtf2, enable them to become a good candidate for further protein engineering to realize the ultimate practical application in biomass industry.

Journal

Applied Biochemistry and BiotechnologySpringer Journals

Published: Oct 12, 2011

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