NDLI: Expression and Displaying of β-Glucosidase from Streptomyces Coelicolor A3 in Escherichia coli

Content Provider	Springer Nature Link
Author	Gu, Ming Zhu Wang, Jing Chao Liu, Wei Bing Zhou, Ying Ye, Bang Ce
Copyright Year	2013
Abstract	Two genes encoding β-glucosidase from Streptomyces coelicolor A3(2) were cloned and expressed in Escherichia coli BL21 (DE3). Two recombinant enzymes (SC1059 and SC7558) were purified and characterized. The molecular mass of the purified SC1059 and SC7558 as determined by SDS-PAGE agrees with the calculated values (51.0 and 52.2 kDa, respectively). Optimal temperature and pH for the two enzymes were both at 35 °C and 6.0. SC7558 exhibited to be much more active than SC1059 under optimal conditions, and it was recombined with ice nucleation protein which could anchor on the surface of the cell. The optimal temperature and pH of the recombinant cells were 55 °C and 8.0, respectively. The resultant cells were to be used as material for immobilized β-glucosidase, which is convenient to catalyze substrates in various complicated conditions.
Starting Page	1713
Ending Page	1723
Page Count	11
File Format	PDF
ISSN	02732289
Journal	Applied Biochemistry and Biotechnology
Volume Number	170
Issue Number	7
e-ISSN	15590291
Language	English
Publisher	Springer US
Publisher Date	2013-05-31
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	β-Glucosidase Surface displaying Streptomyces coelicolor Biotechnology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Environmental Engineering Biochemistry Bioengineering Applied Microbiology and Biotechnology Biotechnology

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