详细信息

Expression and Displaying of β-Glucosidase from Streptomyces Coelicolor A3 in Escherichia coli  ( SCI-EXPANDED收录 EI收录)  

文献类型:期刊文献

英文题名:Expression and Displaying of β-Glucosidase from Streptomyces Coelicolor A3 in Escherichia coli

作者:Gu, Ming-Zhu[1];Wang, Jing-Chao[1];Liu, Wei-Bing[1];Zhou, Ying[1];Ye, Bang-Ce[1]

机构:[1]E China Univ Sci & Technol, State Key Lab Bioreactor Engn, Lab Biosyst & Microanal, Shanghai 200237, Peoples R China

年份:2013

卷号:170

期号:7

起止页码:1713

外文期刊名:APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY

收录:;EI(收录号:20133316610377);WOS:【SCI-EXPANDED(收录号:WOS:000322542900014)】;

基金:This study is supported by the China NSF 21276079, SRFDP (No. 20120074110009), the Key Grant Project (No. 313019) of the Chinese Ministry of Education, and the Fundamental Research Funds for the Central Universities.

语种:英文

外文关键词:beta-Glucosidase; Surface displaying; Streptomyces coelicolor

摘要:Two genes encoding beta-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 A degrees 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 A degrees C and 8.0, respectively. The resultant cells were to be used as material for immobilized beta-glucosidase, which is convenient to catalyze substrates in various complicated conditions.

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