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降解结晶纤维素极耐热葡聚糖酶重组菌的构建(PDF)

《南京林业大学学报(自然科学版)》[ISSN:1000-2006/CN:32-1161/S]

Issue:
2006年03期
Page:
37-40
Column:
研究论文
publishdate:
2006-03-20

Article Info:/Info

Title:
Construction of Recombinant Escherichia coli for Producing Extremely Thermostability Endoglucanase
Article ID:
1000-2006(2006)03-0037-04
Author(s):
LI Xiang-qian12 SHAO Wei-lan13*
1. The Key Laboratory of Industrial Biotechnology of Education Ministry Southern Yangtze University, Wuxi 214036, China; 2. Department of Chemical and Bioengineering Huaiyin Institute of Technology, Huai’an 223001, China; 3. School of Life Science Nanjing Normal University, Nanjing 210097, China
Keywords:
Crystalline cellulose Gene fusion Thermostability endoglucanase
Classification number :
Q556
DOI:
10.3969/j.jssn.1000-2006.2006.03.007
Document Code:
A
Abstract:
The endoglucanase found in Thermotoga maritirna showed extremely high thermostability and considerable potential in industrial application of enzymatic hydrolysis of cellulose. Endoglucanase (Tin) Cel12B is extracellular enzyme. Tm Cel12B did not contain a cellulose-binding domain(CBD)and lacked activity on crystalline cellulose. Tm XynA is composed of catalytic domain(CD)and cellulose-binding domain(CBD). As such, the gene of CBD from Tm XynA was fused at the earboxyl-terminus of Tm CeI12B and recombinant plasmid pET-2Ob-Cel12B-CBD was obtained. The chimera enzyme was expressed in Escherichia coli and activities were displayed on crystalline cellulose.

References

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Last Update: 2013-05-20