南京林业大学学报(自然科学版) ›› 2006, Vol. 49 ›› Issue (03): 37-40.doi: 10.3969/j.jssn.1000-2006.2006.03.007

• 研究论文 • 上一篇    下一篇

降解结晶纤维素极耐热葡聚糖酶重组菌的构建

李相前1,2,邵蔚蓝1,3*   

  1. 1. 江南大学工业生物技术教育部重点实验室, 江苏 无锡 214036; 2. 淮阴工学院生物工程与化学工程系, 江苏 淮安 223001; 3. 南京师范大学生命科学学院, 江苏 南京 210097
  • 出版日期:2016-06-18 发布日期:2016-06-18

Construction of Recombinant Escherichia coli for Producing Extremely Thermostability Endoglucanase

LI Xiang-qian1,2, SHAO Wei-lan1,3*   

  1. 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
  • Online:2016-06-18 Published:2016-06-18

摘要: <正>运用产业组织理论、经济学原理和企业管理理论研究了林纸一体化的动力机制模型和运行机理,并对其动因机制、产业组织机制和目标机制进行了分析。从而为促进我国林纸一体化进程,提高林纸一体化组织的生命力和竞争力提供了理论指导。

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.

中图分类号: