中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Enhanced thermal stability of lichenase from Bacillus subtilis 168 by SpyTag

文献类型:期刊论文

作者Jindan Wang1; Yilin Wang2; Xinzhe Wang1; Dandan Zhang1; Shuyu Wu1; Guangya Zhang1
刊名Biotechnology for Biofuels
出版日期2016
卷号9期号:1
ISSN号1754-6834
其他题名Enhanced thermal stability of lichenase from Bacillus subtilis 168 by SpyTag
英文摘要SpyTag is a peptide that can form an irreversible covalent linkage to its 12kDa partner SpyCatcher via a spontaneous isopeptide bond. Herein, we fused SpyTag at the N-terminal of lichenase and SpyCatcher at C-terminal so that the termini of lichenase were locked together by the covalent interaction between the partners. In addition, an elastin-like polypeptides tag was subsequently attached to the C-terminus of SpyCatcher, thereby facilitating the non-chromatographic purification of cyclized lichenase.
语种英语
源URL[http://ir.yic.ac.cn/handle/133337/34500]  
专题中国科学院烟台海岸带研究所
作者单位1.华侨大学
2.Yantai Institute of Coastal Zone Research, Chinese Academy of Sciences
推荐引用方式
GB/T 7714
Jindan Wang,Yilin Wang,Xinzhe Wang,et al. Enhanced thermal stability of lichenase from Bacillus subtilis 168 by SpyTag[J]. Biotechnology for Biofuels,2016,9(1).
APA Jindan Wang,Yilin Wang,Xinzhe Wang,Dandan Zhang,Shuyu Wu,&Guangya Zhang.(2016).Enhanced thermal stability of lichenase from Bacillus subtilis 168 by SpyTag.Biotechnology for Biofuels,9(1).
MLA Jindan Wang,et al."Enhanced thermal stability of lichenase from Bacillus subtilis 168 by SpyTag".Biotechnology for Biofuels 9.1(2016).

入库方式: OAI收割

来源:烟台海岸带研究所

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