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
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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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