Enhanced thermal stability of lichenase from Bacillus subtilis 168 by SpyTag

	Enhanced thermal stability of lichenase from Bacillus subtilis 168 by SpyTag
	Jindan Wang 1; Yilin Wang 2; Xinzhe Wang 1; Dandan Zhang 1; Shuyu Wu 1; Guangya Zhang 1
刊名	Biotechnology for Biofuels
	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
内容类型	期刊论文
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).