Enhanced thermal stability of lichenase from Bacillus subtilis 168 by SpyTag

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	Enhanced thermal stability of lichenase from Bacillus subtilis 168 by SpyTag
其他题名	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
发表期刊	Biotechnology for Biofuels
ISSN	1754-6834
	2016
卷号	9 期号:1
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.
中文摘要	Background 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. Results The study showed that the optimum temperature of the cyclized lichenase was about 5°C higher in comparison to its linear counterpart. Moreover, nearly 80% of the cyclized lichenase activities were retained after 100°C exposure, whereas the linear form lost almost all of its activities. Therefore, the cyclized variant displayed a significantly higher thermal stability as temperature elevated and was resistant to hyperthermal denaturation. Besides, the Km value of the cyclized lichenase (7.58±0.92mg Conclusions This new SpyTag
语种	英语
文献类型	期刊论文
条目标识符	http://ir.yic.ac.cn/handle/133337/34501
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).