Display of Thermotoga maritima MSB8 nitrilase on the spore surface of Bacillus subtilis using out coat protein CotG as the fusion partner

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	Display of Thermotoga maritima MSB8 nitrilase on the spore surface of Bacillus subtilis using out coat protein CotG as the fusion partner
	Chen, Huayou 1,2; Chen, Zhi 1; Ni, Zhong 1; Tian, Rui 1; Zhang, Tianxi 1; Jia, Jinru 1; Chen, Keping 1; Yang, Shengli 1
刊名	JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
	2016
卷号	123 期号:JAN 页码:73-80
关键词	Nitrilase B. subtilis Spore surface display Enzyme immobilization
ISSN号	1381-1177
通讯作者	Chen, HY (reprint author), Jiangsu Univ, Inst Life Sci, Xuefu Rd 301, Zhenjiang 212000, Peoples R China.
英文摘要	In the present study, probiotic Bacillus spores were used as a matrix for enzyme immobilization, because of their inherent resistance to extreme temperatures, UV irradiation, solvents and drying. An Escherichia coli- Bacillus subtilis shuttle vector (pHS-CotG-nit) was constructed for the spore surface display of the nitrilase from hyperthermophilic bacterium Thermotoga maritima MSB8. The successful display of CotG-nit fusion protein on the spore surface of B. subtilis was verified by western blot analysis and activity measurement. The optimal temperature and pH of the spore surface-dispalyed nitrilase were observed to be 50 degrees C and pH 8.0, respectively, which were higher than the free nitrilase (45 degrees C and pH 7.5). The analysis of thermal and pH stability indicated that the spore surface-displayed nitrilase retained 79% and 97% at 75 degrees C and pH 8.0 after 1 h of incubation, whereas it were 32% and 52%, respectively, for free nitrilase. Furthermore, the reusability experiments indicated that the activity of the spore surface displayed nitrilase was not significantly decreased throughout the reusability process, which still retained 83% of the initial activity at the fifth cycle. Above all, these results suggested that surface display of enzymes on the spore of B. subtilis might be an effective method for enzyme immobilization and help to meet the ever-increasing industrial demand for preparation and stabilization of biocatalysts. (C) 2015 Elsevier B.V. All rights reserved.
WOS标题词	Science & Technology ; Life Sciences & Biomedicine ; Physical Sciences
类目[WOS]	Biochemistry & Molecular Biology ; Chemistry, Physical
研究领域[WOS]	Biochemistry & Molecular Biology ; Chemistry
关键词[WOS]	BIOCHEMICAL-CHARACTERIZATION ; EFFICIENT PRODUCTION ; BIOCATALYSIS ; IMMOBILIZATION ; SYSTEM ; HYDROLYSIS ; RESISTANCE ; LACCASE ; ENZYME ; CELLS
收录类别	SCI
原文出处	ELSEVIER SCIENCE BV
语种	英语
WOS记录号	WOS:000369681800012
内容类型	期刊论文
源URL	[http://ir.ipe.ac.cn/handle/122111/20655]
专题	过程工程研究所_研究所（批量导入）
作者单位	1.Jiangsu Univ, Inst Life Sci, Xuefu Rd 301, Zhenjiang 212000, Peoples R China 2.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing, Peoples R China
推荐引用方式 GB/T 7714	Chen, Huayou,Chen, Zhi,Ni, Zhong,et al. Display of Thermotoga maritima MSB8 nitrilase on the spore surface of Bacillus subtilis using out coat protein CotG as the fusion partner[J]. JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,2016,123(JAN):73-80.
APA	Chen, Huayou.,Chen, Zhi.,Ni, Zhong.,Tian, Rui.,Zhang, Tianxi.,...&Yang, Shengli.(2016).Display of Thermotoga maritima MSB8 nitrilase on the spore surface of Bacillus subtilis using out coat protein CotG as the fusion partner.JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,123(JAN),73-80.
MLA	Chen, Huayou,et al."Display of Thermotoga maritima MSB8 nitrilase on the spore surface of Bacillus subtilis using out coat protein CotG as the fusion partner".JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC 123.JAN(2016):73-80.