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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, Huayou1,2; Chen, Zhi1; Ni, Zhong1; Tian, Rui1; Zhang, Tianxi1; Jia, Jinru1; Chen, Keping1; Yang, Shengli1
2016
发表期刊JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
ISSN1381-1177
卷号123期号:JAN页码:73-80
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.

关键词Nitrilase B. suB.ilis Spore Surface Display Enzyme Immobilization
文章类型Article
WOS标题词Science & Technology ; Life Sciences & Biomedicine ; Physical Sciences
DOI10.1016/j.molcatb.2015.11.002
URL查看原文
收录类别SCI
语种英语
关键词[WOS]Biochemical-characterization ; Efficient Production ; Biocatalysis ; Immobilization ; System ; Hydrolysis ; Resistance ; Laccase ; Enzyme ; Cells
WOS研究方向Biochemistry & Molecular Biology ; Chemistry
WOS类目Biochemistry & Molecular Biology ; Chemistry, Physical
项目资助者National Key Basic Research Program of China (973 Program)(2011CBA00800) ; Key Agriculture Support Project of Jiangsu Province, China(BE2013400) ; Open Funding Project of National Key Laboratory of Biochemical Engineering
WOS记录号WOS:000369681800012
引用统计
被引频次:9[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.ipe.ac.cn/handle/122111/20655
专题研究所(批量导入)
通讯作者Chen, Huayou
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
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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.
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