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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
Source PublicationJOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
ISSN1381-1177
Volume123Issue:JANPages:73-80
Abstract

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.

KeywordNitrilase B. suB.ilis Spore Surface Display Enzyme Immobilization
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine ; Physical Sciences
DOI10.1016/j.molcatb.2015.11.002
URL查看原文
Indexed BySCI
Language英语
WOS KeywordBiochemical-characterization ; Efficient Production ; Biocatalysis ; Immobilization ; System ; Hydrolysis ; Resistance ; Laccase ; Enzyme ; Cells
WOS Research AreaBiochemistry & Molecular Biology ; Chemistry
WOS SubjectBiochemistry & Molecular Biology ; Chemistry, Physical
Funding OrganizationNational 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 IDWOS:000369681800012
Citation statistics
Cited Times:15[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.ipe.ac.cn/handle/122111/20655
Collection研究所(批量导入)
Corresponding AuthorChen, Huayou
Affiliation1.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
Recommended Citation
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.
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