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Surface display of the thermophilic lipase Tm1350 on the spore of Bacillus subtilis by the CotB anchor protein
Chen, Huayou1,2; Tian, Rui1; Ni, Zhong1; Zhang, Qing1; Zhang, Tianxi1; Chen, Zhi1; Chen, Keping1; Yang, Shengli1
2015-07-01
Source PublicationEXTREMOPHILES
ISSN1431-0651
Volume19Issue:4Pages:799-808
Abstract

Lipases expressed in microbial hosts have great commercial value, but their applications are restricted by the high costs of production and harsh conditions used in industrial processes, such as high temperature and alkaline environment. In this study, an Escherichia coli-Bacillus subtilis shuttle vector (pHS-cotB-Tm1350) was constructed for the spore surface display of the lipase Tm1350 from hyperthermophilic bacterium Thermotoga maritima MSB8. Successful display of the CotB-Tm1350 fusion protein on spore surface was confirmed by Western blot analysis and activity measurements. The optimal catalytic temperature and pH of the spore surface-displayed Tm1350 were 80 A degrees C and 9, respectively, which were higher than non-immobilized Tm1350 (70 A degrees C and pH 7.5). Analysis of thermal and pH stability showed that spore surface-displayed Tm1350 retained 81 or 70 % of its original activity after 8 h of incubation at pH 8 or pH 9 (70 A degrees C), which were 18 % higher than the retained activity of the non-immobilized Tm1350 under the same conditions. Meanwhile, recycling experiments showed that the recombinant spores could be used for up to three reaction cycles without a significant decrease in the catalytic rate (84 %). These results suggested that enzyme display on the surface of the B. subtilis spore could serve as an effective approach for enzyme immobilization, which has potential applications in the harsh biochemical industry.

KeywordThermophilic Lipase Bacillus Subtilis Cotb Spore Surface Display
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
DOI10.1007/s00792-015-0755-0
Indexed BySCI
Language英语
WOS KeywordORGANIC-SOLVENTS ; RECOMBINANT PROTEINS ; COAT ; SYSTEM ; IMMOBILIZATION ; EXTREMOPHILES ; PURIFICATION ; EXPRESSION
WOS Research AreaBiochemistry & Molecular Biology ; Microbiology
WOS SubjectBiochemistry & Molecular Biology ; Microbiology
WOS IDWOS:000358290000009
Citation statistics
Document Type期刊论文
Identifierhttp://ir.ipe.ac.cn/handle/122111/19404
Collection生化工程国家重点实验室
Affiliation1.Jiangsu Univ, Inst Life Sci, Zhenjiang 212013, Peoples R China
2.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 10090, Peoples R China
Recommended Citation
GB/T 7714
Chen, Huayou,Tian, Rui,Ni, Zhong,et al. Surface display of the thermophilic lipase Tm1350 on the spore of Bacillus subtilis by the CotB anchor protein[J]. EXTREMOPHILES,2015,19(4):799-808.
APA Chen, Huayou.,Tian, Rui.,Ni, Zhong.,Zhang, Qing.,Zhang, Tianxi.,...&Yang, Shengli.(2015).Surface display of the thermophilic lipase Tm1350 on the spore of Bacillus subtilis by the CotB anchor protein.EXTREMOPHILES,19(4),799-808.
MLA Chen, Huayou,et al."Surface display of the thermophilic lipase Tm1350 on the spore of Bacillus subtilis by the CotB anchor protein".EXTREMOPHILES 19.4(2015):799-808.
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