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 | |
刊名 | EXTREMOPHILES |
2015-07-01 | |
卷号 | 19期号:4页码:799-808 |
关键词 | Thermophilic lipase Bacillus subtilis CotB Spore Surface display |
ISSN号 | 1431-0651 |
英文摘要 | 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. |
WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
类目[WOS] | Biochemistry & Molecular Biology ; Microbiology |
研究领域[WOS] | Biochemistry & Molecular Biology ; Microbiology |
关键词[WOS] | ORGANIC-SOLVENTS ; RECOMBINANT PROTEINS ; COAT ; SYSTEM ; IMMOBILIZATION ; EXTREMOPHILES ; PURIFICATION ; EXPRESSION |
收录类别 | SCI |
语种 | 英语 |
WOS记录号 | WOS:000358290000009 |
内容类型 | 期刊论文 |
源URL | [http://ir.ipe.ac.cn/handle/122111/19404] |
专题 | 过程工程研究所_生化工程国家重点实验室 |
作者单位 | 1.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 |
推荐引用方式 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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