Expression and display of a novel thermostable esterase from Clostridium thermocellum on the surface of Bacillus subtilis using the CotB anchor protein
文献类型：期刊论文
| 作者 | Chen, Huayou1,2,3; Zhang, Tianxi1; Jia, Jinru1; Vastermark, Ake3; Tian, Rui1; Ni, Zhong1; Chen, Zhi1; Chen, Keping1; Yang, Shengli1 |
| 刊名 | JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY
 |
| 出版日期 | 2015-11-01 |
| 卷号 | 42期号:11页码:1439-1448 |
| 关键词 | Thermophilic Esterase Bacillus subtilis CotB Surface display |
| ISSN号 | 1367-5435 |
| 英文摘要 | Esterases expressed in microbial hosts are commercially valuable, but their applications are limited due to high costs of production and harsh industrial processes involved. In this study, the esterase-DSM (from Clostridium thermocellum) was expressed and successfully displayed on the spore surface, and the spore-associated esterase was confirmed by western blot analysis and activity measurements. The optimal temperature and pH of spore surface-displayed DSM was 60 and 8.5 A degrees C, respectively. It also demonstrates a broad temperature and pH optimum in the range of 50-70, 7-9.5 A degrees C. The spore surface-displayed esterase-DSM retained 78, 68 % of its original activity after 5 h incubation at 60 and 70 A degrees C, respectively, which was twofold greater activity than that of the purified DSM. The recombinant spores has high activity and stability in DMSO, which was 49 % higher than the retained activity of the purified DSM in DMSO (20 % v/v), and retained 65.2 % of activity after 7 h of incubation in DMSO (20 % v/v). However, the recombinant spores could retain 77 % activity after 3 rounds of recycling. These results suggest that enzyme displayed on the surface of the Bacillus subtilis spore could serve as an effective approach for enzyme immobilization. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biotechnology & Applied Microbiology |
| 研究领域[WOS] | Biotechnology & Applied Microbiology |
| 关键词[WOS] | SPORE COAT ; RECOMBINANT PROTEINS ; ORGANIC-SOLVENTS ; IMMOBILIZATION ; ENZYMES ; SYSTEM ; VACCINE ; LIPASE ; CLASSIFICATION ; STABILIZATION |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000362964900002 |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/19642]  |
| 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, Jiangsu, Peoples R China 2.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 10090, Peoples R China 3.Univ Calif San Diego, Div Biol Sci, La Jolla, CA 92093 USA |
| 推荐引用方式 GB/T 7714 | Chen, Huayou,Zhang, Tianxi,Jia, Jinru,et al. Expression and display of a novel thermostable esterase from Clostridium thermocellum on the surface of Bacillus subtilis using the CotB anchor protein[J]. JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY,2015,42(11):1439-1448. |
| APA | Chen, Huayou.,Zhang, Tianxi.,Jia, Jinru.,Vastermark, Ake.,Tian, Rui.,...&Yang, Shengli.(2015).Expression and display of a novel thermostable esterase from Clostridium thermocellum on the surface of Bacillus subtilis using the CotB anchor protein.JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY,42(11),1439-1448. |
| MLA | Chen, Huayou,et al."Expression and display of a novel thermostable esterase from Clostridium thermocellum on the surface of Bacillus subtilis using the CotB anchor protein".JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY 42.11(2015):1439-1448. |
入库方式： OAI收割
来源：过程工程研究所
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