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Expression and display of a novel thermostable esterase from Clostridium thermocellum on the surface of Bacillus subtilis using the CotB anchor protein
Chen, Huayou1,2,3; Zhang, Tianxi1; Jia, Jinru1; Vastermark, Ake3; Tian, Rui1; Ni, Zhong1; Chen, Zhi1; Chen, Keping1; Yang, Shengli1
2015-11-01
Source PublicationJOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY
ISSN1367-5435
Volume42Issue:11Pages:1439-1448
AbstractEsterases 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.
KeywordThermophilic Esterase Bacillus Subtilis Cotb Surface Display
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
DOI10.1007/s10295-015-1676-8
Indexed BySCI
Language英语
WOS KeywordSPORE COAT ; RECOMBINANT PROTEINS ; ORGANIC-SOLVENTS ; IMMOBILIZATION ; ENZYMES ; SYSTEM ; VACCINE ; LIPASE ; CLASSIFICATION ; STABILIZATION
WOS Research AreaBiotechnology & Applied Microbiology
WOS SubjectBiotechnology & Applied Microbiology
WOS IDWOS:000362964900002
Citation statistics
Cited Times:14[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.ipe.ac.cn/handle/122111/19642
Collection生化工程国家重点实验室
Affiliation1.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
Recommended Citation
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.
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