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   <subfield code="a">Expression and display of a novel thermostable esterase from Clostridium thermocellum on the surface of Bacillus subtilis using the CotB anchor protein</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Huayou Chen, Tianxi Zhang, Jinru Jia, Ake Vastermark, Rui Tian, Zhong Ni, Zhi Chen, Keping Chen, Shengli Yang]</subfield>
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   <subfield code="a">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°C, respectively. It also demonstrates a broad temperature and pH optimum in the range of 50-70, 7-9.5°C. The spore surface-displayed esterase-DSM retained 78, 68% of its original activity after 5h incubation at 60 and 70°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 7h 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.</subfield>
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   <subfield code="a">Society for Industrial Microbiology and Biotechnology, 2015</subfield>
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   <subfield code="a">Metadata rights reserved</subfield>
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