Effect of the C-terminal domains and terminal residues of catalytic domain on enzymatic activity and thermostability of lichenase from Clostridium thermocellum |
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Authors: | Dong Niu Xu-xia Zhou Tao-yan Yuan Zhi-wei Lin Hui Ruan Wei-fen Li |
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Affiliation: | 1. College of Animal Sciences, Zhejiang University, 310029, Hangzhou, China 2. Key Laboratory of Molecular Animal Nutrition, Ministry of Education, 310029, Hangzhou, China 3. School of Biosystems Engineering and Food Science, Zhejiang University, 310029, Hangzhou, China
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Abstract: | To elucidate the effects of C-terminal domains of LicMB (mature lichenase from Clostridium thermocellum) and terminal residues of LicMB-CD (catalytic domain of LicMB) on the properties of lichenase, a series of truncated genes were constructed and expressed in E. coli. The Thr-Pro box had a positive effect while the dockerin domain had a negative impact on the properties of LicMB. The N-terminal 10–25th and C-terminal 1–9th residues of LicMB-CD were necessary to retain high thermostability while the N-terminal 1–7th and C-terminal 1–3rd residues were not necessary to maintain enzymatic activity. |
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