Simultaneously Improved Thermostability and Hydrolytic Pattern of Alpha-Amylase by Engineering Central Beta Strands of TIM Barrel-Reference-Cited by-同舟云学术

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Simultaneously Improved Thermostability and Hydrolytic Pattern of Alpha-Amylase by Engineering Central Beta Strands of TIM Barrel

Published:2020-03-27 Issue:1 Volume:192 Page:57-70
ISSN:0273-2289
Container-title:Applied Biochemistry and Biotechnology
language:en
Short-container-title:Appl Biochem Biotechnol

Author:

Wang Cheng-Hua,Lu Liang-Hua,Huang Cheng,He Bing-Fang,Huang Ri-Bo

Funder

National Natural Science Foundation of China

National Basic Research Program of China

Major Program of Natural Science Foundation of Guangxi

Guangxi BaGui Scholars of Guangxi Zhuang Autonomous Region of China

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Applied Microbiology and Biotechnology,Biochemistry,General Medicine,Bioengineering,Biotechnology

Link

http://link.springer.com/content/pdf/10.1007/s12010-020-03308-8.pdf

Reference46 articles.

1. Farber, G. K., & Petsko, G. A. (1990). The evolution of [alpha]/[beta] barrel enzymes. Trends in Biochemical Sciences, 15(6), 228–234.

2. Brändén, R. I. (1991). The TIM barrel—The most frequently occurring folding motif in proteis. Current Opinion in Structural Biology, 1, 978–983.

3. Petsko, G. A. (2000). Enzyme evolution. Design by necessity. Nature, 403(6770), 606–607.

4. Wierenga, R. K. (2001). The TIM-barrel fold: A versatile framework for efficient enzymes. FEBS Letters, 492(3), 193–198.

5. Hocker, B., Jurgens, C., Wilmanns, M., & Sterner, R. (2001). Stability, catalytic versatility and evolution of the (beta alpha)(8)-barrel fold. Current Opinion in Biotechnology, 12(4), 376–381.

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