Rational design of a thermophilic β-mannanase fromBacillus subtilis TJ-102 to improve its thermostability-Reference-Cited by-同舟云学术

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Rational design of a thermophilic β-mannanase fromBacillus subtilis TJ-102 to improve its thermostability

Published:2018-11 Issue: Volume:118 Page:50-56
ISSN:0141-0229
Container-title:Enzyme and Microbial Technology
language:en
Short-container-title:Enzyme and Microbial Technology

Author:

Wang Xiang-Chao,You Sheng-Ping,Zhang Jia-Xing,Dai Ye-Mei,Zhang Cheng-Yu,Qi Wei,Dou Tong-Yi^ORCID,Su Rong-Xin,He Zhi-Min

Funder

Key Project of Science and Technology Committee of Tianjin

Natural Science Foundation of China

State Key Laboratory of Chemical Engineering

Beiyang Young Scholar Program of Tianjin University

Publisher

Elsevier BV

Subject

Applied Microbiology and Biotechnology,Biochemistry,Biotechnology,Bioengineering

Reference34 articles.

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2. Conformational stability of globular proteins;Pace;Trends Biochem. Sci.,1990

3. A study on the effects of linker flexibility on acid phosphatase PhoC-GFP fusion protein using a novel linker library;Huang;Enzyme Microb. Technol.,2016

4. Iterative saturation mutagenesis on the basis of B factors as a strategy for increasing protein thermostability;Reetz;Angew. Chem.,2006

5. The thermodynamic signature of ligand binding to histone deacetylase-like amidohydrolases is most sensitive to the flexibility in the L2-loop lining the active site pocket;Meyners;Biochimica et Biophysica Acta (BBA) - General Subjects,2017

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