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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Chen, Ana Li, Yamei Nie, Jianqi McNeil, Brian Jeffrey, Laura Yang, Yankun Bai, Zhonghu |
| Description | Author Affiliation: Chen A ( National Engineering Laboratory for Cereal Fermentation Technology, Jiangnan University, Wuxi 214122, China); Li Y ( National Engineering Laboratory for Cereal Fermentation Technology, Jiangnan University, Wuxi 214122, China); Nie J ( National Engineering Laboratory for Cereal Fermentation Technology, Jiangnan University, Wuxi 214122, China); McNeil B ( University of Strathclyde, Glasgow G1 1XQ, UK.); Jeffrey L ( University of Strathclyde, Glasgow G1 1XQ, UK.); Yang Y ( National Engineering Laboratory for Cereal Fermentation Technology, Jiangnan University, Wuxi 214122, China); Bai Z ( National Engineering Laboratory for Cereal Fermentation Technology, Jiangnan University, Wuxi 214122, China) |
| Abstract | Thermostability has been considered as a requirement in the starch processing industry to maintain high catalytic activity of pullulanase under high temperatures. Four data driven rational design methods (B-FITTER, proline theory, PoPMuSiC-2.1, and sequence consensus approach) were adopted to identify the key residue potential links with thermostability, and 39 residues of Bacillus acidopullulyticus pullulanase were chosen as mutagenesis targets. Single mutagenesis followed by combined mutagenesis resulted in the best mutant E518I-S662R-Q706P, which exhibited an 11-fold half-life improvement at 60 °C and a 9.5 °C increase in Tm. The optimum temperature of the mutant increased from 60 to 65 °C. Fluorescence spectroscopy results demonstrated that the tertiary structure of the mutant enzyme was more compact than that of the wild-type (WT) enzyme. Structural change analysis revealed that the increase in thermostability was most probably caused by a combination of lower stability free-energy and higher hydrophobicity of E518I, more hydrogen bonds of S662R, and higher rigidity of Q706P compared with the WT. The findings demonstrated the effectiveness of combined data-driven rational design approaches in engineering an industrial enzyme to improve thermostability. |
| File Format | HTM / HTML |
| ISSN | 01410229 |
| Volume Number | 78 |
| e-ISSN | 18790909 |
| Journal | Enzyme and Microbial Technology |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-10-01 |
| Publisher Place | United States |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Microbiology Discipline Biochemistry Discipline Biotechnology Bacillus Enzymology Bacterial Proteins Metabolism Glycoside Hydrolases Amino Acid Sequence Amino Acid Substitution Genetics Chemistry Binding Sites Computer Simulation Enzyme Stability Hydrogen-ion Concentration Kinetics Models, Molecular Molecular Sequence Data Mutagenesis, Site-directed Protein Conformation Protein Engineering Methods Sequence Homology, Amino Acid Temperature Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biochemistry Bioengineering Applied Microbiology and Biotechnology Biotechnology |
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