Search

Your search keyword '"Wei-Juan Ru"' showing total 2 results
Start Over Author "Wei-Juan Ru"
2 results on '"Wei-Juan Ru"'

1. Research progress on structure and catalytic mechanism of dextranase

Author

Xue‐Qin Hu, Bing‐Bing Xia, Wei‐Juan Ru, Yu‐Xin Zhang, Jing‐Wen Yang, and Hong‐Bin Zhang

Subjects
catalytic mechanism, catalytic pocket, dextranase, molecular simulation and molecular docking, structural characteristics, Food processing and manufacture, TP368-456, Toxicology. Poisons, RA1190-1270
Abstract

Abstract Dextranase is an important industrial enzyme for the preparation of isomalto‐oligosaccharides. According to the crystal structures of 20 dextranases of four classes, we summarized the structural characteristics of enzymes and the binding modes of enzymes and ligands in this paper. Based on the characteristics of the products, we analyzed the characteristics of the binding domain and functions of dextranase by means of molecular simulation and molecular docking. The relationship between the product specificity of dextranase, its catalytic pocket shape, and its catalytic mode was briefly summarized. The catalytic mechanism of dextranase was systematically discussed, which provided the basis and reference for the rational transformation of dextranase.

Published
2023
Full Text
View/download PDF

2. Development of thermostable dextranase from Streptococcus mutans (SmdexTM) through in silico design employing B-factor and Cartesian-ΔΔG

Author

Wei-Juan Ru, Bing-Bing Xia, Yu-Xin Zhang, Jing-Wen Yang, Hong-Bin Zhang, and Xue-Qin Hu

Subjects
Streptococcus mutans, Enzyme Stability, Bioengineering, General Medicine, Dextranase, Applied Microbiology and Biotechnology, Biotechnology
Abstract

The thermal stability of enzymes dramatically limits their application in the industrial field. Based on the crystal structure, we conducted a semi-rational design according to the B-factor and free energy values to improve the stability of dextranase from Streptococcus mutans (SmdexTM). The B-factor values of Asn102, Asn503, Asp501 and Asp500 were the highest predicted by B-FITTER. Then Rosetta was used to simulate the saturation mutations of Asn102, Asn503, Asp501 and Asp500. The mutated amino acid was designed according to the change of acG. The results showed that the thermal stability of N102P, N102C, D500G, and D500T was improved, and the half-lives of N102P/D500G and N102P/D500T at 45 °C were increased to 3.14 times and 2.44 times, respectively. Analyzing the interaction of amino acids by using Discovery Studio 4.5, it was observed that the thermal stability of dextranase was improved due to the increase in hydrophobicity and the number of hydrogen bonds of the mutant enzyme. The catalytic efficiency of N102P/D500T was increased. Compared with the hydrolyzed products of SmdexTM, the mutant enzymes do not change the specificity of hydrolysates.

Published
2022

Catalog

Books, media, physical & digital resources
See catalog results