Xiaomin Wei
Shandong University
9 Papers
100 Citations
Xiaomin Wei is an academic researcher from Shandong University. The author has contributed to research in topics: Trichoderma reesei & Penicillium decumbens. The author has an hindex of 8, co-authored 8 publications.
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Papers
Genomic and secretomic analyses reveal unique features of the lignocellulolytic enzyme system of Penicillium decumbens.
Guodong Liu,Lei Zhang,Xiaomin Wei,Gen Zou,Yuqi Qin,Liang Ma,Jie Li,Huajun Zheng,Shengyue Wang,Chengshu Wang,Luying Xun,Luying Xun,Guoping Zhao,Guoping Zhao,Zhihua Zhou,Yinbo Qu +15 more
TL;DR: Comparative genomics analysis with the phylogenetically most similar species Penicillium chrysogenum and proteomic analysis of secretomes revealed that P. decumbens has evolved with more genes involved in plant cell wall degradation, but fewer genes in cellular metabolism and regulation.
Engineering endoglucanase II from Trichoderma reesei to improve the catalytic efficiency at a higher pH optimum.
TL;DR: More stable helixes and changed electrostatic interactions between the catalytic residues and substrates may explain the higher activities and higher pH optima of the variants of Trichoderma reesei endo-beta-1,4-glucanase II.
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Long-term strain improvements accumulate mutations in regulatory elements responsible for hyper-production of cellulolytic enzymes.
Guodong Liu,Lei Zhang,Yuqi Qin,Gen Zou,Zhonghai Li,Xing Yan,Xiaomin Wei,Mei Chen,Ling Chen,Kai Zheng,Jun Zhang,Liang Ma,Jie Li,Rui Liu,Hai Xu,Xiaoming Bao,Xu Fang,Lushan Wang,Yaohua Zhong,Weifeng Liu,Huajun Zheng,Shengyue Wang,Chengshu Wang,Luying Xun,Luying Xun,Guoping Zhao,Guoping Zhao,Tianhong Wang,Zhihua Zhou,Yinbo Qu +29 more
TL;DR: In this article, the genome of the hyper-producer P. decumbens JU-A10-T was sequenced and compared with that of the wild-type strain 114-2.
The role of the site 342 in catalytic efficiency and pH optima of endoglucanase II from Trichoderma reesei as probed by saturation mutagenesis
TL;DR: The role of site 342 of endoglucanase II from Trichoderma reesei in catalytic efficiency and pH optima was investigated by site saturation mutagenesis and molecular modelling indicated that residue 342 was located at the C-terminus of one of the α-helices near two catalytic residues.
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