Results 11 to 20 of about 38,411 (253)

Predicting Enzyme Turnover Numbers and Enabling Rational Enzyme Evolution. [PDF]

Adv Sci (Weinh)
MCKcat, a deep learning framework combining multi‐scale convolution and cross‐attention, accurately predicts enzyme turnover number (kcat) by fusing sequence and reaction representations. It couples with rational design in a two‐step strategy for Bacillus aryabhattai laccase engineering, achieving a 75% positive rate with synergistically enhanced ...
Ge F, Ma X, Li J, Wang M, Lu F, Liu Y, Wang L.   +6 more
europepmc   +2 more sources

Enhancement of protein thermostability by three consecutive mutations using loop-walking method and machine learning

Scientific Reports, 2021
We developed a method to improve protein thermostability, “loop-walking method”. Three consecutive positions in 12 loops of Burkholderia cepacia lipase were subjected to random mutagenesis to make 12 libraries.
Kazunori Yoshida, Shun Kawai, Masaya Fujitani, Satoshi Koikeda, Ryuji Kato, Tadashi Ema   +5 more
doaj   +1 more source

Enzyme activity and thermostability of a non-specific nuclease from Yersinia enterocolitica subsp. palearctica by site-directed mutagenesis

Electronic Journal of Biotechnology, 2016
Background: To identify the critical amino acid residues that contribute to the high enzyme activity and good thermostability of Yersinia enterocolitica subsp. palearctica (Y. NSN), 15 mutants of Y.
Yu Zhang, Zhen-Hua Li, Wei Zheng, Zhen-Xing Tang, Zhi-Liang Zhang, Lu-E Shi   +5 more
doaj   +1 more source

Taming nitroformate through encapsulation with nitrogen-rich hydrogen-bonded organic frameworks

Nature Communications, 2021
Nitroformate is an attractive oxidant compound in propellants and explosives but its poor thermostability prevents it from application. Here, the authors demonstrate that incorporation of nitroformate in a hydrogen-bonded organic framework increases the ...
Jichuan Zhang, Yongan Feng, Richard J. Staples, Jiaheng Zhang, Jean’ne M. Shreeve   +4 more
doaj   +1 more source

Improvement of thermostability and catalytic efficiency of glucoamylase from Talaromyces leycettanus JCM12802 via site-directed mutagenesis to enhance industrial saccharification applications

Biotechnology for Biofuels, 2021
Background Glucoamylase is an important industrial enzyme in the saccharification of starch into glucose. However, its poor thermostability and low catalytic efficiency limit its industrial saccharification applications.
Lige Tong, Jie Zheng, Xiao Wang, Xiaolu Wang, Huoqing Huang, Haomeng Yang, Tao Tu, Yuan Wang, Yingguo Bai, Bin Yao, Huiying Luo, Xing Qin   +11 more
doaj   +1 more source

Consensus design for improved thermostability of lipoxygenase from Anabaena sp. PCC 7120

BMC Biotechnology, 2018
Background Lipoxygenase (LOX) from Anabaena sp. PCC 7120 (Ana-rLOX) offers important applications in the food industry, especially for improving aroma and dough rheological properties.
Hui Qian, Chong Zhang, Zhaoxin Lu, Bingjie Xia, Xiaomei Bie, Haizhen Zhao, Fengxia Lu, Guang-Yu Yang   +7 more
doaj   +1 more source

Thermostability Improvement of L-Asparaginase from Acinetobacter soli via Consensus-Designed Cysteine Residue Substitution

Molecules, 2022
To extend the application range of L-asparaginase in food pre-processing, the thermostability improvement of the enzyme is essential. Herein, two non-conserved cysteine residues with easily oxidized free sulfhydryl groups, Cys8 and Cys283, of ...
Linshu Jiao, Huibing Chi, Bingjie Xia, Zhaoxin Lu, Xiaomei Bie, Haizhen Zhao, Fengxia Lu, Meirong Chen   +7 more
doaj   +1 more source

The Frequencies of Oppositely Charged, Uncharged Polar, and β-Branched Amino Acids Determine Proteins’ Thermostability

IEEE Access, 2020
Enhancing proteins' thermostability is an important aspect of enzyme engineering. Many studies have investigated the properties that determine the proteins' thermostability. However, no consensus has emerged.
Shanwen Sun, Chunyan Ao, Donghua Wang, Benzhi Dong   +3 more
doaj   +1 more source

Structural Rigidity and Protein Thermostability in Variants of Lipase A from Bacillus subtilis. [PDF]

PLoS ONE, 2015
Understanding the origin of thermostability is of fundamental importance in protein biochemistry. Opposing views on increased or decreased structural rigidity of the folded state have been put forward in this context.
Prakash Chandra Rathi, Karl-Erich Jaeger, Holger Gohlke   +2 more
doaj   +1 more source

Directed Evolution of Pseudomonas fluorescens Lipase Variants With Improved Thermostability Using Error-Prone PCR

Frontiers in Bioengineering and Biotechnology, 2020
Lipases catalyze the hydrolysis of fats and oils, and have been widely used in various industrial fields. However, bacterial lipases have a lower thermostability in industrial processes, which was a limiting factor in their industrial application.
Lijun Guan, Yang Gao, Jialei Li, Kunlun Wang, Zhihong Zhang, Song Yan, Nina Ji, Ye Zhou, Shuwen Lu   +8 more
doaj   +1 more source