Results 11 to 20 of about 55,424 (301)

Enhancing the thermostability of Streptomyces cyaneofuscatus strain Ms1 tyrosinase by multi-factors rational design and molecular dynamics simulations.

PLoS ONE, 2023
This study presents a multi-factor rational design strategy combined with molecular dynamics simulation to improve the thermostability of Streptomyces cyaneofuscatus strain Ms1 tyrosinase.
Zhengtao Li, Chen Zhao, Duanhua Li, Lu Wang   +3 more
doaj   +1 more source

Improved thermostability of creatinase from Alcaligenes Faecalis through non-biased phylogenetic consensus-guided mutagenesis

Microbial Cell Factories, 2020
Background Enzymatic quantification of creatinine has become an essential method for clinical evaluation of renal function. Although creatinase (CR) is frequently used for this purpose, its poor thermostability severely limits industrial applications ...
Xue Bai, Daixi Li, Fuqiang Ma, Xi Deng, Manjie Luo, Yan Feng, Guangyu Yang   +6 more
doaj   +1 more source

Thermostable Endotoxin of Rickettsiae [PDF]

Nature, 1946
Kligler and Oleinik1 reported the presence of a labile toxin in yolksac cultures of Rickettsise. The following experiments were designed in order to test whether the toxic effects of Rickettsiae are wholly brought about by this labile toxin, or are due also to the action of a thermostable toxin.
L. OLITZKI, E. OLEINIK, J. W. CZACZKES, A. KUTZENOK   +3 more
openaire   +2 more sources

Directed evolution converts subtilisin E into a functional equivalent of thermitase [PDF]

, 1999
We used directed evolution to convert Bacillus subtilis subtilisin E into an enzyme functionally equivalent to its thermophilic homolog thermitase from Thermoactinomyces vulgaris.
Arnold, Frances H., Zhao, Huimin
core   +2 more sources

Enzyme thermostability and thermoactivity [PDF]

"Protein Engineering, Design and Selection", 1996
Proteins from hyperthermophilic micro-organisms (living at >85°C) are thermostable in that they are usually able to withstand temperatures that would rapidly denature most proteins from mesophiles (living at 20-40°C) such as Escherichia coli or humans. In most cases, the stability is intrinsic to the protein, although in some hyperthermophilic Archaea ...
M J, Danson, D W, Hough, R J, Russell, G L, Taylor, L, Pearl   +4 more
openaire   +2 more sources

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

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

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

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

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