Structural and biochemical characterization of a novel thermophilic Coh01147 protease

Proteases play an essential role in living organisms and represent one of the largest groups of industrial enzymes. The aim of this work was recombinant production and characterization of a newly identified thermostable protease 1147 from thermophilum indigenous Cohnella sp. A01. Phylogenetic tree a...

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Veröffentlicht in:	PloS one 2020-06, Vol.15 (6), p.e0234958-e0234958
Hauptverfasser:	Tarrahimofrad, Hossein, Meimandipour, Amir, Arjmand, Sareh, Beigi Nassiri, Mohammadtaghi, Jahangirian, Ehsan, Tavana, Hossein, Zamani, Javad, Rahimnahal, Somayyeh, Aminzadeh, Saeed, Lesner, Adam, Ho, Paulo Lee
Format:	Artikel
Sprache:	eng
Schlagworte:	Affinity chromatography Algorithms Amino acids Animal sciences Binding sites Biology and Life Sciences Biotechnology Cadmium Casein Chemical properties Chromatography Cobalt Computer simulation Crystal structure Cysteine Cysteine proteinase Deactivation Deoxyribonucleic acid DNA E coli Enzymes Escherichia coli Fluorescence Food science Gel electrophoresis Genetic engineering Hydrogen Hydrogen bonding Hydrogen bonds Inactivation Ligands Manufacturing Metal ions Microbial enzymes Microorganisms Molecular docking Molecular dynamics Natural resources PARK7 protein pH effects Phylogenetics Phylogeny Physical Sciences Physiological aspects Protease Protease inhibitors Proteases Protein structure Proteinase inhibitors Proteins Research and Analysis Methods Simulation Sodium lauryl sulfate Structural analysis Structure Substrates Tertiary structure Thermal shock Thermophiles Zoology
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