Cohnella 1759 cysteine protease shows significant long term half-life and impressive increased activity in presence of some chemical reagents.

Saghian, Rayan; Mokhtari, Elham; Aminzadeh, Saeed

Saghian, Rayan; Mokhtari, Elham; Aminzadeh, Saeed.

Affiliation

Saghian R; Bioprocess Engineering Group, Institute of Industrial and Environmental Biotechnology, National Institute of Genetic Engineering and Biotechnology (NIGEB), Tehran, Iran.
Mokhtari E; Bioprocess Engineering Group, Institute of Industrial and Environmental Biotechnology, National Institute of Genetic Engineering and Biotechnology (NIGEB), Tehran, Iran.
Aminzadeh S; Bioprocess Engineering Group, Institute of Industrial and Environmental Biotechnology, National Institute of Genetic Engineering and Biotechnology (NIGEB), Tehran, Iran. aminzade@nigeb.ac.ir.

Sci Rep ; 11(1): 4573, 2021 02 25.

Article in En | MEDLINE | ID: mdl-33633359

Subject(s)

Bacillales/enzymology; Cysteine Proteases/metabolism; Amino Acid Sequence; Bacillales/drug effects; Bacillales/genetics; Binding Sites; Cysteine Proteases/chemistry; Cysteine Proteases/genetics; Enzyme Activation/drug effects; Enzyme Stability/drug effects; Hydrogen-Ion Concentration; Molecular Docking Simulation; Molecular Dynamics Simulation; Phylogeny; Protein Binding; Protein Conformation; Sequence Analysis, DNA; Structure-Activity Relationship; Temperature

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacillales / Cysteine Proteases Language: En Journal: Sci Rep Year: 2021 Document type: Article Affiliation country: Iran Country of publication: United kingdom

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