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• W3029193261 abstract "The proteolytic strain Bacillus cereus-S6-3 was subjected to mutagenic treatments viz. UV irradiations and methyl methane sulfonate (MMS). The obtained mutant strain, B. cereus-S6-3/UM90 showed 1.34 fold over the parent strain. Molecular characterization of proteases from the parent (PP/S6-3) and mutant (PM/UM90) strains indicated that they were consisted of two domains and binds a zinc ion and 4 calcium ions in the active site. Amino acid sequence alignment of PM/UM90 protease showed 19 amino acid residues were substituted compared to that of the wild-type enzyme. However, both proteases contained equal number of aromatic and hydrophobic amino acids. Protease from PM/UM90 showed an effective improvement in thermal properties in terms of reaction temperature, t1/2, the values of kd, activation energy (Ea), and decimal reduction time (D) within the temperature range from 60 to 80 °C. In addition, the kinetic and thermodynamic parameters for substrate hydrolysis (i.e., Km, Vmax, ΔH*, ΔG*, ΔS*, kcat, Vmax/Km, kcat/Km, ΔG*E–T and ΔG*E–S) showed a significant improvement of the catalytic efficiency for PM/UM90 protease. Furthermore, the correlation between thermodynamic properties and the patterns of amino acid substitution of wild-type enzyme to has been discussed." @default.
• W3029193261 created "2020-06-05" @default.
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• W3029193261 date "2020-10-01" @default.
• W3029193261 modified "2023-09-27" @default.
• W3029193261 title "Molecular characterization, catalytic, kinetic and thermodynamic properties of protease produced by a mutant of Bacillus cereus-S6-3" @default.
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• W3029193261 doi "https://doi.org/10.1016/j.ijbiomac.2020.05.241" @default.
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