Characterization of detergent compatible protease of a halophilic Bacillus sp. EMB9: differential role of metal ions in stability and activity
R Sinha, SK Khare - Bioresource technology, 2013 - Elsevier
A moderately halophilic protease producer, Bacillus sp. strain isolated from sea water is
described. The protease is purified to homogeneity by ammonium sulphate precipitation and
CM cellulose chromatography. The serine protease has a molecular mass of 29 kDa.
Enzymatic characterization of protease revealed K m 2.22 mg mL− 1, V max 1111.11 U mL−
1, pH optimum 9.0, t 1/2 190 min at 60° C and salt optima 1%(w/v) NaCl. The protease is
remarkably stable in hydrophilic and hydrophobic solvents at high concentrations. The …
described. The protease is purified to homogeneity by ammonium sulphate precipitation and
CM cellulose chromatography. The serine protease has a molecular mass of 29 kDa.
Enzymatic characterization of protease revealed K m 2.22 mg mL− 1, V max 1111.11 U mL−
1, pH optimum 9.0, t 1/2 190 min at 60° C and salt optima 1%(w/v) NaCl. The protease is
remarkably stable in hydrophilic and hydrophobic solvents at high concentrations. The …
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