%0 Journal Article
%T Partial purification and characterization of a thermostable alkaline protease from Lactobacillus brevis
%A Femi-Ola
%A T.O.
%A Oladokun
%A D.O.
%J Malaysian Journal of Microbiology
%D 2012
%I Malaysian Society for Microbiology
%X Aims: The research was done to study the partial purification and characterization of thermostable alkaline protease from Lactobacillus brevis.Methodology and Results: The enzyme was purified in a two-step procedure involving ammonium sulphate precipitation and Sephadex G-150 gel permeation chromatography. The protease was purified 8.04 fold with a yield of approximately 30% after purification with Sephadex G-150 column. It has a relative molecular weight of 33.2 kDa and optimally active at a temperature of 60 oC and pH 9.0. The maximum velocity Vmax and Michaelis constant Km of the protease produced during the hydrolysis of casein were 66.66 U/mg protein and 3.33 mg/ml. It was strongly activated by Ca2+ and ethylene diamine tetra acetic acid (EDTA), mildly inhibited by Na+, K+, Mg2+ and Fe2+ and strongly inhibited by Cu2+ and Hg2+. The ability of the enzyme to improve the cleansing power of various detergents was also studied. Conclusion, significance and impact of study: The findings in this study suggest that the protease is a suitable candidate for detergent formulation and biotechnological applications.
%K Protease
%K Lactobacillus
%K Alkaline
%K Inhibitors
%K Detergent
%U http://web.usm.my/mjm/issues/vol8no1/Research%201.pdf