Characterization of extracellular protease from Bacillus pumilus I7
Summary: Proteases (also termed peptidase or proteinase) are the most important industrial enzymes, they occur naturally in all living organisms. A protease is an enzyme that conducts proteolysis, that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in the polypeptide chain forming the protein. Therefore, these enzymes have been widely used in many industrial fields such as food processing, leather processing, weaving processing, pharmaceutical industry, waste management, washing detergent, and chemical industry. They account for approximately 40% of the total enzyme sale markets in above applications. Bacillus pumilus strain I7, which produces extracellular protease, was isolated from wastewater of abattoir in Hue, Vietnam. Total and specific activities of protease from B. pumilus I7 reached a maximum value of 64.8 unit/ml and 179 unit/mg, respectively, after 22 hours of culture in medium containing 1% soybean, 1% soluble starch, 0.1% KH2PO4, 0.02% MgSO4 and 0.5% NaCl. Protease from B. pumilus I7 strongly operated at pH 8 and 50oC. Mn2+ ion stimulated an increase of protease activity at 0.5 mM concentration, whereas various ions (Hg2+, Fe3+, Cu2+, Ca2+, Mg2+, Na+, Zn2+, and Co2+) inhibited its activity. Protease from B. pumilus I7 was completely prohibited by SDS (sodium dodecyl sulfate). However, PMSF (phenylmethane sulfonyl fluoride), EDTA (ethylenediaminetetraacetic acid), H2O2 (hydrogen peroxide) and Tween 20 partially inhibited this enzyme’s activity. SDS-PAGE (SDS-polyacrylamide gel electrophoresis) with 0.5% casein showed three proteolytic bands. These bands were in the position of proteins with molecular weights of approximately 97, 65 and 48 kDa.
Type: Domestic
Author: Cù Lê Nguyên, Trần Nguyên Thảo, Nguyễn Đức Huy, Hoàng Tấn Quảng, Nghiêm văn Tùng, Nguyễn Hoàng Lộc
Unit: Director board of Institute, Laboratory of Gene technology
Journal:Tạp chí Công nghệ Sinh học
Issue, Number, Pages10, 4A, 825-831
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Year of publication: 2012
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