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Extracellular protease from culture supernatants of Streptomyces sp. LCJ12A was purified and characterized in this study. The collected supernatant of Streptomyces sp. LCJ12A was purified by ammonium sulfate precipitation and diethylaminoethyl cellulose chromatography. The molecular weight of the enzyme was 20.1 kDa. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis was used to determine the molecular weight of the enzyme. The culture filtrate, partially purified enzyme, and ammonium sulfate precipitate displayed catalysis and stability over pH 3–11.5 and showed optimal activity at pH 10. The culture filtrate, ammonium sulfate precipitate, and partially purified enzyme were good between 30 and 40°C and the optimum temperature was 35°C. The purified protease exhibited high catalytic activity and stability under different pH and temperature. The partially purified protease from Streptomyces sp. LCJ12A showed a substantial relative activity of 78% with bovine serum albumin (BSA), 43% with gelatin, and 96% relative activity with casein. Lineweaver–Burk plot was used to calculate the Km and Vmax values for the partially purified protease. The Km values of Streptomyces sp. LCJ12A were 73.5 mM for casein, 44.54 mM for BSA, and 43.45 mM for gelatin. The Vmax values were 500 mM min−1 for casein, 303.03 mM min−1 for BSA, and 270.27 mM min−1 for gelatin from Streptomyces sp. LCJ12A. The statistical analysis confirmed that compared to the other substrates, casein was significant.

Purification and characterization of extracellular alkaline protease from Streptomyces sp. LCJ12A isolated from Pichavaram mangroves