The biotechnological potential of subtilisin-like fibrinolytic enzyme from a newly isolated Lactobacillus plantarum KSK-II in blood destaining and antimicrobials

摘要: An antimicrobial oxidative- and SDS-stable fibrinolytic alkaline protease designated as KSK-II was produced by Lactobacillus plantarum isolated from kishk, a traditional Egyptian food. Maximum enzyme productivity obtained in medium containing 1% lactose 0.5% soybean flour carbon nitrogen sources, respectively. Purification of increased its specific activity to 1,140-fold with recovery 33% molecular weight 43.6 kDa. Enzyme totally lost the presence ethylenediaminetetraacetic acid restored after addition Fe2+ suggesting that is metalloprotease acts cofactor. hydrolyzed not only natural proteins but also synthetic substrates, particularly Suc-Ala-Ala-Pro-Phe-pNA. can hydrolyze Lys-X easier than Arg-X; thus, it considered subtilisin-family protease. Its apparent Km, Vmax, Kcat were 0.41 mM, 6.4 µmol mg−1 min−1, 28.0 s−1, industrially important perspectives maximal at 50°C (stable up 70°C), ability function pH (10.0), stability broad ranges (7.5–12.0) toward SDS, H2O2, organic solvents, detergents. We emphasize for first time potential proteases used detergents especially blood destaining. © 2014 American Institute Chemical Engineers Biotechnol. Prog., 31:316–324, 2015