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This study is the first report on production and characterization of the enzyme from an Ornithinibacillus species. A 4.2-fold increase in the extracellular protease (called L9 T ) production from Ornithinibacillus caprae L9 T was achieved through the one-factor-at-a-time approach and response surface methodological optimization. L9 T protease exhibited a unique protein band with a mass of 25.9 kDa upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This novel protease was active over a range of pH (4-13), temperatures (30-80°C) and salt concentrations (0-220 g/l), with the maximal activity observed at pH 7, 70°C and 20 g/l NaCl. Proteolytic activity was upgraded in the presence of Ag + , Ca 2+ and Sr 2+ , but was totally suppressed by 5 mM phenylmethylsulfonyl fluoride, which suggests that this enzyme belongs to the serine protease family. L9 T protease was resistant to certain common organic solvents and surfactants; particularly, 5 mM Tween 20 and Tween 80 improved the activity by 63 and 15%, respectively. More importantly, L9 T protease was found to be effective in dehairing of goatskins, cowhides and rabbit-skins without damaging the collagen fibers. These properties confirm the feasibility of L9 T protease in industrial applications, especially in leather processing.

journal of microbiology and biotechnology

Exoproduction and Biochemical Characterization of a Novel Serine Protease from <i>Ornithinibacillus caprae</i> L9<sup>T</sup> with Hide-Dehairing Activity

Exoproduction and Biochemical Characterization of a Novel Serine Protease from Ornithinibacillus caprae L9T with Hide-Dehairing Activity

Exoproduction and Biochemical Characterization of a Novel Serine Protease from Ornithinibacillus caprae L9^T with Hide-Dehairing Activity