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• W4200192018 endingPage "109" @default.
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• W4200192018 abstract "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 L9T) production from Ornithinibacillus caprae L9T was achieved through the one-factor-at-a-time approach and response surface methodological optimization. L9T 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+, Ca2+ and Sr2+, but was totally suppressed by 5 mM phenylmethylsulfonyl fluoride, which suggests that this enzyme belongs to the serine protease family. L9T 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, L9T 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 L9T protease in industrial applications, especially in leather processing." @default.
• W4200192018 created "2021-12-31" @default.
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• W4200192018 date "2022-01-28" @default.
• W4200192018 modified "2023-10-16" @default.
• W4200192018 title "Exoproduction and Biochemical Characterization of a Novel Serine Protease from <i>Ornithinibacillus caprae</i> L9^T with Hide-Dehairing Activity" @default.
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• W4200192018 doi "https://doi.org/10.4014/jmb.2108.08037" @default.
• W4200192018 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/34818664" @default.
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