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( Xiaoguang Li ),( Qian Zhang ),( Longzhan Gan ),( Guangyang Jiang ),( Yongqiang Tian ),( Bi Shi ) 한국미생물 · 생명공학회 2022 Journal of microbiology and biotechnology Vol.32 No.1
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<sup>T</sup>) production from Ornithinibacillus caprae L9<sup>T</sup> 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℃) and salt concentrations (0-220 g/l), with the maximal activity observed at pH 7, 70℃ and 20 g/l NaCl. Proteolytic activity was upgraded in the presence of Ag<sup>+</sup>, Ca<sup>2+</sup> and Sr<sup>2+</sup>, but was totally suppressed by 5 mM phenylmethylsulfonyl fluoride, which suggests that this enzyme belongs to the serine protease family. L9<sup>T</sup> 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<sup>T</sup> 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<sup>T</sup> protease in industrial applications, especially in leather processing.