Pseudoxanthomonas sp. WD12와 WD32의 세포외 단백질분해효소 특성 = Characterization of extracellular protease from Pseudoxanthomonas sp. WD12 and WD32

다국어 초록 (Multilingual Abstract)

Proteolytic enzymes perform hydrolysis of the peptide bonds in the protein and most commonly use in the industry. Pseudoxanthomonas sp. WD12 and WD32 were previously isolated as protease producers from a rotten wood sample. Here, we report the secreted proteolytic enzymes. The optimum enzyme reaction temperature for the secreted crude enzyme from the strain WD12 and WD32 were 50 oC at pH 9.0 and 45 oC at pH 8.0, respectively. The enzyme activities of both strains were increased by addition of KCl, NaCl, CaCl2 or MnSO4, and decreased by addition of AgNO3, CuSO4, FeCl3 or AlCl3. Secreted enzymes of both strains were most strongly inhibited by addition of FeCl3 or CuSO4. Taken together these results, WD12 could be a candidate strain of industrial alkaline protease production.

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