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박인재,JerngChangYoon,SeongJooPark,EungHoKim,Yeon-JaeCho,Kwang-SooShin 한국미생물학회 2003 The journal of microbiology Vol.41 No.2
Four proteolytic bacteria were isolated and identified from a rotating biological contactor based on Bacillus. The four isolates, Ni 26, 36, 39 and 49 were identified as B. vallismortis, B. subtilis, Aeromonas hydrophila and B. amyloliquefaciens, respectively, based on their biochemical properties and 16S rDNA sequence analyses. The optimal proteolytic activity was observed in the temperature and pH ranges of 40-70ºC and 8.0-8.5, respectively. The proteolytic activities of all the isolates were partially inhibited by phenylmethylsulfonylfluoride (PMSF), and the isolates Ni 26, Ni 39 and Ni 49 were inhibited by the metalloprotease inhibitor, 1,10-phenanthroline. Zymographic analyses of the culture supernatants revealed the presence of at least two proteases in all isolates.
Soo-JinCho,Jong-HoPark,SeongJooPark,Jong-SoonLim,EungHoKim,Yeon-JaeCho,Kwang-SooShin 한국미생물학회 2003 The journal of microbiology Vol.41 No.3
Extracellular protease, from Aeromonas hydrophila Ni 39, was purified 16.7-fold to electrophoretic homogeneity with an overall yield of 19.9%, through a purification procedure of acetone precipitation, and Q Sepharose and Sephacryl S-200 chromatographies. The isoelectric point of the enzyme was 6.0 and the molecular mass, as determined by Sephacryl S-200 HR chromatography, was found to be about 102 kDa. SDS/PAGE revealed that the enzyme consisted of two subunits, with molecular masses of 65.9 kDa. Under standard assay conditions, the apparent Km value of the enzyme toward casein was 0.32 mg/ml. About 90% of the proteolytic activity remained after heating at 60oC for 30 min. The highest rate of azocasein hydrolysis for the enzyme was reached at 60oC, and the optimum pH of the enzyme was 9.0. The enzyme was inhibited by the serine protease inhibitor, phenylmethylsulfonyl fluoride (PMSF), by about 87.9%, but not by E64, EDTA, pepstatin or 1,10-phenanthroline. The enzyme activity was inhibited slightly by Ca2+, Mg2+ and Zn2+ ions.