Purification and Characterization of an Alkaline Proteinase Produced by Pimelobacter sp. Z-483
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概要
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An extracellular alaline proteinase was purified from the culture filtrate of Pimelobacter sp. Z-483. The molecular mass of the purifiewd enzyme was estimated to be approximetely 23 kDa by SDS-PAGE and 27 kDa be gel filtration. The optimum pH and temperature for the hydrolysis of casein were approximetely 9 and 50℃, respectively. The enzyme activity was strongly inhibited by 1,10-phenanthroline and mercury chloride, but not by EDTA, phosphoramidon and Zincov. The amino terminal sequence of the enzyme was similar to that of an alkaline elastase (MAP1) from Myxococcus xanthus. However, the specificity of the alkaline proteinase in the cleavage of the oxidized insullin B-chain was different from those of the Myxococcus enzyme and animal elastase.
- 社団法人日本生物工学会の論文
- 1997-10-25
著者
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Murao Sawao
Department of Agricultural Chemistry, College of Agriculture, University of Osaka Prefecture
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Oyama Hiroshi
Department Of Applied Biology Faculty Of Textile Science Kyoto Institute Of Technology
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Oyama Hiroshi
Department Of Applied Microbial Technology The Kumamoto Institute Of Technology
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Murao Sawao
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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KINJOH MITSURU
Department of Applied Microbial Technology, The Kumamoto Institute of Technology
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WATARI MITSUNORI
Department of Applied Microbial Technology, The Kumamoto Institute of Technology
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Watari Mitsunori
Department Of Applied Microbial Technology The Kumamoto Institute Of Technology
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Kinjoh Mitsuru
Department Of Applied Microbial Technology The Kumamoto Institute Of Technology
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