Purification and Some Properties of Chitinases from Aeromonas sp. No. 10S-24
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概要
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Chitinases I and II were purified from the culture supernatant of Aeromonas sp. 10S-24 by ammonium sulfate precipitation, SP-Sephadex C-50 chromatography, Sephacryl S-200 gel filtration, and chromatofocusing. Both enzymes were most active at pH 4.0 and the optimum temperature for I and II were 50℃ and 60℃. Chitinase I was stable at pHs between 4 and 9 and at temperatures below 50℃ and chitinase II was stable at pHs between 5 and 7 and at temperatures below 45℃. The molecular weights were estimated by SDS polyacrylamide gel electrophoresis to be 112,000 and 115,000 for I and II respectively, while gel filtration showed the molecular weight to be 114,000 for both types of the enzyme. The pIs for I and II were 7.9 and 8.1,respectively. The activities of both enzymes were inhibited by Ag^+ and iodoacetic acid.
- 社団法人日本農芸化学会の論文
- 1992-03-23
著者
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Arai Motoo
Department of Agricultural Chemistry, College of Agriculture, University of Osaka Prefecture
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UEDA MITSUHIRO
Department of Applied Biological Chemistry, College of Agriculture, Osaka Prefecture University
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Arai Motoo
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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Ueda Mitsuhiro
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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