Purification and Characterization of Amidase which Participates in Nitrile Degradation
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概要
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Amidase was purified from the cell-free extract of acetonitrile-grown Arthrobacter sp. J-1 by a procedure involving protamine sulfate precipitation, ammonium sulfate fractionation, and column chromatographies on DEAE-cellulose, hydroxyapatite and Sephadex G-200. The overall purification was 47-fold. The purified enzyme was homogeneous as judged by ultracentrifugal analysis and disc gel electrophoresis. The molecular weight of the enzyme was estimated to be about 300, 000 and 320, 000 by disc gel electrophoresis and gel filtration, respectively. The enzyme was possibly composed of eight identical subunits of a molecular weight of 39, 000. The isoelectric point was 3.8. The enzyme catalyzed the stoichiometric hydrolysis of acetamide to form acetic acid and ammonia. The enzyme was active toward acetamide, acrylamide and propionamide and the Km values were 0.97, 23.3 and 8.05 mM, respectively. The enzyme showed acyltransferase activity.
- 社団法人 日本農芸化学会の論文
著者
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Asano Yasuhisa
Department Of Agricultural Chemistry Kyoto University
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Tani Yoshiki
Department Of Agricultural Chemistry College Of Agriculture Kyoto University
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Yamada Hideaki
Department Of Agricultural Chemistry Faculty Of Agriculture Kyoto University
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TACHIBANA Mineo
Department of Agricultural Chemistry, Kyoto University
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