Purification and Properties of Oxidized Poly(vinyl alcohol)- Degrading Enzyme
Purification and Properties of Oxidized Poly(vinyl alcohol)- Degrading Enzyme
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DOI:
10.1271/bbb1961.45.63
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发表时间:
1981-07
期刊:
影响因子:
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通讯作者:
K. Sakai;M. Morita;N. Hamada;Yasuto Watanabe
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文献类型:
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作者:
K. Sakai;M. Morita;N. Hamada;Yasuto Watanabe
An enzyme catalyzing the degradation of secondary alcohol oxidase-oxidized poly(vinyl alcohol), in which hydroxyl groups of poly(vinyl alcohol) are partially converted to keto groups, was purified to an electrophoretically homogeneous state from a mixed culture broth of at least three different soil bacteria. The enzyme was active to the oxidized poly(vinyl alcohol), but not to intact poly(vinyl alcohol) and to a variety of examined low molecular weight keto compounds. The enzyme was, therefore, tentatively called oxidized poly(vinyl alcohol)-degrading enzyme. The enzyme was a single polypeptide having a molecular weight of 38,000. The N- and C-terminal amino acids were alanine and threonine, respectively. The isoelectric point was pH 10.0. The optimum pH for activity was 6.5 and the optimum temperature 45°C. The enzyme activity was inhibited by Hg2+ and recovered by reduced glutathione, although p-chloromercuribenzoate had no effect. The enzyme reaction on oxidized poly(vinyl alcohol) required neither ox...