Debranching Enzymes of Potato Tubers (Solanum tuberosum L.). I. Purification and Some Properties of Potato Isoamylase
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概要
- 論文の詳細を見る
Potato tubers contain 3 debranching enzymes separable by polyacrylamide gel electrophoresis. One of them, isoamylase, has been purified to apparent homogeneity on disc gel electrophoresis by isoelectric precipitation, fractionation with ammonium sulfate, gel filtration on Sepharose 6B and finally affinity chromatography on Sepharose 4B-soluble starch, successively. The purified enzyme has a specific activity of 8.0U/mg of protein. It hydrolyzes the α-1, 6-glucosidic bonds in glycogen and phytoglycogen not only as rapidly as those in amylopectin but also completely, but cannot hydrolyze pullulan. From these results potato isoamylase was found to have the same substrate specificity as that of Pseudomonas isoamylase. However, different from the latter, it has an optimum pH of 5.5-6.0, optimum temperature of 50°C and was reversibly inactivated by p-chloromercuri-benzoate.
- 社団法人 日本農芸化学会の論文
著者
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Maruyama Yoshiharu
Department Of Agricultural Chemistry Faculty Of Agriculture The University Of Tokyo
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Nakamura Michinori
Department Of Agricultural Chemistry Faculty Ofagriculture The University Of Tokyo
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TANIGUCHI Hajime
Department of Agricultural Chemistry, The University of Tokyo:(Present office)National Food Reserach Institute
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ISHIZAKI Yukuo
Department of Agricultural Chemistry, The University of Tokyo
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TANIGUCHI Hajime
Department of Agricultural Chemistry, The University of Tokyo
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