Purification and Properties of an exo-α-Amylase from Pseudomonas stutzeri
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概要
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A maltotetraose-forming amylase from Pseudomonas stutzeri was highly purified by adsorption on starch granules and by chromatographies on Sephadex G-100 and DEAE-cellulose. The purified enzyme showed a single band in polyacrylamide gel electrophoreses with or without sodium dodecylsulfate. The optimum pH for enzyme action on starch was 6.0-6.5, and the optimum temperature was 45°C. The purified enzyme attacked starch from the non-reducing end to produce α-anomer oligosaccharides. This indicated that the enzyme was an exo-α-amylase which had not hitherto been found. The enzyme activity was markedly inhibited by the addition of Cu2+, Hg2+, N-bromosuccinimide and 2, 3-butanedione. The molecular weight of the enzyme determined by the method of Weber and Osborn was about 5.7×104. The isoelectric point of the enzyme was estimated to be 5.3 by polyacrylamide gel electrofocusing. The Km and ko values of this enzyme for starch, glycogen, short chain amylose and some maltooligosaccharides were calculated from Lineweaver-Burk plots.
- 社団法人 日本農芸化学会の論文
著者
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KOBAYASHI Tsuneo
Laboratory of Biological Chemistry, Department of Agricultural Chemistry, Faculty of Agriculture, To
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Sakano Yoshiyuki
Laboratory Of Biochemistry Department Of Agricultural Chemistry Tokyo University Of Agriculture And
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KASHIWAGI Yutaka
Laboratory of Biochemistry, Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology
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SAKANO Yoshiyuki
Laboratory of Biochemistry, Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology
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KOBAYASHI Tsuneo
Laboratory of Biochemistry, Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology
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