Purification and Properties of Cyclodextrin Glucanotransferase from Brevibacterium sp. No. 9605
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概要
- 論文の詳細を見る
Cyclodextrin glucanotransferase (EC 2.4.1.19) from Brevibacterium sp. No.9605 was purified to homogeneity by chromatography on butyl-Toyopearl 650M, γ-cyclodextrin-Sepharose 4B, and Toyopearl HW-55S. The molecular weight of the purified enzyme was estimated to be 75,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The isoelectric point of the purified enzyme was 2.8. The optimum pH and temperature were pH 10 and 45℃, respectively. The enzyme was stable at the range of pH 6-8and at temperatures 50℃ or less in the presence of CaCl_2. The enzyme produced mainly γ-cyclodextrin from starch in the initial stage of reaction, but later, the proportion of β-cyclodextrin was increased.
- 社団法人日本農芸化学会の論文
- 1994-11-23
著者
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KITAHATA Sumio
Osaka Municipal Technical Research Institute
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Kitahata S
Department Of Bioscience And Biotecnology Shinshu University
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MORI SHIGEHARU
Research and Development Division, Amano Pharmaceutical Co. Ltd.,
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Oya Takaichi
Amano Pharmaceutical Co. Ltd.
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Mori S
Sagami Chemical Res. Center Kanagawa Jpn
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Mori Shigeharu
Amano Enzyme
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Hirose Susumu
Amano Pharmaceutical Co. Ltd.
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