Purification of a Latent Form of Polyphenoloxidase from La France Pear Fruit and Its Pressure- activation
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概要
- 論文の詳細を見る
A latent form, mostly soluble, of polyphenoloxidase of La France pear fruit (Pyrus communis) was purified to homogeneity by ammonium sulfate fractionation and anion-exchange chromatography with DEAE-Sephadex A-25 and then DEAE-Toyopearl 650M, followed by gel permeation chromatography with Toyopearl HW-55s. The addition of 10% glycerol to the eluting buffer was needed for purification. The purified latent enzyme seemed to be a monomeric protein ; the molecular weight was estimated to be 70, 000 by gel permeation chromatography and 65, 000 by SDS-polyacrylamide gel electrophoresis. The enzyme was activated by pressurization at 400MPa or higher or by treatment with SDS. The highest activity was obtained by pressurization at 600MPa and 20℃ for 6h.
- 社団法人日本農芸化学会の論文
- 1994-08-23
著者
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AOYAMA Yoritaka
Division of Applied Bioscience, Graduate School of Agriculture, Hokkaido University
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Aoyama Y
Hokkaido Univ. Sapporo Jpn
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HAYASHI Rikimaru
Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University
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Asaka Masashi
Toyo Institute of Food Technology
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Aoyama Yoshio
Toyo Institute of Food Technology
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Nakanishi Ritsuko
Toyo Institute of Food Technology
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Hayashi R
Laboratory Of Biomacromolecular Chemistry Division Of Applied Life Sciences The Graduate School Of A
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Hayashi R
Kyoto Univ. Kyoto
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Hayashi Rikimaru
Department Of Agricultural Chemistry Faculty Of Agriculture Kyoto University
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