Purification and Characterization of Extracellular β-Galactosidase Secreted by Supension Cultured Rice (Oryza sativa L.) Cells(Biochemistry & Molecular Biology)
スポンサーリンク
概要
- 論文の詳細を見る
A β-galactosidase was purified 1300-fold by lactosyl-Sepharose 4B and Sephacryl S-200 column chromatographies from the cultured medium of a rice-cell suspension. The purified enzyme appeared as 47 kD and 40 kD polypeptides on SDS-PAGE and had a specific activity of 65.1 units/mg. Optimum activity was observed at pH 3.5 and 60℃. The enzyme released galactose from galactoxyloglucan and pectic galactans.
- 2003-03-23
著者
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KOBAYASHI Hideyuki
National Astronomical Observatory of Japan
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Kaneko Satoshi
National Food Res. Inst.
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Kobayashi Hideyuki
National Food Research Institute
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