Purification and Characterization of β-D-Glucosidases from Euphausia superba(Biological Chemistry)

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概要

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• Two β-glucosidases (EC 3.2.1.21) from Euphausia superba designated as I and II were purified by ammonium sulfate fractionation and chromatographies on DEAE-cellulose and Con A-Sepharose 4B. They had the following similar properties: pH optima at 6.0; temperature optima at 55℃; molecular weight of about 155,000; stability at low temperature in pH 5.6〜9; and kinetic parameters. Both enzymes had β-glucosidase, β-fucosidase, β-galactosidase, and β-xylosidase activities. Inhibition studies indicated that these four activities shared a common active site on β-glucosidase I. These two enzymes also had very low α-L-arabinosidase activities.

• 社団法人日本農芸化学会の論文
• 1986-05-23

著者

• Lian Kuang-tzung

  Institute Of Botany Academia Sinica

• Chen Ching-san

  Institute Of Botany Academia Sinica

関連論文

• Cloning, Expression and Purification of Bacillus cereus Endochitinase in the Escherichia coli AD494(DE3)pLysS Expression System
• Purification and Characterization of β-D-Glucosidases from Euphausia superba(Biological Chemistry)

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