Abstract
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°C; 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.
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