Purification and Substrate Specificity of Debaryomyces sp. α-Galactosidase by Mannobiose-Sepharose Affinity Column Chromatograpy
2006
Park, G.G. (Kyungwon University, Seongnam, Republic of Korea), E-mail: [email protected]
α-Galactosidase was partially purified from the culture filtrate of Debaryomyces sp. by Mannobiose-Sepharose affinity column chromatography. The galactosidase exhibited maximum activity at pH 4.0 and 60℃, and was stable in the pH and temperature ranges of 3 to 4.5 and 30 to 50℃, respectively. The enzyme was inhibited by Hg²+ and Ag²+. The enzyme activity was not affected considerably by treatment with other metal compounds. The enzyme hydrolyzed melibiose to galactose and glucose, raffinose to galactose and sucrose, and Gal³Man₃ (6³-α-galactosyl-1,4-mannotriose) to galactose and mannotriose.
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