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Rudra,Majhighariani Institute of Science and Technology
Indian Journal of Biotechnology | Year: 2010

α-Galactosidase from Penicillium purpurogenum was induced to a greater extent in the culture medium by arabinose, galactose, lactose and guar galactomannan. The enzyme was purified by acetone precipitation and DEAE-Sephacel column chromatography. The purified enzyme showed a single band in both native-PAGE and SDS-PAGE. The molecular mass of enzyme was found to be between 107 and 110 kDa. The enzyme exhibited the optimum pH and temperature at 5.0 and 55°C, respectively. α-Galactosidase was strongly inhibited by Ag+ and Hg2+, while Fe2+ enhanced the activity. PMSF did not inhibit α-galactosidase activity, whereas N-bromosuccinimide completely inhibited the enzyme activity. Further, galactose and melibiose moderately inhibited the enzyme activity. The Km values for PNPG, melibiose, raffinose and stachyose were found to be 0.20, 5.26, 10 and 9.1, respectively. α-Galactosidase completely hydrolyzed flatulence-causing raffinose and stachyose of soymilk in 1.45 h.

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