Purification and Characterization of α-Galactosidase from Bifidibacterium longum

doi:10.7506/spkx1002-6630-201407024

Abstract

Abstract:

An α-galactosidase from Bifidibacterium longum KLDS2.0509 was purified by ammonium sulfate precipitationand Sephadex G-100 filtration chromatography, and its enzymatic properties were characterized. The molecular weightof the purified enzyme was approximately 45 kD as determined by SDS-PAGE. The optimal pH and temperature of theenzyme were pH 5.0 and 42 ℃, respectively. The α-galactosidase activity was not significantly influenced by most of theinvestigated metal ions, but slightly inhibited by Fe2+, Mn2+, Ag+ and Cu2+, and completely inhibited by Hg2+. This enzymewas able to degrade natural substrates such as melibiose, raffinose and stachyose, but could not degrade galactose-containingpolysaccharides.

Key words: Bifidibacterium longum, α-galactosidase, purification, enzymatic properties

CHEN Jun-liang, TIAN Fen, HUO Gui-cheng, ZHANG Hui-yun. Purification and Characterization of α-Galactosidase from Bifidibacterium longum[J]. FOOD SCIENCE, doi: 10.7506/spkx1002-6630-201407024.

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Purification and Characterization of α-Galactosidase from Bifidibacterium longum

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