alexa Purification and Characterization of Two Novel β-Galactosidases from Lactobacillus reuteri


Journal of Food & Industrial Microbiology

Author(s): Thuha Nguyen, Dietmar Haltrich, Klaus D Kulbe, Hans Peter Lettner, Wolfgang Kneifel, Marlene Steinbck, Barbara Splechtna

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The intracellular β-galactosidase (β-gal) enzymes from two strains of Lactobacillus reuteri, L103 and L461, were purified by ammonium sulfate fractionation, hydrophobic interaction, and affinity chromatography. Both enzymes are heterodimers with a molecular mass of 105 kDa, consisting of a 35 kDa subunit and a 72 kDa subunit. Active staining of L. reuteri L103 and L461 β-gal with 4-methylumbelliferyl β-d-galactoside showed that the intact enzymes as well as the larger subunits possess β-galactosidase activity. The isoelectric points of L. reuteri L461 and L103 β-gal were found to be in the range of 3.8−4.0 and 4.6−4.8, respectively. Both enzymes are most active in the pH range of 6−8; however, they are not stable at pH 8. The L. reuteri β-galactosidases are activated by various mono- and divalent cations, including Na+, K+, and Mn2+, and are moderately inhibited by their reaction products d-glucose and d-galactose. Because of their origin from beneficial and potentially probiotic lactobacilli, these enzymes could be of interest for the synthesis of prebiotic galacto-oligosaccharides.

This article was published in Journal of Agricultural and Food Chemistry and referenced in Journal of Food & Industrial Microbiology

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