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Nguyen, TH; Splechtna, B; Steinböck, M; Kneifel, W; Lettner, HP; Kulbe, KD; Haltrich, D.
(2006): Purification and characterization of two novel beta-galactosidases from Lactobacillus reuteri.
J Agric Food Chem. 2006; 54(14):4989-4998 FullText FullText_BOKU

The intracellular beta-galactosidase (beta-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 beta-gal with 4-methylumbelliferyl, beta-D-galactoside showed that the intact enzymes as well as the larger subunits possess,- galactosidase activity. The isoelectric points of L. reuteri L461 and L103,- 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,- 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 galactooligosaccharides.
Authors BOKU Wien:
Domig Konrad
Haltrich Dietmar
Kneifel Wolfgang
Kulbe Klaus Dieter
Nguyen Thu Ha
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Cations -
Dimerization -
Enzyme Stability -
Fermentation -
Hydrogen-Ion Concentration -
Isoelectric Point -
Kinetics -
Lactobacillus reuteri - enzymology
Molecular Weight - enzymology
beta-Galactosidase - chemistry

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