Beta-galactosidases (EC 3.2.1.23) have attracted increasing attention due to their transgalactosylation potential to form prebiotic galacto-oligosaccharides (GOS). In this study, the coding region of a �-galactosidase (�-gal II) from Bifidobacterium breve was cloned and overexpressed in Escherichia coli. In addition to biochemical characterization, recombinant �-galactosidase was investigated in detail with respect to its propensity to transfer galactosyl moieties onto lactose, the primary hydrolysis products D-glucose and D-galactose, and certain sugar acceptors such as L-fucose, N-acetyl-D-galactosamine and N-acetyl-D-glucosamine under defined, initial-velocity conditions. The rate constant ratios determined for these different acceptors can be used as a measure for the ability of a certain substance to act as a galactosyl acceptor, which in turn allows an estimation of the transgalactosylation products obtained. Novel hetero-oligosacharides (HOS) are of interest because of a potentially extended functionality in addition to GOS. The resulting HOS mixture was analyzed using HPLC with pulsed amperometric detection and capillary electrophoresis.

Beta-galactosidase (β-gal II) from <i>Bifidobacterium breve</i> DSM 20213 for production of prebiotic galacto- and hetero-oligosaccharides

245th National Meeting (2013)

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Beta-galactosidase (β-gal II) from Bifidobacterium breve DSM 20213 for production of prebiotic galacto- and hetero-oligosaccharides