A genomic library of Bifidobacterium adolescentis was constructed in Escherichia coli and a gene encoding an alpha-galactosidase was isolated. The identified open reading frame showed high similarity and identity with bacterial alpha-galactosidases, which belong to Family 36 of the glycosyl hydrolases. For the purification of the enzyme from the medium a single chromatography step was sufficient. The yield of the recombinant enzyme was 100 times higher than from B. adolescentis itself. In addition to hydrolytic activity the alpha-galactosidase showed transglycosylation activity and can be used for the production of alpha-galacto-oligosaccharides.