Abstract
A β-galactosidase gene (PbBGal2A) was cloned from Paenibacillus barengoltzii and expressed in Escherichia coli. The in silico analysis of the deduced amino acid sequences revealed that PbBGal2A shared the highest identity of 40% with the characterized glycoside hydrolase (GH) family 2 β-galactosidase from Actinobacillus pleuropneumoniae. The recombinant β-galactosidase (PbBGal2A) was purified with a molecular mass of 124.2kDa on SDS-PAGE. The optimal pH and temperature of PbBGal2A were determined to be pH 7.5 and 45°C, respectively. PbBGal2A was stable within pH 6.0-8.0 and up to 45°C. It completely hydrolyzed the lactose in milk and whey powder solution. In addition, PbBGal2A exhibited high transglycosylation activity and a maximum yield of 47.9% (w/w) for galactooligosaccharides (GOS) production was obtained in 8h at a lactose concentration of 350g/L. These properties make PbBGal2A an ideal candidate for commercial use in the production of lactose-free milk and GOS.
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