Abstract.
Two α-glucosidase encoding genes (aglA and aglB) from Bifidobacterium adolescentis DSM 20083 were isolated and characterized. Both α-glucosidases belong to family 13 of the glycosyl hydrolases. Recombinant AglA (EC 3.2.1.10) and AglB (EC 3.2.1.20), expressed in Escherichia coli, showed high hydrolytic activity towards isomaltose and pnp-α-glucoside. The K m for pnp-α-glucoside was 1.05 and 0.47 mM and the V max was 228 and 113 U mg–1 for AglA and AglB, respectively. Using pnp-α-glucoside as substrate, the pH optimum for AglA was 6.6 and the temperature optimum was 37°C. For AglB, values of pH 6.8 and 47°C were found. AglA also showed high hydrolytic activity towards isomaltotriose and, to a lesser extent, towards trehalose. AglB has a high preference for maltose and less activity towards sucrose; minor activity was observed towards melizitose, low molecular weight dextrin, maltitol, and maltotriose. The recombinant α-glucosidases were tested for their transglucosylation activity. AglA was able to synthesize oligosaccharides from trehalose and sucrose. AglB formed oligosaccharides from sucrose, maltose, and melizitose.
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van den Broek, .L., Struijs, .K., Verdoes, .J. et al. Cloning and characterization of two α-glucosidases from Bifidobacterium adolescentis DSM20083. Appl Microbiol Biotechnol 61, 55–60 (2003). https://doi.org/10.1007/s00253-002-1179-1
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DOI: https://doi.org/10.1007/s00253-002-1179-1