Characterization of Two Novel α-Glucosidases fromBifidobacterium breveUCC2003
Open Access
- 15 February 2009
- journal article
- research article
- Published by American Society for Microbiology in Applied and Environmental Microbiology
- Vol. 75 (4), 1135-1143
- https://doi.org/10.1128/aem.02391-08
Abstract
Two α-glucosidase-encoding genes (agl1andagl2) fromBifidobacterium breveUCC2003 were identified and characterized. Based on their similarity to characterized carbohydrate hydrolases, the Agl1 and Agl2 enzymes are both assigned to a subgroup of the glycosyl hydrolase family 13, the α-1,6-glucosidases (EC 3.2.1.10). Recombinant Agl1 and Agl2 into which a His12sequence was incorporated (Agl1Hisand Agl2His, respectively) exhibited hydrolytic activity towards panose, isomaltose, isomaltotriose, and four sucrose isomers—palatinose, trehalulose, turanose, and maltulose—while also degrading trehalose and, to a lesser extent, nigerose. The preferred substrates for both enzymes were panose, isomaltose, and trehalulose. Furthermore, the pH and temperature optima for both enzymes were determined, showing that Agl1Hisexhibits higher thermo and pH optima than Agl2His. The two purified α-1,6-glucosidases were also shown to have transglycosylation activity, synthesizing oligosaccharides from palatinose, trehalulose, trehalose, panose, and isomaltotriose.Keywords
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