Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 55-60 |
| Journal | Applied Microbiology and Biotechnology |
| Volume | 61 |
| DOIs | |
| Publication status | Published - 2003 |
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Keywords
- intestinal microflora
- beta-galactosidase
- enzymatic methods
- oligosaccharides
- purification
- bacteria
- growth
- longum
- rats
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Cloning and characterization of two a-glucosidases from Bifidobacterium adolescentis DSM20083. / van den Broek, L.A.M.; Struijs, K.; Verdoes, J.C.; Beldman, G.; Voragen, A.G.J.
In: Applied Microbiology and Biotechnology, Vol. 61, 2003, p. 55-60.Research output: Contribution to journal › Article › Academic › peer-review
TY - JOUR
T1 - Cloning and characterization of two a-glucosidases from Bifidobacterium adolescentis DSM20083.
AU - van den Broek, L.A.M.
AU - Struijs, K.
AU - Verdoes, J.C.
AU - Beldman, G.
AU - Voragen, A.G.J.
PY - 2003
Y1 - 2003
N2 - Two alpha-glucosidase encoding genes (aglA and aglB) from Bifidobacterium adolescentis DSM 20083 were isolated and characterized. Both alpha-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-alpha-glucoside. The K,, for pnp-alpha-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-a-glucoside as substrate, the pH optimum for AglA was 6.6 and the temperature optimum was 37degreesC. For AglB, values of pH 6.8 and 47degreesC 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 a-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.
AB - Two alpha-glucosidase encoding genes (aglA and aglB) from Bifidobacterium adolescentis DSM 20083 were isolated and characterized. Both alpha-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-alpha-glucoside. The K,, for pnp-alpha-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-a-glucoside as substrate, the pH optimum for AglA was 6.6 and the temperature optimum was 37degreesC. For AglB, values of pH 6.8 and 47degreesC 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 a-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.
KW - intestinal microflora
KW - beta-galactosidase
KW - enzymatic methods
KW - oligosaccharides
KW - purification
KW - bacteria
KW - growth
KW - longum
KW - rats
U2 - 10.1007/s00253-002-1179-1
DO - 10.1007/s00253-002-1179-1
M3 - Article
VL - 61
SP - 55
EP - 60
JO - Applied Microbiology and Biotechnology
JF - Applied Microbiology and Biotechnology
SN - 0175-7598
ER -