3,000 Units at 40oC
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|Content:||3,000 Units at 40oC|
|Formulation:||In 3.2 M ammonium sulphate|
|Stability:||> 4 years at 4oC|
|Synonyms:||alpha-glucosidase; alpha-D-glucoside glucohydrolase|
|Concentration:||Supplied at ~ 1,500 U/mL|
|Expression:||Recombinant from Bacillus stearothermophilus|
|Specificity:||Hydrolysis of terminal, non-reducing α-1,4-linked D-glucose residues with release of D-glucose.|
|Specific Activity:||~ 80 U/mg (40oC, pH 6.5 on p-nitrophenyl-α-D-glucopyranoside)|
|Unit Definition:||One Unit of α-D-glucosidase activity is defined as the amount of enzyme required to release one µmole of p-nitrophenol per minute from 4-nitrophenyl α-D-glucopyranoside (5 mM), in sodium phosphate buffer (100 mM), pH 6.5 at 40oC.|
|Application examples:||Applications in carbohydrate and biofuels research and diagnostic and analytical procedures.|
High purity recombinant α-Glucosidase (Bacillus stearothermophilus) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.
Kralj, S., Stripling, E., Sanders, P., van Geel-Schutten, G. H. & Dijkhuizen, L. (2005). Applied and Environmental Microbiology, 71(7), 3942-3950.
Lactobacillus reuteri strain ATCC 55730 (LB BIO) was isolated as a pure culture from a Reuteri tablet purchased from the BioGaia company. This probiotic strain produces a soluble glucan (reuteran), in which the majority of the linkages are of the α-(1→4) glucosidic type (~70%). This reuteran also contains α-(1→6)-linked glucosyl units and 4,6-disubstituted α-glucosyl units at the branching points. The LB BIO glucansucrase gene (gtfO) was cloned and expressed in Escherichia coli, and the GTFO enzyme was purified. The recombinant GTFO enzyme and the LB BIO culture supernatants synthesized identical glucan polymers with respect to linkage type and size distribution. GTFO thus is a reuteransucrase, responsible for synthesis of this reuteran polymer in LB BIO. The preference of GTFO for synthesizing α-(1→4) linkages is also evident from the oligosaccharides produced from sucrose with different acceptor substrates, e.g., isopanose from isomaltose. GTFO has a relatively high hydrolysis/transferase activity ratio. Complete conversion of 100 mM sucrose by GTFO nevertheless yielded large amounts of reuteran, although more than 50% of sucrose was converted into glucose. This is only the second example of the isolation and characterization of a reuteransucrase and its reuteran product, both found in different L. reuteri strains. GTFO synthesizes a reuteran with the highest amount of α-(1→4) linkages reported to date.Hide Abstract