S0937
Sucrose Phosphorylase
recombinant, expressed in E. coli, lyophilized powder, ≥45 units/mg solid
Synonyme(s) :
SPase, disaccharide glucosyltransferase, sucrose glucosyltransferase, Sucrose:orthophosphate α-D-glucosytransferase
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About This Item
Numéro CAS:
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54
Produits recommandés
Produit recombinant
expressed in E. coli
Niveau de qualité
Forme
lyophilized powder
Activité spécifique
≥45 units/mg solid
Poids mol.
56 kDa by SDS-PAGE
Conditions d'expédition
wet ice
Température de stockage
−20°C
Description générale
Research area: Cell signaling
Sucrose Phosphorylase belongs to glycoside hydrolase, GH13 family. It comprises of four domains with the glucose anomeric carbon-binding site and a glucoside-binding site. The active site residues include Asp192 and Glu232. It is majorly produced by bifidobacteria and lactic acid bacteria. The cross-linked sucrose phosphorylase aggregates is thermostable and could be exploited for industrial catalysis of glycosylation.
Sucrose Phosphorylase belongs to glycoside hydrolase, GH13 family. It comprises of four domains with the glucose anomeric carbon-binding site and a glucoside-binding site. The active site residues include Asp192 and Glu232. It is majorly produced by bifidobacteria and lactic acid bacteria. The cross-linked sucrose phosphorylase aggregates is thermostable and could be exploited for industrial catalysis of glycosylation.
Application
Sucrose Phosphorylase has been used in sucrose determination in wheat plant and in sucrose hydrogen production.
Sucrose phosphorylase has been used:
- To assess the enzymatic synthesis of stable, odorless, and powdered furanone glucosides.
- To investigate the novel transglucosylating reaction with carboxylic compounds.
- In sucrose determination in wheat plant and in sucrose hydrogen production.
Actions biochimiques/physiologiques
Sucrose phosphorylase catalyzes the reversible conversion of sucrose (α-D-glucopyranosyl-1,2-β-D-fructofuranoside) and phosphate into D-fructose and α-D-glucose 1-phosphate. This reaction plays a crucial role in generating the vital glucose component through sucrose metabolism.(1)
Définition de l'unité
One unit will produce 1.0 μmole of D-fructose from sucrose per min with the corresponding reduction of NADP to NADPH at pH 7.6, at 25 °C.
Forme physique
Contains sucrose as stabilizer.
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Resp. Sens. 1
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
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Les clients ont également consulté
Jin-Ha Lee et al.
Biotechnology letters, 30(4), 749-754 (2007-11-27)
The gene encoding sucrose phosphorylase (742sp) in Leuconostoc mesenteroides NRRL B-742 was cloned and expressed in Escherichia coli. The nucleotide sequence of the transformed 742sp comprised an ORF of 1,458 bp giving a protein with calculated molecular mass of 55.3
Christiane Goedl et al.
Journal of biotechnology, 129(1), 77-86 (2007-01-12)
Sucrose phosphorylase catalyzes the reversible conversion of sucrose (alpha-D-glucopyranosyl-1,2-beta-D-fructofuranoside) and phosphate into D-fructose and alpha-D-glucose 1-phosphate. We report on the molecular cloning and expression of the structural gene encoding sucrose phosphorylase from Leuconostoc mesenteroides (LmSPase) in Escherichia coli DH10B. The
Koji Nomura et al.
Bioscience, biotechnology, and biochemistry, 72(1), 82-87 (2008-01-08)
Transglucosylation from sucrose to acetic acid by sucrose phosphorylase (EC 2.4.1.7) was studied. 1-O-Acetyl-alpha-D-glucopyranose was isolated as the main product of the enzyme reaction. We also compared the pH-dependence of transglycosylation catalyzed by sucrose phosphorylase toward carboxyl and hydroxyl groups.
Genotypic variation in water-soluble carbohydrate accumulation in wheat
Ruuska SA, et al.
Functional plant biology, 33(9), 799-809 (2006)
Alexandra Schwarz et al.
The Biochemical journal, 403(3), 441-449 (2007-01-20)
The role of acid-base catalysis in the two-step enzymatic mechanism of alpha-retaining glucosyl transfer by Leuconostoc mesenteroides sucrose phosphorylase has been examined through site-directed replacement of the putative catalytic Glu237 and detailed comparison of purified wild-type and Glu237-->Gln mutant enzymes
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