S0937
Sucrose Phosphorylase
recombinant, expressed in E. coli, lyophilized powder, ≥45 units/mg solid
Synonym(s):
SPase, disaccharide glucosyltransferase, sucrose glucosyltransferase, Sucrose:orthophosphate α-D-glucosytransferase
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
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recombinant
expressed in E. coli
form
lyophilized powder
specific activity
≥45 units/mg solid
mol wt
56 kDa by SDS-PAGE
shipped in
wet ice
storage temp.
−20°C
General description
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.
Biochem/physiol Actions
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)
Unit Definition
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.
Physical form
Contains sucrose as stabilizer.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
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Cloning and expression of the sucrose phosphorylase gene in Bacillus subtilis and synthesis of kojibiose using the recombinant enzyme
WangM, et al
Microbial cell factories, 17(1), 23-23 (2018)
Thornthan Sawangwan et al.
Organic & biomolecular chemistry, 7(20), 4267-4270 (2009-10-02)
Regioselective glucosylation of R-glycerate catalysed by sucrose phosphorylase in the presence of sucrose as the donor substrate provided the natural compatible solute (R)-2-O-alpha-D-glucopyranosyl glycerate with complete regioselectivity in an optimised synthetic yield of 90% R-glycerate converted and a concentration of
A Kasperowicz et al.
Journal of applied microbiology, 107(3), 812-820 (2009-03-27)
To verify the taxonomic affiliation of bacterium Butyrivibrio fibrisolvens strain A from our collection and to characterize its enzyme(s) responsible for digestion of sucrose. Comparison of the 16S rRNA gene of the bacterium with GenBank showed over 99% sequence identity
Mario Mueller et al.
FEBS letters, 581(20), 3814-3818 (2007-07-31)
Site-directed mutagenesis was used to examine the specificity of Leuconostoc mesenteroides sucrose phosphorylase for utilization of fructose and phosphate as leaving group/nucleophile of the reaction. The largest catalytic defect in Arg(137)-->Ala (approximately 60-fold) and Tyr(340)-->Ala (approximately 2500-fold) concerned phosphate dependent
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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