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S0937

Sigma-Aldrich

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:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in E. coli

Quality Level

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.

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.

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3


Certificates of Analysis (COA)

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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
Kazuhisa Sugimoto et al.
Journal of bioscience and bioengineering, 104(1), 22-29 (2007-08-19)
We examined the synthesis of benzoyl glucoside using the transglucosylation reaction of sucrose phosphorylase. Sucrose phosphorylase from Streptococcus mutans showed marked transglucosylating activity, particularly under acidic conditions. On the other hand, sucrose phosphorylase from Leuconostoc mesenteroides showed very weak transglucosylating
Mamoru Nishimoto et al.
Carbohydrate research, 344(18), 2573-2576 (2009-10-24)
Beta-D-Galactopyranosyl-(1-->3)-2-acetamido-2-deoxy-D-galactose (galacto-N-biose, GNB) is an important core structure in functional sugar chains such as T-antigen disaccharide and the core 1 sugar chain in mucin glycoproteins. We successfully developed a one-pot enzymatic production of GNB from sucrose and GalNAc by the
Structural rearrangements of sucrose phosphorylase from Bifidobacterium adolescentis during sucrose conversion
Mirza O, et al.
The Journal of Biological Chemistry, 281(46), 35576-35584 (2006)
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.

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