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Literature summary for 2.4.1.7 extracted from

  • Cerdobbel, A.; De Winter, K.; Desmet, T.; Soetaert, W.
    Sucrose phosphorylase as cross-linked enzyme aggregate: improved thermal stability for industrial applications (2010), Biotechnol. J., 5, 1192-1197.
    View publication on PubMed

Application

Application Comment Organism
synthesis sucrose phosphorylase can glycosylate a variety of small molecules using sucrose as cheap ut efficient donor substrate. The immobilized enzyme is optimized due to a higher temperature tolerance compared to the soluble enzyme from Bifidobacterium adolescentis, overview Bifidobacterium adolescentis

Protein Variants

Protein Variants Comment Organism
additional information immobilization of the enzyme by cross-linking leads to a 17 degree higher temperature tolerance compared to the soluble enzyme from Bifidobacterium adolescentis, overview Bifidobacterium adolescentis

General Stability

General Stability Organism
the immobilized enzyme is stable for over 10 reaction cycles in glycosylation of molecules Bifidobacterium adolescentis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
sucrose + phosphate Bifidobacterium adolescentis
-
D-fructose + alpha-D-glucose 1-phosphate
-
?

Organism

Organism UniProt Comment Textmining
Bifidobacterium adolescentis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sucrose + phosphate
-
Bifidobacterium adolescentis D-fructose + alpha-D-glucose 1-phosphate
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
the immobilized enzyme is stable for one week without loss of activity Bifidobacterium adolescentis