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Sucrose Phosphorylase and Related Enzymes in Glycoside Hydrolase Family 13: Discovery, Application and Engineering.
- Source :
-
International journal of molecular sciences [Int J Mol Sci] 2020 Apr 05; Vol. 21 (7). Date of Electronic Publication: 2020 Apr 05. - Publication Year :
- 2020
-
Abstract
- Sucrose phosphorylases are carbohydrate-active enzymes with outstanding potential for the biocatalytic conversion of common table sugar into products with attractive properties. They belong to the glycoside hydrolase family GH13, where they are found in subfamily 18. In bacteria, these enzymes catalyse the phosphorolysis of sucrose to yield α-glucose 1-phosphate and fructose. However, sucrose phosphorylases can also be applied as versatile transglucosylases for the synthesis of valuable glycosides and sugars because their broad promiscuity allows them to transfer the glucosyl group of sucrose to a diverse collection of compounds other than phosphate. Numerous process and enzyme engineering studies have expanded the range of possible applications of sucrose phosphorylases ever further. Moreover, it has recently been discovered that family GH13 also contains a few novel phosphorylases that are specialised in the phosphorolysis of sucrose 6 <superscript>F</superscript> -phosphate, glucosylglycerol or glucosylglycerate. In this review, we provide an overview of the progress that has been made in our understanding and exploitation of sucrose phosphorylases and related enzymes over the past ten years.
- Subjects :
- Bacterial Proteins chemistry
Bacterial Proteins genetics
Biocatalysis
Enzyme Stability
Glucosyltransferases chemistry
Glucosyltransferases genetics
Glycoside Hydrolases chemistry
Glycoside Hydrolases genetics
Glycosides chemical synthesis
Substrate Specificity
Bacterial Proteins metabolism
Glucosyltransferases metabolism
Glycoside Hydrolases metabolism
Protein Engineering methods
Subjects
Details
- Language :
- English
- ISSN :
- 1422-0067
- Volume :
- 21
- Issue :
- 7
- Database :
- MEDLINE
- Journal :
- International journal of molecular sciences
- Publication Type :
- Academic Journal
- Accession number :
- 32260541
- Full Text :
- https://doi.org/10.3390/ijms21072526