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Glycoside hydrolases in Aplysia fasciata: analysis and applications
- Source :
- Biotechnology & genetic engineering reviews, edited by Harding SE; Tombs MP, pp. 129–148, 2008, info:cnr-pdr/source/autori:A Trincone; A Tramice; A Giordano; G Andreotti/titolo:Glycoside hydrolases in Aplysia fasciata: analysis and applications/titolo_volume:Biotechnology & genetic engineering reviews/curatori_volume:Harding SE; Tombs MP/editore:/anno:2008
- Publication Year :
- 2008
-
Abstract
- Glycosylation is considered to be an important reaction for the chemical modification of compounds with useful biological activities. Glycoside hydrolases are biotechnologically attractive enzymes which can be used in synthetic reactions for assembling glycosidic linkages with absolute stereoselectivity at an anomeric centre. Most of these enzymes are commercially available but there is great interest in the search for new biocatalysts with original catalytic characteristics. The marine environment has shown to be a very interesting source for new glycosyl hydrolases for both hydrolytic and synthetic aspects. In particular, Aplysia fasciata a marine herbivorous mollusc has been shown to be a potent producer of a library of glycoside hydrolases applied to the synthesis of glycosidic bonds. The impressive assortment of glycosidases in marine organisms clearly indicates that the potential biodiversity of these enzymes is still largely unexplored and that potential applications of biocatalysts from the sea will increase in the near future.
- Subjects :
- glycosylation
marine enzymes
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Journal :
- Biotechnology & genetic engineering reviews, edited by Harding SE; Tombs MP, pp. 129–148, 2008, info:cnr-pdr/source/autori:A Trincone; A Tramice; A Giordano; G Andreotti/titolo:Glycoside hydrolases in Aplysia fasciata: analysis and applications/titolo_volume:Biotechnology & genetic engineering reviews/curatori_volume:Harding SE; Tombs MP/editore:/anno:2008
- Accession number :
- edsair.doi.dedup.....165f32119d467feefd9b7d50610112fc