The GLICOENZ consortium is formed by four groups specialized in the discovery of novel enzymes from microorganisms, the improvement of enzyme properties by molecular biology techniques, the development of biotransformations employing immobilized enzymes and the study of structure-function relationships of enzymes using structural and molecular modelling approaches.
Several glycosidic enzymes are being investigated: β-galactosidases (GH2), xylanases (GH10), α-amylases and cyclodextrin-glucantransferases (GH13), chitinases and chitosanases (GH18), α-glucosidases and glucoamylases (GH31) and β-fructofuranosidases (GH32). These enzymes are being applied to the preparation of well-established prebiotics (galactooligosaccharides, GOS; Fructooligosaccharides, FOS), as well as second-generation prebiotics (isomaltooligosachharides, IMOS; xylooligosachharides, XOS; chitooligosachharides, COS) and hetero-oligosaccharides.
Several glycosidic enzymes are being investigated: β-galactosidases (GH2), xylanases (GH10), α-amylases and cyclodextrin-glucantransferases (GH13), chitinases and chitosanases (GH18), α-glucosidases and glucoamylases (GH31) and β-fructofuranosidases (GH32). These enzymes are being applied to the preparation of well-established prebiotics (galactooligosaccharides, GOS; Fructooligosaccharides, FOS), as well as second-generation prebiotics (isomaltooligosachharides, IMOS; xylooligosachharides, XOS; chitooligosachharides, COS) and hetero-oligosaccharides.
In addition, the consortium GLICOENZ investigates the synthesis of glycoconjugates of bioactive molecules, namely plant polyphenols; glycosylation dramatically changes their physico-chemical properties and bioavailability. The yield of such glycoderivatives is usually very low because the active-site architecture of these enzymes is not appropriate to accommodate the phenolic acceptors in contrast with typical carbohydrates. A synergistic combination of structural analysis and protein engineering helps us to build up enzymatic strategies for such bioprocesses.