Improved activity and stability of an immobilized recombinant laccase in organic solvents
Laccase (E.C. 1.10.3.2) from Trametes versicolor was immobilized (adsorbed) by drying on various supports (glass, glass powder, silica gel, and Nylon 66 membrane). The enzyme activity and stability were determined in diethyl ether, ethyl acetate, and methylene chloride. The initial rate for the oxidation of syringaldazine varied up to 245-fold depending on the solvent and support, the best results being obtained with Nylon 66 membrane. No inactivation of immobilized laccase over 72 h was observed in diethyl ether and ethyl acetate, while exposure to methylene chloride resulted in significant activity decreases regardless of the support material.
Synthesis and modification of carbohydrates using glycosidases and lipases.- Chemical transformations employing glycosyltransferases.- Enzymatic and chemical glycosylations of ergot alkaloids and biological aspects of new compounds.- Enzymatic synthesis of peptide conjugates - Tools for the study of biological signal transduction.- Tandem asymmetric C-C bond formations by enzyme catalysis.- The synthesis of novel sialic acids as biological probes.- Synthesis of oligosaccharides of bacterial origin containing heptoses, uronic acids and fructofuranoses as synthetic challenges.- Pyruvated saccharides - Novel strategies for oligosaccharide synthesis.