Abstract
Various lipid-coated glycoside hydrolases were prepared, which were soluble in most organic solvents such as isopropyl ether, isooctane and benzene but insoluble in aqueous solution. They could act as efficient catalysts for transglycosylation of α-D-or β-D-mannoside, N-acetyl-β-D-glucosaminide, β-D-glucoside or β-D-galactoside to hydrophobic acceptor alcohols in dry isopropyl ether. When a native β-D-galactosidase was used in the aqueous solution containing acetonitrile for the same reaction (a conventional method), the yield of the transgalactosylation was low due to the predominant process of hydrolysis reaction. The enzyme activity for glycosylation depends on the coating of lipids as well as the orgin or type of enzyme. These lipid-coated glycoside hydrolases could also act as an efficient catalyst for transglycosylation in the two water-organic phases: both the hydrophobic lipid-coated enzyme and alcohols were solubilized in isopropyl ether and mixed with an aqueous solution of glycosyl donors such as lactose and cellobiose.
