ACCELERATED ESTERIFICATION OF AMINO-ACIDS WITH LIPOGLYCOSYLATED ALPHA-CHYMOTRYPSIN IN POLAR-SOLVENTS

A lipodisaccharide possessing a reactive aldopentose function, the 6-O-octyl-β-D-galactopyranosyl-(l→5)-L-arabinose (5), has been prepared. The reductive alkylation of four of the lysine residues of the bovine α-chymotrypsin led to a lipo-1-deoxyglycytolated enzyme. This modified protein efficiently catalyzed the synthesis of N-acetyl aminoacid ethyl esters in different solvents with 2.5-3% water contents. Compared to the native enzyme, enhanced esterification rates were determined, particularly in tetrahydrofuran, ethyl acetate and acetonitrile. © 1990.