Accelerated esterification of aminoacids with lipoglycosylated α-chymotrypsin in polar solvents

Article abstract of DOI:10.1016/0040-4039(90)80090-9

A lipodisaccharide possessing a reactive aldopentose function, the 6-O-octyl-β-D-galactopyranosyl-(1→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.