Enzymatic transesterification of monosaccharides and amino acid esters in organic solvents

Abstract

Lipases and proteases from different sources were screened for their ability to catalyze the transesterification of glucose and activated N-blocked phenylalanine. A commercial protease from Bacillus licheniformis was found to be most effective for this purpose. On a basis of C-NMR analysis, glucose was acylated at the C-6 position. The enzyme showed a broad substrate specificity toward various monosaccharides.