Abstract
The coupling efficiency in α-chymotrypsin-catalyzed peptide synthesis has been significantly improved and hydrolysis of an acyl donor comparatively decreased by the use of an N-benzyloxycarbonyl (Z)-protected amino acid carbamoylmethyl (Cam) ester as acyl donor in frozen aqueous solution. Under frozen state conditions, the protease was able to catalyze peptide bond formation more effectively than in aqueous reaction mixtures.