Chymotrypsin catalysed hydrolysis of a drug model, p-nitroanalide bound onto polyanionic carriers

Enzymatic hydrolysis of polymeric substrates bearing identical side chains (containing N- (6-aminohexanoyl)-L-phenylalanine-p-nitroanilide moieties) was studied as a function of chemical structure of the main chain. Kinetic parameters of synthesized derivatives, i.c. poly(N-vinylpyrrolidone-co-maleic acid) (A), poly(trimethylene hydrogen phosphate) (B), and poly(2-hydroxypropylmethacrylamide) (C) were evaluated and referred to the corresponding literature data. The Michaelis constants were found to decrease in the following sequence: B > C > A.