Enzyme and Nonenzyme Hydrolyses of Pendent Ester Units in the Copolymer of p-Nitrophenyl Methacrylate and Acrylamide

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Abstract
The enzyme and nonenzyme hydrolyses of the pendent ester groups in the copolymer of p-nitrophenyl methacrylate and acrylamide [poly(p-NPMA/AAm)] were kinetically investigated. The pendent ester groups in poly(p-NPMA/AAm) were cleaved by esterase and .alpha.-chymotripsin but were not cleaved by lipase. The catalytic ability of esterase to hydrolyze the ester groups in the copolymer was smaller that that in p-nitrophenylacetate (p-NPA), which is a monomeric model. The maximal velocity for the esterase-catalyzed hydrolysis of ester groups in poly(p-NPMA/AAm) increased with an increase in the mole fraction of AAm units in poly-(p-NPMA/AAm), while the Michaelis constant was almost independent of the composition of the copolymer. The pendent ester groups in poly(p-NPMA/AAm) are known to be strongly hydrolyzed by alkaline solution but only slightly hydrolyzed by acidic solution. The alkaline hydrolysis velocity of poly(p-NPMA/AAm) was larger than that of monomeric p-NPA, and it was enhanced by increasing the mole fraction of AAm in poly(p-NPMA/AAm). [This research was conducted as part of on-going drug synthesis studies].

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