Kinetics of enzymolysises for the production of D p hydro xyphenylglycine from DL p hydro xyphenylhydantion by Pseudomonas Putida cells containing both hydroxypyrimidinehydrase and N carbamoyl D aminoacid amidohydrolase were studied. Dissolution process of DL p hydroxyphenylhydantoin and characteristics of both enzymes were investigated. The results showed that enzymolysis catalyzed by hydro xypyrimidinehydrase accorded approximately with first order kinetics

while that catalyzed by N carbamoyl D aminoacid amidohydrolase could be described by modified Michaelis Menton equation. It was found that enzymolysis catalyzed by N carbamoyl D aminoacid amidohydrolase was inhibited by the high concentration substrate and the byproduct NH 3. The kinetic model of whole process was developed. The values of model parameters were given. The influence of pH on model parameters was discussed and optimum operation conditions were established .