Enzymetic synthesis of D-p-hydroxyphenylglycine from DL-p-hydroxyphenylhydantoin in the presence of organic cosolvent
Dong-Man Kim and Hak-Sung Kim
Bacterial strain KBEL101 isolated from soil was immobilized within polyacrylamide gel and used for the synthesis of D-p-hydroxyphenylglycine from DL-5-substituted hydantoin. The optimum reaction conditions for immobilized whole cell enzyme were pH 8.0 and temperature 30C. Various water-miscible organic solvents were tested Àç¼Ò respect to the activity and the stability of whole cell enzyme, and 5% dimethylsulfoxide(DMSO) was chosen to be a proper solvent : hydantoinase activity increased twofold in the presence of 5% DMSO. From a practical standpoint, it is a advantageous to obtain the highest conversion yield, and enzymetic synthesis of N-carbamoiyl-D-p-hydroxyphenylglycine was carried out in repeated batch operation in the presence fo 5% DMSO. THe time required to reach 99% conversion yield was increased with increasing number of batch operations when batch operation was conducted four times.