Production of D-p-hydroxyphenylglycine from D,L-5-(4-hydroxyphenyl)hydantoin using immobilized thermostable D-htdantoinase from Bacillus stearothermopjilus SD-1
Dong-Cheol Lee, Seung -Goo Lee and Hak-Sung Kim
Thermostable D-hydantoinase from thermophilic Baccilus stearothermophilus SD-1 was used to produce N-carbamoyl-D-p-hydorxyphenylglycine (NC-HPG) from D,L-5-(4-hydroxyphenyl)hydantoin (DL-5-HPH). Culture conditions for the production of the enzyme from B. stearothermophilus SD-1 were optimized. The D-hydatoinase was immobilized on various support matrices by adsorption, and DEAE-cellulose resin was found to be most effective in terms of the activity recovery and the amount of protein bound. The activity of enzyme immobilized on DEAE-cellulose was retained >90%, and the optimal reaction conditions for the immobilized enzyme were determined to be 55C and pH 9.0 respectively. Immobilized enzyme was applied to the production of NC-HPG from DL-%-HPH in repeated batch, and the production rate was maintained constantly overnine succesive operations.