A microorganism with the ability to form D-p-hydroxyphenylglycine (D-pHPG) from DL-5-p-hydroxyphenylhydantoin (DL-5-pHPH) was isolated and identified as Sinorhizobium morelens S-5. Hydantoinase and carbamoylase involved in this bioconversion process were both strictly D-stereospecific. Addition of DL-5-(2-indolymethyl)hydantoin in the medium could enhance the biotransfromation ability of the cells of S. morelens S-5. The optimum temperature and pH for D-pHPG production, respectively, were 45 degreesC and 8.2 when resting cells were used during the biotransformation process. Partially purified D-carbamoylase exhibited a temperature optimum at 60 degreesC and pH optimum at 7.0 in 0.1 M phosphate buffer. The thermostablility of the enzyme was remarkable, with no loss of activity detected after 40 min at 50 degreesC. (C) 2004 Elsevier Inc. All rights reserved.