A New Method for the Production of Optically Active Aminoacids

d-p-Hydroxyphenylglycine production from dl-5-p-hydroxyphenylhydantoin by Agrobacterium sp.

“…The presence of the racemase in this microorganism is an interesting characteristic. Dinelli et al (1975) showed that the rates of chemical racemization of several 5-substituted hydantoins depended mostly on the nature of the substituent in the 5-position of the hydantoin ring, and this rate might become the limiting step in the production of some amino acids.…”

“…Unless otherwise stated, a standard assay mixture consisted of 250 mg DL-5-PHPH and 250 mg cells (dry weight) in 25 ml of 0.1 M potassium phosphate buffer (pH 8.0), as most of the hydantoins are known to racemize easily under slightly alkaline conditions (Dinelli et al 1975). The reaction was carried out at 40°C for 6 h with moderate stirring and nitrogen sparging to prevent oxidation of the hydantoin.…”

Production of optically pure d- and l-α-amino acids by Bioconversion of d,l-5-monosubstituted hydantoin derivatives

“…Other suitable inducers were 5-methylthioethylenehydantoin and 5-(p-hydroxyphenyl)hydantoin, while hydantoin, 5-methylhydantoin, uracil, and dihydrouracil caused only slight induction. In contrast to other publications [6,10,27,67,68], Pseudomonas sp. AJ-11220 was able to form D-glutamic acid from the corresponding hydantoin [24].…”

“…At first Cecere et al [67,68] successfully tried to use the immobilized calf liver dihydropyrimidinase for the production of N-carbamoyl-D-phenylglycine and its p-chloroandp-hydroxy-derivatives from the corresponding chemically synthesized racemic hydantoins (see Sect. 6.2).…”

“…Table 14. Substrate specificities of bacterial N-carbamoyl-L-amino acid amidohydrolases [67,136,137] (Fig. 7b) pioneered the field of industrial application of enzymatic D-specific hydantoin hydrolysis (see also Sect.…”