Bacillus fordii MH602 strain菌株菌种 BioVector NTCC质粒载体菌种细胞基因保藏中心

Bacillus fordii MH602 strain菌株菌种

Bacillus fordii MH602 was newly screened from soil at 45 °C and exhibited high activities of hydantoinase and carbamoylase, efficiently yielding L-amino acids including phenylalanine, phenylglycine and tryptophan with the bioconversion yield of 60–100% from the corresponding DL-5-substituted hydantoins. Hydantoinase activity was found to be cell-associated and inducible. The optimal inducer was DL-5-methylhydantoin with concentration of 0.014 mol L−1 and added to the fermentation medium in the exponential phase of growth. In the production of optically pure amino acids from DL-5-benylhydantoin, the optimal temperature and pH of this reaction were 45–50 °C and 7.5 respectively. The hydantoinase was non-stereoselective, while carmbamoylase was L-selective. The hydantoinase activity was not subject to substrate inhibition, or product inhibition by ammonia. In addition, The activities of both enzymes from crude extract of the strain were thermostable; the hydantoinase and carbamoylase retained about 90% and 60% activity after 6 h at 50 °C, respectively. Since reaction at higher temperature is advantageous for enhancement of solubility and for racemization of DL-5-substituted hydantoins, the relative paucity of L-selective hydantoinase systems, together with the high level of hydantoinase and carbamoylase activity and unusual substrate selectivity of the strain MH602, suggest that it has significant potential applications. Cultivation conditions: Medium 220 + MnSO4, 30°C

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