Purification and Characterization of Hydantoin Racemase from Microbacterium liquefaciens AJ 3912

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概要

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• A hydantoin racemase that catalyzed the racemization of 5-benzyl-hydantoin was detected in a cell-free extract of Microbacterium liquefaciens AJ 3912, a bacterial strain known to produce L-amino acids from their corresponding DL-5-substituted-hydantoins. This hydantoin racemase was purified 658-fold to electrophoretic homogeneity by serial chromatography. The N-terminal amino acid sequence of the enzyme showed homology with known hydantoin racemases from other microorganisms. The apparent molecular mass of the purified enzyme was 27 kDa on sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) and 117 kDa on gel-filtration in the purification conditions, indicating a homotetrameric structure. The purified enzyme exhibited optimal activity at pH 8.2 and 55 °C, and showed a chiral preference for L-5-benzyl- rather than D-5-benzyl-hydantoin.

• 社団法人 日本農芸化学会の論文
• 2005-03-23

著者

• Yokozeki Kenzo

  Aminoscience Laboratories Ajinomoto Co. Inc.

• Onishi Norimasa

  Amino Science Laboratories Ajinomoto Co. Inc.

• Yokozeki Kenzo

  Res. Inst. For Bioscience Products And Fine Chemicals Ajinomoto Co. Inc.

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