Partial Purification and Properties of Alanine Racemase from the Muscle of Black Tiger Prawn Penaeus monodon

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  • Fujita Eriko
    Department of Food Science and Nutrition, Kyoritsu Women's University
  • Okuma Emiko
    Department of Food Science and Nutrition, Kyoritsu Women's University
  • Abe Hiroki
    Department of Food Science and Nutrition, Kyoritsu Women's University

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  • Partial Purification and Properties of Alanine Racemase from the Muscle of Black Tiger Prawn <i>Penaeus monodon</i>
  • Partial Purification and Properties of

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Alanine racemase [EC 5. 1. 1. 1], which catalyzes the interconversion of D-, L-alanine, was partially purified from the muscle of the black tiger prawn Penaeus monodon using DEAE-cellulose, DEAE-Toyopearl, hydroxyapatite, Phenyl- and Butyl-Toyopearl, and Gel-Toyopearl HW column chro-matographies. The final enzyme preparation was not homogeneous but the purification was as high as about 17, 700-fold with a final yield of 2.5%.<br> Apparent molecular weight of the enzyme in its native form was 85, 000. The maximal activity was attained at 35-40°C and at around pH 8. 5. The alanine racemase was inactivated between 40 and 60°C and was also rather unstable during low temperature storage. The enzyme acts specifically on D-, L-alanine as substrates, but not on the other amino acids in the present assay conditions. The enzyme did not require pyridoxal 5'-phosphate or FAD as a cofactor. The enzyme was inhibited strongly with pyruvate and L-alanine, which are metabolites from D-alanine.

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