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Partial purification and characterization of limonoate dehydrogenase from Rhodococcus fascians for the degradation of limonin
An extracellular limonoate dehydrogenase was purified 10-fold from a cell-free extract of Rhodococcus fascians by ammonium sulfate precipitation, dialysis, and ultrafiltration. This purified dehydrogenase catalyzed theconversion of limonoate to 17-dehydrolimonoate. The enzyme showed optimum activity at pH 8.0 and 40oC, with Km value of 0.9 µM, and requires Zn ions and sulfhydryl groups for catalytic action. The enzyme activity was inhibited by Hg2+ and NaN3 ions. The degradation of limonin (66%) in Kinnow mandarin juice was successfully demonstrated with partiallypurified limonoate dehydrogenase. With scale-up preparation of limonoate dehydrogenase, a successful debittering operation of fruit juices appears feasible.<br /