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KMID : 0545120020120040669
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Journal of Microbiology and Biotechnology
2002 Volume.12 No. 4 p.669 ~ p.673
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Partial Purification and Characterization of Limonoate Dehydrogenase from Rhodococcus fascians for the Degradation of Limonin
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PURI, MUNISH
KAUR, LAKHWINDER/MARWAHA, SATWINDER SINGH
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Abstract
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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 the conversion of limonoate to 17-dehydrolimonoate. The enzyme showed optimum activity at pH 8.0 and 40℃, with K_m value of 0.9μM, and requires Zn ions and sulfhydryl groups for catalytic action. The enzyme activity was inhibited by Hg^2+ and NaN_3 ions. The degradation of limonin (66%) in Kinnow mandarin juice was successfully demonstrated with partially purified limonoate dehydrogenase. With scale-up preparation of limonoate dehydrogenase, a successful debittering operation of fruit juices appears feasible.
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