Partial purification and characterization of limonoate dehydrogenase from Rhodococcus fascians for the degradation of limonin
Puri, Munish, Kaur, Lakhwinder and Marwaha, Satwinder Singh 2002, Partial purification and characterization of limonoate dehydrogenase from Rhodococcus fascians for the degradation of limonin, Journal of microbiology and biotechnology, vol. 12, no. 4, pp. 669-673.
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An extracellular limonoate dehydrogenase was purified 10-fold from a cell-free extract of Rhodococcusfascians 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 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 partially purified limonoate dehydrogenase. With scale-up preparation of limonoate dehydrogenase, a successful debittering operation of fruit juices appears feasible.
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Field of Research
100399 Industrial Biotechnology not elsewhere classified 100301 Biocatalysis and Enzyme Technology 100302 Bioprocessing, Bioproduction and Bioproducts
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