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.
Attached Files
(Some files may be inaccessible until you login with your Deakin Research Online credentials)
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.
Notes
Every reasonable effort has been made to ensure that permission has been obtained for items included in Deakin Research Online. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au
Language
eng
Field of Research
100399 Industrial Biotechnology not elsewhere classified 100301 Biocatalysis and Enzyme Technology 100302 Bioprocessing, Bioproduction and Bioproducts
Unless expressly stated otherwise, the copyright for items in Deakin Research Online is owned by the author, with all rights reserved.
Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO.
If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.