Journal
FOOD CHEMISTRY
Volume 107, Issue 1, Pages 129-135Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2007.07.068
Keywords
polyphenol oxidase; purification; lettuce; Lactuca sativa var. capitata L.; characterization; inhibitors
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Polyphenol oxidase (PPO) was isolated from butter lettuce (Lactuca sativa var. capitata L.) grown in Poland and its biochemical characteristic were studied. PPO from butter lettuce showed a higher affinity to 4-methylcatechol than to catechol. The K-m and V-max values were: 3.20 +/- 0.01 mM and 4081 +/- 8 U/ml min(-1) for catechol and 1.00 +/- 0.09 mM and 5405 +/- 3 U/ml min(-1) for 4-methylcatechol. The optimum pHs of the enzyme were found to be 5.5 using catechol and 6.8 using 4-methylcatechol as substrate. The enzyme had a temperature optimum of 35 degrees C. The enzyme was relatively stable at 30 degrees C and 40 degrees C. The times required for 50% inactivation of activity at 50 degrees C, 60 degrees C and 70 degrees C were found to be about 30, 20 and 5 min, respectively. Inhibitors used for investigation in this study were placed in relative order of inhibition: p-hydroxybenzoic acid > glutathione approximate to ascorbic acid > L-cysteine > EDTA > citric acid. The enzyme eluted in the chromatographic separations was analyzed electrophoretically under denaturating conditions. The analysis revealed a single band on the SDS-PAGE which corresponded to a molecular weight of 60 kDa. (C) 2007 Elsevier Ltd. All rights reserved.
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