Purification of grape polyphenoloxidase with hydrophobic chromatography
1980
Wissemann, K.W. | Lee, C.Y. (Cornell Univ., Geneva, NY (USA). New York State Agricultural Experiment Station, Dept. of Food Science and Technology)
The oxidation reaction associated with the darkening of damaged tissue in fresh fruits and vegetables is catalyzed by the enzyme polyphenoloxidase (PPO) (monophenol, dihydroxyphenylalanine: oxygen oxidoreductase: E.C. 1.14.18.1). To better control the action of PPO in different fruit and vegetable products, it is necessary to characterize the enzyme isolated from those different sources. However, the isolation of PPO is difficult, and several methods for the purification of PPO have been reported with varying degrees of success. In this report, hydrophobic chromatography is used to isolate and purify grape PPO. The use of hydrophobic chromatography for the separation of proteins is relatively new: Flurkey and Jen appear to be the first to use such columns to purify PPO. The use of hydrophobic chromatography as a rapid, reproducible and successful purification technique for grape PPO is presented in this paper
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