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Plant Physiology 78:256-262 (1985)
© 1985 American Society of Plant Biologists

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Articles

Purification of d'Anjou Pear (Pyrus communis L.) Polyphenol Oxidase 1

Kimberly W. Wissemann2 and Morris W. Montgomery3

Department of Food Science and Technology, Oregon State University, Corvallis, Oregon 97331

Polyphenol oxidase (PPO) was extensively purified to homogeneity from d'Anjou pear (Pyrus communis L.) by extraction in the presence of the phenolic binder AG 2-X8 andTriton X-100. Chlorophyll pigment was removed by chromatography resulting in a clear, colorless enzyme extract. Purification of pear PPO was achieved after chromatography on Phenyl Sepharose CL-4B, DEAE-cellulose, and hydroxylapatite columns. Only after the columns were run at room temperature rather than at 4°C were sharp peaks and good resolution obtained. Reproducibility of the entire scheme was excellent with chromatography on the hydrophobic resin as a key to successful purification. Three separate fractions of pear PPO were homogeneous when stained for protein with the silver stain after polyacrylamide slab gel electrophoresis and corresponded to relative mobilities of 0.41, 0.43, and 0.73. The effect of dimethylsulfoxide on enzyme activity was investigated and found to increase significantly the activity of purified pear PPO over the control.

2 Present address: Biochemistry Department, University of Massachusetts, Amherst, MA 01003.

3 Present address: Department of Food Science and Human Nutrition, University of Hawaii at Manoa, Honolulu, HI 96822.

1 Technical Paper 7144, Oregon Agricultural Experiment Station.




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