Taken in part from a thesis submitted to Oregon State Univ. in partial fulfillment of the requirements for the Ph.D. degree.
Strawberry Polyphenoloxidase: Purification and Characterization
Article first published online: 25 AUG 2006
Journal of Food Science
Volume 55, Issue 5, pages 1315–1319, September 1990
How to Cite
WESCHE-EBELING, P. and MONTGOMERY, M. W. (1990), Strawberry Polyphenoloxidase: Purification and Characterization. Journal of Food Science, 55: 1315–1319. doi: 10.1111/j.1365-2621.1990.tb03924.x
Author Wesche-Ebeling acknowledges the financial support from the ‘Consejo National de Ciencia y Technologóa, México’ during the stay at O.S.U.
- Issue published online: 25 AUG 2006
- Article first published online: 25 AUG 2006
- Ms received 8/28/88; revised 10/20/89; accepted 2/28/90.
Stable and highly active polyphenoloxidase (PPO) extracts were obtained using polyvinylpyrrolidone, Amberlite XAD-4, Triton X-100, and protease inhibitor in pH 5.25 buffer. Citrate and phosphate prevented binding of PPO to pectin. Phenyl sepharose chromatography resolved PPO into two isozymes (PPO-F1 and PPO-F2) both separated from pectin. PPO-F1 had a molecular weight of 111,000, did not penetrate the running gel during electrophoresis, and was bound by concanavalin suggesting that it contained carbohydrate. PPO-F2 resolved into two peaks during DEAE-chromatography, had a molecular weight of 34,500, and resolved into two bands during electrophoresis.