Polyphenol Oxidase System in Red Delicious Apples
Authors:
- C. SatjawatcharaphongCSC. Satjawatcharaphong
- K.S. RymalKRK.S. Rymal
- W. A. DozierWDW. A. Dozier
- R. C. SmithRSR. C. Smith
- 1 November 1983
- journal article
- Published by Wiley in Journal of Food Science
- Vol. 48 (6) , 1879-1880
Abstract
The polyphenol oxidase system (E.C. 1.14.18.1) in‘Red Delicious’apples ( Malus domestica ) was investigated. Polyacrylamide gel electrophoresis (PAGE) revealed two active isoenzymes as detected with pyrocatechol substrate. The crude enzyme extract (acetone powder) was found to have one optimum pH of 6.2 and one optimum temperature for the browning reaction of 30°C with the experimental conditions described. The Michaelis constant (Km) as an average of the two active enzyme forms was 2.2 × 10 −l M pyrocatechol and the average maximum velocity (Vmax) was 4.8 × 10 −l AA390 per minute.Keywords
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