Activity and inhibition of polyphenol oxidase in extracts of bran and other milling fractions from a variety of wheat cultivars
2001
Okot-Kotber, M. | Liavoga, A. | Yong, K.J. | Bagorogoza, K.
Studies were conducted to compare polyphenol oxidase (PPO) specific activities in various milling fractions of a variety of wheat cultivars and determine the levels of activities in a number of cultivars from different localities and harvesting seasons. Substrate specificities were also investigated. Bran was singled out as the richest source of PPO activity, which may also influence the activity in the other milling fractions that are known to have some proportion of bran content. We showed by gel electrophoresis and spectrophotometrically that the protein responsible for PPO activity apparently exists as a single isoform in bran and that the observed enzyme activity is likely to be a tyrosinase type, not a laccase or peroxidase. The specific activity was not significantly different between the reduction shorts and break shorts from the same cultivar, indicating a similar level of bran contamination in these fractions. Very low levels of PPO activity were recorded in the flour of all cultivars studied. Bran was used, therefore, to determine the varietal differences in the PPO activities in a number of cultivars from different localities and seasons of harvest. Results showed that the most significant determinant of PPO activity was the genotype, and this may be influenced by seasonality. We also determined that, apart from substrate preferences by the PPO enzyme, some phenolic acids actually inhibit PPO. Furthermore, we found that bran of some cultivars extracted with acidified methanol inhibited PPO activity substantially, whereas other extracts had less inhibitory properties. Thus, these unknown compounds in wheat may inhibit endogenous PPO activity.
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