Abstract
Peroxidase activity in isolated thylakoids from degreening canola (Brassica napus cv. Westar) seeds was demonstrated. The enzyme catalyzes the degradation of thylakoid‐bound pigments in the presence of H2O2 and 2,4‐dichlorophenol. Peroxidase activity is related to degreening, with periods of rapid degreening associated with high enzyme activity. Both de novo synthesis and substrate availability appear to control enzyme activity. Peroxidase is initially inhibited and then stimulated by sublethal freezing. Therefore, inhibition of peroxidase activity following sublethal freezing may be responsible, in part, for a failure of the seed to degreen.
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