ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Polyphenoloxidase (PPO) from cherimoya epicarp catalyzed the hydroxylation of monphenols like L(−)tyrosine, tyramine, and p-cresol (monophenolase activity), and oxidation of o-dihydroxyphenols like catechol and L-DOPA (dihydroxyphenolase activity). The hydroxylation of monophenols occurred after a lag period which was shortened by diphenols. The Km values indicated a low affinity of PPO to the substrates. Aliphatic mono- and dicarboxylic acids and sugars did not show any inhibitory effect on PPO cherimoya epicarp. Cysteine and mercaptoethanol, but not ascorbic acid, appeared to be protective agents of PPO cherimoya epicarp.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1988.tb13559.x
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