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) was isolated from two varieties of grapes grown in the northeastern United States and its characteristics were studied. The temperature and pH optima for both enzymes were 25°C and 5.5, respectively. The thermal inactivation of PPO followed first-order kinetics; with the Niagara enzyme being more heat stable than Ravat PPO. The substrate specificity of the grape PPO clearly showed high affinity toward the o-diphenolic compounds, with a high affinity toward caffeic acid. Inhibition studies indicated that L-cysteine and sodium diethyldithiocarbamate were the most potent.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1981.tb04897.x
