[Thermostabilities of plant phenol oxidase and peroxidase, determining the technology of their use in food industry].
Stabilities of phenol oxidase and peroxidase from tea plant (Camellia sinensis L.) clone Kolkhida leaves, apple (Malus domestica L.) cultivar Kekhura fruits, walnut (Juglans regia L.) green pericarp, and horseradish (Armoracia lapathifolia Gilib) roots were studied using different storage temperature modes and storage duration. It was demonstrated that both enzymes retained residual activities (approximately 10%) upon 20-min incubation at 80 degrees C. Phenol oxidases from tea, walnut, and, especially, apple, as well as tea peroxidase were stable during storage. A technology for treatment of plant oxidases was proposed, based on the use of a natural inhibitor phenol oxidase and peroxidase, isolated from tea leaves, which solving the problem of residual activities of these enzymes, arising during pasteurization and storage of beverages and juices. It was demonstrated that browning of apple juice during pasteurization and beer turbidity during storage could be efficiently prevented using the natural inhibitor of these enzymes.
Mchedlishvili
N I
NI
Omiadze
N T
NT
Gulua
L K
LK
Sadunishvili
T A
TA
Zamtaradze
R K
RK
Abutidze
M O
MO
Bendeliani
E G
EG
Kvesitadze
G I
GI
D004795:Enzyme Stability; D019649:Food Industry; D014442:Monophenol Monooxygenase / Q000378:metabolism*; D010544:Peroxidases / Q000378:metabolism*; D010944:Plants / Q000201:enzymology*
D010544:Peroxidases; D014442:Monophenol Monooxygenase