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Thermostabilities of plant phenol oxidase and peroxidase determining the technology of their use in the food industry

Thermostabilities of plant phenol oxidase and peroxidase determining the technology of their use... Stabilities of phenol oxidase and peroxidase from tea plant (Camellia sinensis L.) clone Kolkhida leaves, apple (Mallus 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 (∼10%) upon 20-min incubation at 8°C. Phenol oxidases from tea, walnut, and especially apple, as well as tea peroxidase, were stable during storage. A technology for the treatment of plant oxidases was proposed, based on the use of a natural inhibitor of phenol oxidase and peroxidase, isolated from tea leaves, which solves the problem of residual activities of these enzymes that arises 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied Biochemistry and Microbiology Springer Journals

Thermostabilities of plant phenol oxidase and peroxidase determining the technology of their use in the food industry

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References (15)

Publisher
Springer Journals
Copyright
Copyright © 2005 by MAIK “Nauka/Interperiodica”
Subject
Life Sciences; Medical Microbiology; Biochemistry, general; Microbiology
ISSN
0003-6838
eISSN
1608-3024
DOI
10.1007/s10438-005-0024-6
Publisher site
See Article on Publisher Site

Abstract

Stabilities of phenol oxidase and peroxidase from tea plant (Camellia sinensis L.) clone Kolkhida leaves, apple (Mallus 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 (∼10%) upon 20-min incubation at 8°C. Phenol oxidases from tea, walnut, and especially apple, as well as tea peroxidase, were stable during storage. A technology for the treatment of plant oxidases was proposed, based on the use of a natural inhibitor of phenol oxidase and peroxidase, isolated from tea leaves, which solves the problem of residual activities of these enzymes that arises 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.

Journal

Applied Biochemistry and Microbiology – Springer Journals

Published: Mar 21, 2005

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