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Improved solubility of proteins from white and red clover – inhibition of redox enzymes
Author(s) -
Amer Bashar,
Juul Louise,
Møller Anders Hauer,
Møller Hanne Søndergård,
Dalsgaard Trine Kastrup
Publication year - 2021
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.14632
Subject(s) - polyphenol oxidase , browning , peroxidase , enzyme , biochemistry , chemistry , polyphenol , food science , rubisco , red clover , antioxidant , catechol oxidase , biology , botany
Abstract New alternative protein sources are needed. Clover grasses as white clover (WC) and red clover (RC) may provide a novel protein source to achieve high‐quality food protein. To prevent protein oxidation, endogenous oxidative enzymes as polyphenol oxidase (PPO) and peroxidases were inhibited with sulphite. RC showed higher PPO activity than WC. Low sulphite inhibited the PPO activity in both species, but browning still occurred in RC. Sulphite did not affect the polyphenol (PP) content in WC, rather suggesting peroxidase than PPO activity. In RC juice, the PP content increased in a dose‐dependent manner with increasing sulphite. High sulphite impaired browning and increased the content of soluble rubisco in RC, mainly by increasing the content of native rubisco. In vitro digestibility of RC protein increased with increasing sulphite. In conclusion, sulphite inhibited oxidative enzymes and increased the quality of protein extracted from WC and RC.