Journal
FOOD CHEMISTRY
Volume 309, Issue -, Pages -Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2019.125651
Keywords
Myoglobin oxidation; Polyacrylamide gel electrophoresis (PAGE); Intrinsic fluorescence; Circular dichroism (CD) spectroscopy
Funding
- Chinese National Natural Science Foundation [31771993, 31271903]
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The effects of low frequency magnetic field on myoglobin (Mb) oxidation stability were evaluated by treatments at 0, 3, 6, 9, 12 mT and storage for 10 h. The results showed that Mb oxidation was inhibited under all magnetic field treatments, due to the increase of total sulfhydryl and free amino groups (9 or 12 mT) from unfolding of Mb clusters (3, 9, 12 mT) as well as beta-turn and beta-sheet structures (9 or 12 mT). The unfolding also induced (i) the destruction or burial of iron porphyrin and tyrosine residues; (ii) the exposure of tryptophan; (iii) more uniform Mb particle size distribution (3, 9, 12 mT) and increased zeta potential (3, 6, 12 mT). Overall, magnetic field promoted exposed active groups as the preferred oxidation target, thus decreasing the oxidation rate of central iron atoms. It also promoted Mb stability by redistributing particle size and increasing zeta potential.
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