Electrophoretic pattern, thermal denaturation, and in vitro digestibility of oxidized myosin

Gang Liu; Youling L. Xiong

doi:10.1021/jf990520h

Electrophoretic pattern, thermal denaturation, and in vitro digestibility of oxidized myosin

Gang Liu, Youling L. Xiong

Animal and Food Sciences

Research output: Contribution to journal › Article › peer-review

170 Scopus citations

Abstract

Physicochemical changes and in vitro digestibility of chicken breast myosin oxidized with a nonenzymic free-radical-generating system (FeCl₃/H₂O₂/ascorbate) were studied by SDS-PAGE, differential scanning calorimetry, and o-phthaldialdehyde assay. Oxidation caused fragmentation and polymerization of myosin. Myosin polymers were cross-linked mainly through disulfide bonds. Hydroxyl radicals destabilized myosin, lowering its denaturation temperature by up to 4°C. Oxidized myosin also produced a new thermal transition in the 60-80 °C temperature range, which could be attributed to the formation of disulfide-stabilized polymers. The proteolytic susceptibility of myosin to pepsin, trypsin, and chymotrypsin was increased by oxidation. Under nonreducing conditions, however, oxidized myosin showed decreased digestibility. The results may help explain variations in the functionality and nutritional quality of muscle foods in meat processing in which oxidation is involved.

Original language	English
Pages (from-to)	624-630
Number of pages	7
Journal	Journal of Agricultural and Food Chemistry
Volume	48
Issue number	3
DOIs	https://doi.org/10.1021/jf990520h
State	Published - 2000

Keywords

Digestibility
Electrophoresis
Myosin
Oxidation
Thermal denaturation

ASJC Scopus subject areas

General Chemistry
General Agricultural and Biological Sciences

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10.1021/jf990520h

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title = "Electrophoretic pattern, thermal denaturation, and in vitro digestibility of oxidized myosin",

abstract = "Physicochemical changes and in vitro digestibility of chicken breast myosin oxidized with a nonenzymic free-radical-generating system (FeCl3/H2O2/ascorbate) were studied by SDS-PAGE, differential scanning calorimetry, and o-phthaldialdehyde assay. Oxidation caused fragmentation and polymerization of myosin. Myosin polymers were cross-linked mainly through disulfide bonds. Hydroxyl radicals destabilized myosin, lowering its denaturation temperature by up to 4°C. Oxidized myosin also produced a new thermal transition in the 60-80 °C temperature range, which could be attributed to the formation of disulfide-stabilized polymers. The proteolytic susceptibility of myosin to pepsin, trypsin, and chymotrypsin was increased by oxidation. Under nonreducing conditions, however, oxidized myosin showed decreased digestibility. The results may help explain variations in the functionality and nutritional quality of muscle foods in meat processing in which oxidation is involved.",

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AU - Liu, Gang

AU - Xiong, Youling L.

PY - 2000

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N2 - Physicochemical changes and in vitro digestibility of chicken breast myosin oxidized with a nonenzymic free-radical-generating system (FeCl3/H2O2/ascorbate) were studied by SDS-PAGE, differential scanning calorimetry, and o-phthaldialdehyde assay. Oxidation caused fragmentation and polymerization of myosin. Myosin polymers were cross-linked mainly through disulfide bonds. Hydroxyl radicals destabilized myosin, lowering its denaturation temperature by up to 4°C. Oxidized myosin also produced a new thermal transition in the 60-80 °C temperature range, which could be attributed to the formation of disulfide-stabilized polymers. The proteolytic susceptibility of myosin to pepsin, trypsin, and chymotrypsin was increased by oxidation. Under nonreducing conditions, however, oxidized myosin showed decreased digestibility. The results may help explain variations in the functionality and nutritional quality of muscle foods in meat processing in which oxidation is involved.

AB - Physicochemical changes and in vitro digestibility of chicken breast myosin oxidized with a nonenzymic free-radical-generating system (FeCl3/H2O2/ascorbate) were studied by SDS-PAGE, differential scanning calorimetry, and o-phthaldialdehyde assay. Oxidation caused fragmentation and polymerization of myosin. Myosin polymers were cross-linked mainly through disulfide bonds. Hydroxyl radicals destabilized myosin, lowering its denaturation temperature by up to 4°C. Oxidized myosin also produced a new thermal transition in the 60-80 °C temperature range, which could be attributed to the formation of disulfide-stabilized polymers. The proteolytic susceptibility of myosin to pepsin, trypsin, and chymotrypsin was increased by oxidation. Under nonreducing conditions, however, oxidized myosin showed decreased digestibility. The results may help explain variations in the functionality and nutritional quality of muscle foods in meat processing in which oxidation is involved.

KW - Digestibility

KW - Electrophoresis

KW - Myosin

KW - Oxidation

KW - Thermal denaturation

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Electrophoretic pattern, thermal denaturation, and in vitro digestibility of oxidized myosin

Abstract

Keywords

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