Effects of hydroxyl radical oxidation on the structural and functional properties of mutton myosin

To research the impact of free radical oxidation on myosin, we established a hydroxyl radical oxidation system using iron/hydrogen peroxide/ascorbic acid. By varying hydrogen peroxide concentrations (0, 0.5, 1, 5, 10, 20 mmol.L-1), we achieved different oxidation levels of myosin and investigated th...

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Main Authors: Yingying Cao, Huaiyu Li, Fubing Wang
Format: Article
Language:English
Published: Czech Academy of Agricultural Sciences 2024-12-01
Series:Czech Journal of Food Sciences
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Online Access:https://cjfs.agriculturejournals.cz/artkey/cjf-202406-0005_effects-of-hydroxyl-radical-oxidation-on-the-structural-and-functional-properties-of-mutton-myosin.php
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author Yingying Cao
Huaiyu Li
Fubing Wang
author_facet Yingying Cao
Huaiyu Li
Fubing Wang
author_sort Yingying Cao
collection DOAJ
description To research the impact of free radical oxidation on myosin, we established a hydroxyl radical oxidation system using iron/hydrogen peroxide/ascorbic acid. By varying hydrogen peroxide concentrations (0, 0.5, 1, 5, 10, 20 mmol.L-1), we achieved different oxidation levels of myosin and investigated the effects on its structural and functional characteristics. The results showed that when the H2O2 concentration was 20 mmol.L-1, compared with the control group, the carbonyl content of myosin was 2.376 times higher, the sulfhydryl content was decreased by 37.02%, the surface hydrophobicity was increased by 59.13%, the solubility was decreased by 19.54%, and the turbidity was significantly increased (P < 0.05). Myosin emulsification, emulsification stability, and foaming capacity initially increased and then they diminished, and the maximum value was reached when the H2O2 concentration was 5 mmol.L-1, whereas foaming stability remained relatively unchanged. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis research revealed increased crosslinking and protein polymerisation in oxidised myosin. The secondary structure of myosin measured by Fourier infrared spectroscopy showed that the α-helix content decreased by 14.41% and the β-fold content increased by 44.50%. These results suggested that oxidative modification alters the structural and functional properties of myosin, providing valuable insights for its structural and functional analyses.
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spelling doaj-art-7ba8d8cd9afd47588051c8fda0bdc8de2025-08-20T02:57:25ZengCzech Academy of Agricultural SciencesCzech Journal of Food Sciences1212-18001805-93172024-12-0142642343410.17221/133/2024-CJFScjf-202406-0005Effects of hydroxyl radical oxidation on the structural and functional properties of mutton myosinYingying Cao0Huaiyu Li1Fubing Wang2College of Life Science and Engineering, Lanzhou University of Technology, Lanzhou, ChinaCollege of Life Science and Engineering, Lanzhou University of Technology, Lanzhou, ChinaCollege of Life Science and Engineering, Lanzhou University of Technology, Lanzhou, ChinaTo research the impact of free radical oxidation on myosin, we established a hydroxyl radical oxidation system using iron/hydrogen peroxide/ascorbic acid. By varying hydrogen peroxide concentrations (0, 0.5, 1, 5, 10, 20 mmol.L-1), we achieved different oxidation levels of myosin and investigated the effects on its structural and functional characteristics. The results showed that when the H2O2 concentration was 20 mmol.L-1, compared with the control group, the carbonyl content of myosin was 2.376 times higher, the sulfhydryl content was decreased by 37.02%, the surface hydrophobicity was increased by 59.13%, the solubility was decreased by 19.54%, and the turbidity was significantly increased (P < 0.05). Myosin emulsification, emulsification stability, and foaming capacity initially increased and then they diminished, and the maximum value was reached when the H2O2 concentration was 5 mmol.L-1, whereas foaming stability remained relatively unchanged. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis research revealed increased crosslinking and protein polymerisation in oxidised myosin. The secondary structure of myosin measured by Fourier infrared spectroscopy showed that the α-helix content decreased by 14.41% and the β-fold content increased by 44.50%. These results suggested that oxidative modification alters the structural and functional properties of myosin, providing valuable insights for its structural and functional analyses.https://cjfs.agriculturejournals.cz/artkey/cjf-202406-0005_effects-of-hydroxyl-radical-oxidation-on-the-structural-and-functional-properties-of-mutton-myosin.phpsds-pageftiroxidation of proteinsfunctional characteristicsstructural characteristics
spellingShingle Yingying Cao
Huaiyu Li
Fubing Wang
Effects of hydroxyl radical oxidation on the structural and functional properties of mutton myosin
Czech Journal of Food Sciences
sds-page
ftir
oxidation of proteins
functional characteristics
structural characteristics
title Effects of hydroxyl radical oxidation on the structural and functional properties of mutton myosin
title_full Effects of hydroxyl radical oxidation on the structural and functional properties of mutton myosin
title_fullStr Effects of hydroxyl radical oxidation on the structural and functional properties of mutton myosin
title_full_unstemmed Effects of hydroxyl radical oxidation on the structural and functional properties of mutton myosin
title_short Effects of hydroxyl radical oxidation on the structural and functional properties of mutton myosin
title_sort effects of hydroxyl radical oxidation on the structural and functional properties of mutton myosin
topic sds-page
ftir
oxidation of proteins
functional characteristics
structural characteristics
url https://cjfs.agriculturejournals.cz/artkey/cjf-202406-0005_effects-of-hydroxyl-radical-oxidation-on-the-structural-and-functional-properties-of-mutton-myosin.php
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AT fubingwang effectsofhydroxylradicaloxidationonthestructuralandfunctionalpropertiesofmuttonmyosin