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Oxidative mechanism of chicken wooden breast myofibrillar protein

Ke Wanga,bYimin Zhangb ()Jingxin Suna,c()
College of Food Science & Engineering, Qingdao Agricultural University, Qingdao 266109, China
College of Food Science & Engineering, Shandong Agricultural University, Tai’an 271018, China
Shandong Research Center for Meat Food Quality Control, Qingdao Agricultural University, Qingdao 266109, China

Peer review under responsibility of Tsinghua University Press.

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Abstract

To explore the oxidation mechanism of wooden breast myofibrillar protein (WBMP), oxidative breast MP (OBMP) was obtained from different doses (3, 10, and 20 mmol/L) of H2O2 oxidized normal breast MP (NBMP). The results showed that the Zeta-potential, particle size, solubility, sulfhydryl, and carbonyl contents of OBMP-3 (3 mmol/L, low-dose free radicals) and WBMP were similar. Fluorescence spectrum analysis showed that the oxidation of low-dose free radicals led to a significant increase in the surface hydrophobicity (from 214.03 ± 10.03 to 393.50 ± 10.33) and tryptophan fluorescence intensity (from 185.71 to 568.32). In addition, the α-helix content of WBMP decreased significantly from (37.46 ± 1.15)% (NBMP) to (34.70 ± 2.04)%, while β-sheet and random coil contents increased significantly (P < 0.05) from (14.37 ± 0.69)% and (22.24 ± 0.78)% (NBMP) to (17.70 ± 0.87)% and (25.20 ± 1.47)% (WBMP). In summary, low-dose free radical oxidation attacks protein groups, inducing secondary and tertiary structural changes, leading to the formation of WBMP. This work will provide a theoretical basis at the molecular level for exploring the mechanism of functional degradation of WBMP.

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Food Science and Human Wellness
Pages 3415-3423
Cite this article:
Wang K, Zhang Y, Sun J. Oxidative mechanism of chicken wooden breast myofibrillar protein. Food Science and Human Wellness, 2024, 13(6): 3415-3423. https://doi.org/10.26599/FSHW.2023.9250026
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