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Oxidative mechanism of chicken wooden breast myofibrillar protein

Ke Wanga,b, Yimin 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.

Keywords

Wooden breastMyofibrillar proteinFree radicalOxidationPhysicochemical propertyMolecular structure

References

[1]

K. Wang, Y. Li, Y.M. Zhang, et al., Improving physicochemical properties of myofibrillar proteins from wooden breast of broiler by diverse glycation strategies, Food Chem. 382 (2022) 132328. https://doi.org/10.1016/j.foodchem.2022.132328.

Crossref Google Scholar
[2]

G. Baldi, F. Soglia, L. Laghi, et al., Comparison of quality traits among breast meat affected by current muscle abnormalities, Food Res. Int. 115 (2019) 369-376. https://doi.org/10.1016/j.foodres.2018.11.020.

Crossref Google Scholar
[3]

C. Praud, J. Jimenez, E. Pampouille, et al., Molecular phenotyping of white striping and wooden breast myopathies in chicken, Front. Physiol. 11 (2020) 633. https://doi.org/10.3389/fphys.2020.00633.

Crossref Google Scholar
[4]

T. Xing, Y. Xu, J. Qi, et al., Effect of high intensity ultrasound on the gelation properties of wooden breast meat with different NaCl contents, Food Chem. 347 (2021). https://doi.org/10.1016/j.foodchem.2021.129031.

Crossref Google Scholar
[5]

B. Pang, B. Bowker, J. Zhang, et al., Prediction of water holding capacity in intact broiler breast fillets affected by the woody breast condition using time-domain NMR, Food Control 118 (2020) 107391. https://doi.org/10.1016/j.foodcont.2020.107391.

Crossref Google Scholar
[6]

A. Morey, A.E. Smith, L.J. Garner, et al., Application of bioelectrical impedance analysis to detect broiler breast filets affected with woody breast myopathy, Front. Physiol. 11 (2020) 808. https://doi.org/10.3389/fphys.2020.00808.

Crossref Google Scholar
[7]

B. Pang, B. Bowker, G. Gamble, et al., Muscle water properties in raw intact broiler breast fillets with the woody breast condition1, Poult. Sci. 99 (2020) 4626-4633. https://doi.org/10.1016/j.psj.2020.05.031.

Crossref Google Scholar
[8]

J. Zhang, H. Zhuang, B. Bowker, et al., Evaluation of multi blade shear (MBS) for determining texture of raw and cooked broiler breast fillets with the woody breast myopathy, Poult. Sci. 100 (2021) 101123. https://doi.org/10.1016/j.psj.2021.101123.

Crossref Google Scholar
[9]

Y. Wang, Y. Yang, D. Pan, et al., Ertbjerg, Metabolite profile based on 1H NMR of broiler chicken breasts affected by wooden breast myodegeneration, Food Chem. 310 (2020) 125852. https://doi.org/10.1016/j.foodchem.2019.125852.

Crossref Google Scholar
[10]

X. Zhang, W. Zhai, S. Li, et al., Schilling, early postmortem proteome changes in normal and woody broiler breast muscles, J. Agric. Food Chem. 68 (2020) 11000-11010. https://doi.org/10.1021/acs.jafc.0c03200.

Crossref Google Scholar
[11]

K. Wang, Y. Li, Y.M. Zhang, et al., Improving myofibrillar proteins solubility and thermostability in low-ionic strength solution: a review, Meat Sci. 189 (2022) 108822. https://doi.org/10.1016/j.meatsci.2022.108822.

Crossref Google Scholar
[12]

M.J. Davies, Protein oxidation and peroxidation, Biochem. J. 473 (2016) 805-825. https://doi.org/10.1042/bj20151227.

Crossref Google Scholar
[13]

M. Demasi, O. Augusto, E. Bechara, et al., Oxidative modification of proteins: from damage to catalysis, signaling, and beyond, Antioxid. Redox Signal. 35 (2021) 1016-1080.

Crossref Google Scholar
[14]

M. Hellwig, The chemistry of protein oxidation in food, Angew. Chem. Int. Ed. 58 (2019) 16742-16763. https://doi.org/10.1002/anie.201814144.

Crossref Google Scholar
[15]

M. Utrera, M. Estévez, Oxidation of myofibrillar proteins and impaired functionality: Underlying mechanisms of the carbonylation pathway, J. Agric. Food Chem. 60 (2012) 8002. https://doi.org/10.1021/jf302111j.

Crossref Google Scholar
[16]

H. Shen, J. Stephen Elmore, M. Zhao, et al., Effect of oxidation on the gel properties of porcine myofibrillar proteins and their binding abilities with selected flavour compounds, Food Chem. 329 (2020) 127032. https://doi.org/10.1016/j.foodchem.2020.127032.

Crossref Google Scholar
[17]

D. Zhang, H.J. Li, A.M. Emara, et al., Effect of in vitro oxidation on the water retention mechanism of myofibrillar proteins gel from pork muscles, Food Chem. 315 (2020) 126226. https://doi.org/10.1016/j.foodchem.2020.126226.

Crossref Google Scholar
[18]

K. Wang, Y. Li, J.X. Sun, et al., Synergistic effect of preheating and different power output high-intensity ultrasound on the physicochemical, structural, and gelling properties of myofibrillar protein from chicken wooden breast, Ultrason. Sonochem. 86 (2022) 106030. https://doi.org/10.1016/j.ultsonch.2022.106030.

Crossref Google Scholar
[19]

R.A. Bailey, K.A. Watson, S.F. Bilgili, et al., The genetic basis of pectoralis major myopathies in modern broiler chicken lines, Poult. Sci. 94 (2015) 2870-2879. https://doi.org/10.3382/ps/pev304.

Crossref Google Scholar
[20]

T. Gao, X. Zhao, R. Li, et al., Synergistic effects of polysaccharide addition-ultrasound treatment on the emulsified properties of low-salt myofibrillar protein, Food Hydrocoll. 123 (2022) 107143. https://doi.org/10.1016/j.foodhyd.2021.107143.

Crossref Google Scholar
[21]

X. Chen, Y. Zou, M. Han, et al., Solubilisation of myosin in a solution of low ionic strength l-histidine: significance of the imidazole ring, Food Chem. 196 (2016) 42-49. https://doi.org/10.1016/j.foodchem.2015.09.039.

Crossref Google Scholar
[22]

D.Y. Li, Z.F. Tan, Z.Q. Liu, et al., Effect of hydroxyl radical induced oxidation on the physicochemical and gelling properties of shrimp myofibrillar protein and its mechanism, Food Chem. 351 (2021). https://doi.org/10.1016/j.foodchem.2021.129344.

Crossref Google Scholar
[23]

Z.B. Zhu, C. Zhao, J.H. Yi, et al., Impact of interfacial composition on lipid and protein co-oxidation in oil-in-water emulsions containing mixed emulisifers, J. Agric. Food Chem. 66 (2018) 4458-4468. https://doi.org/10.1021/acs.jafc.8b00590.

Crossref Google Scholar
[24]

K.J. Davies, M.E. Delsignore, S.W. Lin, Protein damage and degradation by oxygen radicals. Ⅱ. Modification of amino acids, J. Biol. Chem. 262 (1987) 9902-9907. https://doi.org/10.1016/S0021-9258(18)48020-9.

Crossref Google Scholar
[25]

D. Mukherjee, S.K.C. Chang, Y. Zhang, et al., Effects of ultra-high pressure homogenization and hydrocolloids on physicochemical and storage properties of soymilk, J. Food Sci. 82 (2017) 2313-2320. https://doi.org/10.1111/1750-3841.13860.

Crossref Google Scholar
[26]

X. Huang, L. Sun, L. Liu, et al., Study on the mechanism of mulberry polyphenols inhibiting oxidation of beef myofibrillar protein, Food Chem. 372 (2022) 131241. https://doi.org/10.1016/j.foodchem.2021.131241.

Crossref Google Scholar
[27]

D. Zhang, H. Li, Z. Wang, et al., Effects of in vitro oxidation on myofibrillar protein charge, aggregation, and structural characteristics, Food Chem. 332 (2020) 127396. https://doi.org/10.1016/j.foodchem.2020.127396.

Crossref Google Scholar
[28]

Y.L. Bao, P. Ertbjerg, Effects of protein oxidation on the texture and water-holding of meat: a review, Crit. Rev. Food Sci. Nutr. 59 (2019) 3564-3578. https://doi.org/10.1080/10408398.2018.1498444.

Crossref Google Scholar
[29]

W. Sun, M. Zhao, B. Yang, et al., Oxidation of sarcoplasmic proteins during processing of Cantonese sausage in relation to their aggregation behaviour and in vitro digestibility, Meat Sci. 88 (2011) 462-467. https://doi.org/10.1016/j.meatsci.2011.01.027.

Crossref Google Scholar
[30]

Y. Xu, Y. Zhao, Z. Wei, et al., Modification of myofibrillar protein via glycation: physicochemical characterization, rheological behavior and solubility property, Food Hydrocoll. 105 (2020) 105852. https://doi.org/10.1016/j.foodhyd.2020.105852.

Crossref Google Scholar
[31]

X.H. Cui, Y.L.L. Xiong, B.H. Kong, et al., Hydroxyl radical-stressed whey protein isolate: chemical and structural properties, Food Bioproc. Tech. 5 (2012) 2454-2461. https://doi.org/10.1007/s11947-011-0515-9.

Crossref Google Scholar
[32]

K. Wang, Y. Li, Y.M. Zhang, et al., Preheating and high-intensity ultrasound synergistically affect the physicochemical, structural, and gelling properties of chicken wooden breast myofibrillar protein, Food Res. Int. 162 (2022) 111975. https://doi.org/10.1016/j.foodres.2022.111975.

Crossref Google Scholar
[33]

A. Berardo, E. Claeys, E. Vossen, et al., Protein oxidation affects proteolysis in a meat model system, Meat Sci. 106 (2015) 78-84. https://doi.org/10.1016/j.meatsci.2015.04.002.

Crossref Google Scholar
[34]

Y.L. Xiong, D. Park, T. Ooizumi, Variation in the cross-linking pattern of porcine myofibrillar protein exposed to three oxidative environments, J. Agr. Food Chem. 57 (2009) 153-159. https://doi.org/10.1021/jf8024453.

Crossref Google Scholar
[35]

R. Dominguez, M. Pateiro, P.E.S. Munekata, et al., Protein oxidation in muscle foods: a comprehensive review, Antioxidants 11 (2022). https://doi.org/10.3390/antiox11010060.

Crossref Google Scholar
[36]

Y.F. He, H. Huang, L.H. Li, et al., The effects of modified atmosphere packaging and enzyme inhibitors on protein oxidation of tilapia muscle during iced storage, LWT-Food Sci. Technol. 87 (2018) 186-193. https://doi.org/10.1016/j.lwt.2017.08.046.

Crossref Google Scholar
[37]

Q.Q. Fu, R. Liu, H.O. Wang, et al., Effects of oxidation in vitro on structures and functions of myofibrillar protein from beef muscles, J. Agr. Food Chem. 67 (2019) 5866-5873. https://doi.org/10.1021/acs.jafc.9b01239.

Crossref Google Scholar
[38]

W.Z. Sun, F.B. Zhou, D.W. Sun, et al., Effect of oxidation on the emulsifying properties of myofibrillar proteins, Food Bioproc. Tech. 6 (2013) 1703-1712. https://doi.org/10.1007/s11947-012-0823-8.

Crossref Google Scholar
[39]

R. Wen, Y. Hu, L. Zhang, et al., Effect of NaCl substitutes on lipid and protein oxidation and flavor development of Harbin dry sausage, Meat Sci. 156 (2019) 33-43. https://doi.org/10.1016/j.meatsci.2019.05.011.

Crossref Google Scholar
[40]

M. Xia, Y. Chen, J. Guo, et al., Effects of oxidative modification on textural properties and gel structure of pork myofibrillar proteins, Food Res. Int. 121 (2019) 678-683. https://doi.org/10.1016/j.foodres.2018.12.037.

Crossref Google Scholar
[41]

Z.J. Bao, J.P. Wu, Y. Cheng, et al., Effects of lipid peroxide on the structure and gel properties of ovalbumin, Process Biochem. 57 (2017) 124-130. https://doi.org/10.1016/j.procbio.2017.03.009.

Crossref Google Scholar
[42]

E. Dorta, F. Ávila, E. Fuentes-Lemus, et al., Oxidation of myofibrillar proteins induced by peroxyl radicals: role of oxidizable amino acids, Food Res. Int. 126 (2019) 108580. https://doi.org/10.1016/j.foodres.2019.108580.

Crossref Google Scholar
[43]

Y. Li, Q.M. Wang, L.P. Guo, et al., Effects of ultrafine comminution treatment on gelling properties of myofibrillar proteins from chicken breast, Food Hydrocoll. 97 (2019). https://doi.org/10.1016/j.foodhyd.2019.105199.

Crossref Google Scholar
[44]

Y.T. Xu, L.L. Liu, Structural and functional properties of soy protein isolates modified by soy soluble polysaccharides, J. Agric. Food Chem. 64 (2016) 7275-7284. https://doi.org/10.1021/acs.jafc.6b02737.

Crossref Google Scholar
[45]

N. Wang, L. Hu, X. Guo, et al., Effects of malondialdehyde on the protein oxidation and protein degradation of Coregonus Peled myofibrillar protein, J. Food Meas. Charact. (2022). https://doi.org/10.1007/s11694-022-01452-9.

Crossref Google Scholar
[46]

Y. Zheng, L. Zhang, Z.H. Qiu, et al., Comparison of oxidation extent, structural characteristics, and oxidation sites of myofibrillar protein affected by hydroxyl radicals and lipid-oxidizing system, Food Chem. (2022) 133710. https://doi.org/10.1016/j.foodchem.2022.133710.

Crossref Google Scholar
[47]

M. Hosotani, T. Kawasaki, Y. Hasegawa, et al., Physiological and pathological mitochondrial clearance is related to pectoralis major muscle pathogenesis in broilers with wooden breast syndrome, Front. Physiol. 11 (2020). https://doi.org/10.3389/fphys.2020.00579.

Crossref Google Scholar
Food Science and Human Wellness
Volume 13 Issue 6,
November 2024
Pages 3415-3423
DOI: 10.26599/FSHW.2023.9250026
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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Pearson’s correlation coefficients between various indexes.

Zetapotential Solubility Turbidity sulfhydryl Total sulfhydryl Free Carbonyls tyrosine Dimer Hydrophobicity α-Helix β-Sheet β-Turn Random coil
Note: **, Correlation is significant at the 0.01 level; *, Correlation is significant at the 0.05 level.
Zeta-potential 1 -0.6 0.668* -0.930** -0.891** 0.846** 0.776* 0.805** -0.928** 0.958** -0.973** 0.946**
Solubility -0.600* 1 -0.992** 0.489 0.518 -0.873** -0.016 -0.301 0.271 -0.358 0.512 -0.408
Turbidity 0.668* -0.992** 1 -0.589 -0.619* 0.880** 0.079 0.416 -0.366 0.449 -0.603* 0.507
Total sulfhydryl -0.930** 0.489 -0.589 1 0.992** -0.650* -0.669* -0.964** 0.934** -0.950** 0.989** -0.988**
Free sulfhydryl -0.891** 0.518 -0.619* 0.992** 1 -0.62 -0.573 -0.970** -0.884** -0.904** 0.965** -0.963**
Carbonyls 0.846** -0.873** 0.880** -0.650* -0.620* 1 0.478 0.427 -0.591 0.659 -0.725* 0.639*
Dimer tyrosine 0.776* -0.016 0.079 -0.669* -0.573 0.478 1 0.598 -0.889** 0.867** -0.746* 0.774*
Hydrophobicity 0.805** -0.301 0.416 -0.964** -0.970** 0.427 0.598 1 -0.890** 0.888** -0.920** 0.947**
α-Helix -0.928** 0.271 -0.366 0.934** 0.884** -0.591 -0.889** -0.89 1 -0.996** 0.958** -0.977**
β-Sheet 0.958** -0.358 0.449 -0.950** -0.904** 0.659* 0.867** 0.888** -0.996** 1 -0.977** 0.985**
β-Turn -0.973** 0.512 -0.603* 0.989** 0.965** -0.725* -0.746* -0.920** 0.958** -0.977** 1 -0.993**
Random coil 0.946** -0.408 0.507 -0.988** -0.963** 0.639 0.774* 0.947** -0.977** 0.985** -0.993** 1