Oxidative mechanism of chicken wooden breast myofibrillar protein
(
), Jingxin Suna,c()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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References
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
M.J. Davies, Protein oxidation and peroxidation, Biochem. J. 473 (2016) 805-825. https://doi.org/10.1042/bj20151227.
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.
M. Hellwig, The chemistry of protein oxidation in food, Angew. Chem. Int. Ed. 58 (2019) 16742-16763. https://doi.org/10.1002/anie.201814144.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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