The most significant issue influencing the preservation and sale of chicken is its oxidative behavior. The effect of hydroxyl radical oxidation on the hydrolysis of myofibrillar protein by μ-calpain in vitro was explored in this work, which looked at the alteration of chicken myofibrillar protein by hydroxyl radical oxidation. The carbonyl, dimerized tyrosine content and surface hydrophobicity of myofibrillar protein increased significantly as H₂O₂ concentration increased, tryptophan fluorescence intensity and total sulfhydryl content decreased. Compared with the control group, the carbonyl content of 10 mmol/L H₂O₂ treatment group increased to 1.7 nmol/mg protein, the surface hydrophobicity and the dimer tyrosine content increased 32.41% and 14.73%, respectively, the total sulfhydryl content decreased to 67.93 nmol/mg protein. The protein cross-linked and aggregated, and the oxidative modification of chicken myofibrillar protein promoted degradation. Desmin degradation by μ-calcinase is inhibited by MHC, actin, and troponin-T. The findings revealed that oxidation influenced the hydrolysis of myofibrillar protein and the tenderness of chicken after slaughter.

Novelty impact statement

The chicken myofibrillar proteins were cross-linked and aggregated by hydroxyl radical oxidation.
The oxidative modification of hydroxyl radical changes the sensitivity of protein to μ-calpain.
The oxidative modification of chicken myofibrillar protein improved the tenderness of postmortem chicken by promoting the degradation of MHC, actin, and troponin-T caused by μ-calcium-activating enzyme.

CONFLICT OF INTEREST

The authors have declared no conflicts of interest for this article.

Open Research

DATA AVAILABILITY STATEMENT

The data that support the findings of this study are available from the corresponding author upon reasonable request.

REFERENCES

Bao, Y., & Ertbjerg, P. (2019). Effects of protein oxidation on the texture and water-holding of meat: A review. Critical Reviews in Food Science and Nutrition, 59(22), 3564–3578. https://doi.org/10.1080/10408398.2018.1498444
10.1080/10408398.2018.1498444
CAS PubMed Web of Science® Google Scholar
Bhat, Z. F., Morton, J. D., Mason, S. L., & Bekhit, A. E. D. A. (2018). Role of calpain system in meat tenderness: A review. Food Science and Human Wellness, 7(3), 196–204. https://doi.org/10.1016/j.fshw.2018.08.002
10.1016/j.fshw.2018.08.002
Web of Science® Google Scholar
Biswas, A. K., Tandon, S., & Mandal, P. K. (2020). Calpain-assisted postmortem aging of meat and its detection methods. In Meat quality analysis (pp. 101–114). Academic Press. https://doi.org/10.1016/B978-0-12-819233-7.00007-0
10.1016/B978-0-12-819233-7.00007-0
Google Scholar
Chen, J., Zhang, X., Fu, M., Chen, X., Pius, B. A., & Xu, X. (2021). Ultrasound-assisted covalent reaction of myofibrillar protein: The improvement of functional properties and its potential mechanism. Ultrasonics Sonochemistry, 76, 105652. https://doi.org/10.1016/j.ultsonch.2021.105652
10.1016/j.ultsonch.2021.105652
CAS PubMed Web of Science® Google Scholar
Chen, Q., Huang, J., Huang, F., Huang, M., & Zhou, G. (2014). Influence of oxidation on the susceptibility of purified desmin to degradation by μ-calpain, caspase-3 and-6. Food Chemistry, 150, 220–226. https://doi.org/10.1016/j.foodchem.2013.10.149
10.1016/j.foodchem.2013.10.149
CAS PubMed Web of Science® Google Scholar
Chen, X., Xiong, Y. L., & Xu, X. (2019). High-pressure homogenization combined with sulfhydryl blockage by hydrogen peroxide enhance the thermal stability of chicken breast myofibrillar protein aqueous solution. Food Chemistry, 285, 31–38. https://doi.org/10.1016/j.foodchem.2019.01.131
10.1016/j.foodchem.2019.01.131
CAS PubMed Web of Science® Google Scholar
Deng, X., Lei, Y., Liu, J., Zhang, J., & Qin, J. (2019). Biochemical changes of Coregonus peled myofibrillar proteins isolates as affected by HRGS oxidation system. Journal of Food Biochemistry, 43(2), e12710. https://doi.org/10.1111/jfbc.12710
10.1111/jfbc.12710
PubMed Web of Science® Google Scholar
Duan, X., Li, M., Shao, J., Chen, H., Xu, X., Jin, Z., & Liu, X. (2018). Effect of oxidative modification on structural and foaming properties of egg white protein. Food Hydrocolloids, 75, 223–228. https://doi.org/10.1016/j.foodhyd.2017.08.008
10.1016/j.foodhyd.2017.08.008
CAS Web of Science® Google Scholar
Estévez, M. (2011). Protein carbonyls in meat systems: A review. Meat Science, 89(3), 259–279. https://doi.org/10.1016/j.meatsci.2011.04.025
10.1016/j.meatsci.2011.04.025
CAS PubMed Web of Science® Google Scholar
Fu, Q., Liu, R., Wang, H., Hua, C., Song, S., Zhou, G., & Zhang, W. (2019). Effects of oxidation in vitro on structures and functions of myofibrillar protein from beef muscles. Journal of Agricultural and Food Chemistry, 67(20), 5866–5873. https://doi.org/10.1021/acs.jafc.9b01239
10.1021/acs.jafc.9b01239
CAS PubMed Web of Science® Google Scholar
Fu, Q. Q., Liu, R., Zhang, W., Ben, A., & Wang, R. (2020). In vitro susceptibility of oxidized myosin by μ-calpain or caspase-3 and the determination of the oxidation sites of myosin heavy chains. Journal of Agricultural and Food Chemistry, 68(32), 8629–8636. https://doi.org/10.1021/acs.jafc.0c01065
10.1021/acs.jafc.0c01065
CAS PubMed Web of Science® Google Scholar
Gonçalves, T. M., de Almeida Regitano, L. C., Koltes, J. E., Cesar, A. S., da Silva Andrade, S. C., Mourão, G. B., Gasparin, G., Moreira, G. C., Fritz-Waters, E., Reecy, J. M., & Coutinho, L. L. (2018). Gene co-expression analysis indicates potential pathways and regulators of beef tenderness in Nellore cattle. Frontiers in Genetics, 9, 441. https://doi.org/10.3389/fgene.2018.00441
10.3389/fgene.2018.00441
CAS PubMed Web of Science® Google Scholar
Guo, X., Hu, L., Wang, Z., Zhu, X., Deng, X., & Zhang, J. (2021). Effect of rutin on the physicochemical and gel characteristics of myofibrillar protein under oxidative stress. Journal of Food Biochemistry, 45(10), e13928. https://doi.org/10.1111/jfbc.13928
10.1111/jfbc.13928
CAS PubMed Web of Science® Google Scholar
Guo, X., Qiu, H., Deng, X., Mao, X., Guo, X., Xu, C., & Zhang, J. (2019). Effect of chlorogenic acid on the physicochemical and functional properties of Coregonus peled myofibrillar protein through hydroxyl radical oxidation. Molecules, 24(17), 3205. https://doi.org/10.3390/molecules24173205
10.3390/molecules24173205
CAS PubMed Web of Science® Google Scholar
Jongberg, S., Lund, M. N., & Skibsted, L. H. (2017). Protein oxidation in meat and meat products. Challenges for antioxidative protection. In Global food security and wellness (pp. 315–337). Springer. https://doi.org/10.1007/978-1-4939-6496-3
10.1007/978-1-4939-6496-3_17
Google Scholar
Lana, A., & Zolla, L. (2016). Proteolysis in meat tenderization from the point of view of each single protein: A proteomic perspective. Journal of Proteomics, 147, 85–97. https://doi.org/10.1016/j.jprot.2016.02.011
10.1016/j.jprot.2016.02.011
CAS PubMed Web of Science® Google Scholar
Leal-Gutiérrez, J. D., Elzo, M. A., Johnson, D. D., Scheffler, T. L., Scheffler, J. M., & Mateescu, R. G. (2018). Association of μ-calpain and calpastatin polymorphisms with meat tenderness in a Brahman–angus population. Frontiers in Genetics, 9, 56. https://doi.org/10.3389/fgene.2018.00056
10.3389/fgene.2018.00056
PubMed Web of Science® Google Scholar
Li, F., Zhong, Q., Kong, B., Wang, B., Pan, N., & Xia, X. (2020). Deterioration in quality of quick-frozen pork patties induced by changes in protein structure and lipid and protein oxidation during frozen storage. Food Research International, 133, 109142. https://doi.org/10.1016/j.foodres.2020.109142
10.1016/j.foodres.2020.109142
CAS PubMed Web of Science® Google Scholar
Li, K., Fu, L., Zhao, Y. Y., Xue, S. W., Wang, P., Xu, X. L., & Bai, Y. H. (2020). Use of high-intensity ultrasound to improve emulsifying properties of chicken myofibrillar protein and enhance the rheological properties and stability of the emulsion. Food Hydrocolloids, 98, 105275. https://doi.org/10.1016/j.foodhyd.2019.105275
10.1016/j.foodhyd.2019.105275
CAS Web of Science® Google Scholar
Liu, G., Xiong, Y. L., & Butterfield, D. A. (2000). Chemical, physical, and gel-forming properties of oxidized myofibrils and whey-and soy-protein isolates. Journal of Food Science, 65(5), 811–818. https://doi.org/10.1111/j.1365-2621.2000.tb13592.x
10.1111/j.1365-2621.2000.tb13592.x
CAS Web of Science® Google Scholar
Liu, P., Zhang, Z., Guo, X., Zhu, X., Mao, X., Guo, X., Deng, X., & Zhang, J. (2021). μ-Calpain oxidation and proteolytic changes on myofibrillar proteins from Coregonus Peled in vitro. Food Chemistry, 361, 130100. https://doi.org/10.1016/j.foodchem.2021.130100
10.1016/j.foodchem.2021.130100
CAS PubMed Web of Science® Google Scholar
Liu, R., Lonergan, S., Steadham, E., Zhou, G., Zhang, W., & Huff-Lonergan, E. (2019). Effect of nitric oxide on myofibrillar proteins and the susceptibility to calpain-1 proteolysis. Food Chemistry, 276, 63–70. https://doi.org/10.1016/j.foodchem.2018.10.005
10.1016/j.foodchem.2018.10.005
CAS PubMed Web of Science® Google Scholar
Lonergan, E. H., Zhang, W., & Lonergan, S. M. (2010). Biochemistry of postmortem muscle—Lessons on mechanisms of meat tenderization. Meat Science, 86(1), 184–195. https://doi.org/10.1016/j.meatsci.2010.05.004
10.1016/j.meatsci.2010.05.004
CAS PubMed Web of Science® Google Scholar
Pearce, K. L., Rosenvold, K., Andersen, H. J., & Hopkins, D. L. (2011). Water distribution and mobility in meat during the conversion of muscle to meat and ageing and the impacts on fresh meat quality attributes—A review. Meat Science, 89(2), 111–124. https://doi.org/10.1016/j.meatsci.2011.04.007
10.1016/j.meatsci.2011.04.007
PubMed Web of Science® Google Scholar
Qin, J., Deng, X., Lei, Y., Liu, P., Lu, S., & Zhang, J. (2020). Effects of μ-calpain oxidation on Coregonus peled myofibrillar protein degradation in vitro. Journal of Food Science, 85(3), 682–688. https://doi.org/10.1111/1750-3841.15048
10.1111/1750-3841.15048
CAS PubMed Web of Science® Google Scholar
Rawdkuen, S., Jaimakreu, M., & Benjakul, S. (2013). Physicochemical properties and tenderness of meat samples using proteolytic extract from Calotropis procera latex. Food Chemistry, 136(2), 909–916. https://doi.org/10.1016/j.foodchem.2012.08.077
10.1016/j.foodchem.2012.08.077
CAS PubMed Web of Science® Google Scholar
Sante-Lhoutellier, V., Aubry, L., & Gatellier, P. (2007). Effect of oxidation on in vitro digestibility of skeletal muscle myofibrillar proteins. Journal of Agricultural and Food Chemistry, 55(13), 5343–5348. https://doi.org/10.1021/jf070252k
10.1021/jf070252k
CAS PubMed Web of Science® Google Scholar
Smuder, A. J., Kavazis, A. N., Hudson, M. B., Nelson, W. B., & Powers, S. K. (2010). Oxidation enhances myofibrillar protein degradation via calpain and caspase-3. Free Radical Biology and Medicine, 49(7), 1152–1160. https://doi.org/10.1016/j.freeradbiomed.2010.06.025
10.1016/j.freeradbiomed.2010.06.025
CAS PubMed Web of Science® Google Scholar
Sun, W., Zhou, F., Sun, D. W., & Zhao, M. (2013). Effect of oxidation on the emulsifying properties of myofibrillar proteins. Food and Bioprocess Technology, 6(7), 1703–1712. https://doi.org/10.1007/s11947-012-0823-8
10.1007/s11947-012-0823-8
CAS Web of Science® Google Scholar
Wang, J. Y., Yang, Y. L., Tang, X. Z., Ni, W. X., & Zhou, L. (2017). Effects of pulsed ultrasound on rheological and structural properties of chicken myofibrillar protein. Ultrasonics Sonochemistry, 38, 225–233. https://doi.org/10.1016/j.ultsonch.2017.03.018
10.1016/j.ultsonch.2017.03.018
CAS PubMed Web of Science® Google Scholar
Wang, K. Q., Luo, S. Z., Zhong, X. Y., Cai, J., Jiang, S. T., & Zheng, Z. (2017). Changes in chemical interactions and protein conformation during heat-induced wheat gluten gel formation. Food Chemistry, 214, 393–399. https://doi.org/10.1016/j.foodchem.2016.07.037
10.1016/j.foodchem.2016.07.037
CAS PubMed Web of Science® Google Scholar
Xia, T., Cao, Y., Chen, X., Zhang, Y., Xue, X., Han, M., & Xu, X. (2018). Effects of chicken myofibrillar protein concentration on protein oxidation and water holding capacity of its heat-induced gels. Journal of Food Measurement and Characterization, 12(4), 2302–2312. https://doi.org/10.1007/s11694-018-9847-8
10.1007/s11694-018-9847-8
Web of Science® Google Scholar
Xiong, Y. L., Blanchard, S. P., Ooizumi, T., & Ma, Y. (2010). Hydroxyl radical and ferryl-generating systems promote gel network formation of myofibrillar protein. Journal of Food Science, 75(2), C215–C221. https://doi.org/10.1111/j.1750-3841.2009.01511.x
10.1111/j.1750-3841.2009.01511.x
CAS PubMed Web of Science® Google Scholar
Xiong, Y. L., & Decker, E. A. (1995). Alterations of muscle protein functionality by oxidative and antioxidative processes 1. Journal of Muscle Foods, 6(2), 139–160. https://doi.org/10.1111/j.1745-4573.1995.tb00563.x
10.1111/j.1745-4573.1995.tb00563.x
Google Scholar
Zhang, D., Li, H., Emara, A. M., Hu, Y., Wang, Z., Wang, M., & He, Z. (2020). Effect of in vitro oxidation on the water retention mechanism of myofibrillar proteins gel from pork muscles. Food Chemistry, 315, 126226. https://doi.org/10.1016/j.foodchem.2020.126226
10.1016/j.foodchem.2020.126226
CAS PubMed Web of Science® Google Scholar
Zhang, L., Li, Q., Hong, H., & Luo, Y. (2020). Prevention of protein oxidation and enhancement of gel properties of silver carp (Hypophthalmichthys molitrix) surimi by addition of protein hydrolysates derived from surimi processing by-products. Food Chemistry, 316, 126343. https://doi.org/10.1016/j.foodchem.2020.126343
10.1016/j.foodchem.2020.126343
CAS PubMed Web of Science® Google Scholar
Zhang, W., Xiao, S., & Ahn, D. U. (2013). Protein oxidation: Basic principles and implications for meat quality. Critical Reviews in Food Science and Nutrition, 53(11), 1191–1201. https://doi.org/10.1080/10408398.2011.577540
10.1080/10408398.2011.577540
CAS PubMed Web of Science® Google Scholar
Zhang, X., Huang, W., & Xie, J. (2019). Effect of different packaging methods on protein oxidation and degradation of grouper (Epinephelus coioides) during refrigerated storage. Food, 8(8), 325. https://doi.org/10.3390/foods8080325
10.3390/foods8080325
CAS PubMed Web of Science® Google Scholar
Zhang, Z., Liu, P., Deng, X., Guo, X., Mao, X., Guo, X., & Zhang, J. (2021). Effects of hydroxyl radical oxidation on myofibrillar protein and its susceptibility to μ-calpain proteolysis. LWT-Food Science and Technology, 137, 110453. https://doi.org/10.1016/j.lwt.2020.110453
10.1016/j.lwt.2020.110453
CAS Web of Science® Google Scholar

Citing Literature

All articles

Effects of hydroxyl radical oxidation on physicochemical properties and degradation of chicken myofibrillar protein

Abstract

Novelty impact statement

CONFLICT OF INTEREST

Open Research

DATA AVAILABILITY STATEMENT

REFERENCES

Citing Literature

References

Information

About Wiley Online Library

Help & Support

Opportunities

Connect with Wiley

Effects of hydroxyl radical oxidation on physicochemical properties and degradation of chicken myofibrillar protein

Abstract

Novelty impact statement

CONFLICT OF INTEREST

Open Research

DATA AVAILABILITY STATEMENT

REFERENCES

Citing Literature

References

Related

Information