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Research Article | Open Access

Heat-induced oxidation and proteomic changes to yak milk protein

Jinchao Zhang1,§, Yu Zhang2,§, Rong Jing1, Senbiao Shu1, Jie Yang1, Liang Li1,3, Wenhan Wang4( ), Zhendong Liu1,3( )
Tibet Agriculture & Animal Husbandry University, Nyingchi 860000, China
College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China
The Provincial and Ministerial Co-founded Collaborative Innovation Center for R&D in Tibet Characteristic Agricultural and Animal Husbandry Resources, Tibet Agriculture & Animal Husbandry University, Nyingchi 860000, China
National Engineering Research Center of Edible Fungi, Key Laboratory of Applied Mycological Resources and Utilization of Ministry of Agriculture, Shanghai Key Laboratory of Agricultural Genetics and Breeding; Institute of Edible Fungi, Shanghai Academy of Agricultural Sciences, Shanghai 201403, China

§These authors contributed equally to this work.

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Graphical Abstract

Abstract

Yak milk is a dietary source of high-quality protein in the plateau region of China but as yet uncharacterized oxidative changes occur during heat treatment. Therefore, oxidation of and proteomic changes to milk proteins from plateau pasture-fed yaks after at different temperatures were investigated. Content of carbonyl groups, surface hydrophobicity increased, and total sulfhydryl, disulfide bond content decreased. Endogenous fluorescence intensity decreased after at increasing temperatures, indicating increased particle size, and absolute values of the zeta potential decreased. Analysis by Fourier transform infrared spectroscopy showed changes of the secondary structure, with relative content of α-helices increasing and then decreasing, β-sheet showed a trend of decreasing and then increasing while the relative content of random curl did not change. The close range of the β-turn gradually decreased, breaking the protein microstructure, and folding stacking occurred. Proteomics analyses showed a temperature dependent effect. Sixty-two proteins were suppressed and 49 elevated with 4 pathways up-regulated and 7 down-regulated at 65 °C. Thirty-one proteins were suppressed and 37 elevated with 5 pathways up-regulated and 4 down-regulated at 90 °C. The most extensive changes were observed at 120 °C, when 327 proteins were suppressed and 308 elevated with 11 pathways up-regulated and 33 down-regulated.

Keywords

oxidationstructureproteinproteomicsyak milkheat treatments

References

[1]

M. Ajmal, M. Nadeem, M. Imran, et al., Lipid compositional changes and oxidation status of ultra-high temperature treated milk, Lipids Health Dis. 17 (2018) 227. https://doi.org/10.1186/s12944-018-0869-3.
Crossref Google Scholar
[2]

F. Mahmoodani, C. O. Perera, G. Abernethy, et al., Lipid oxidation and vitamin D3 degradation in simulated whole milk powder as influenced by processing and storage, Food Chem. 261 (2018) 149–156. https://doi.org/10.1016/j.foodchem.2018.04.043.
Crossref Google Scholar
[3]

C. B. Afonso, C. M. Spickett, Lipoproteins as targets and markers of lipoxidation, Redox Biol. 23 (2019) 101066. https://doi.org/10.1016/j.redox.2018.101066.
Crossref Google Scholar
[4]

J. H. Kim, H. J. Lee, D. M. Shin, et al., The dry-aging and heating effects on protein characteristics of beef longissiumus dorsi, Korean J. Food Sci. Anim. Resour. 38(5) (2018) 1101–1108. https://doi.org/10.5851/kosfa.2018.e43.
Crossref Google Scholar
[5]

R. T. Dean, S. Fu, R. Stocker, et al., Biochemistry and pathology of radical-mediated protein oxidation, Biochem. J. 324(1) (1997) 1–18. https://doi.org/10.1006/abbi.1997.9982.
Crossref Google Scholar
[6]
A. Aicardo, M. Mastrogiovanni, A. Cassina, et al., Propagation of free-radical reactions in concentrated protein solutions, Free Radic. Res. 2018, 52(2): 159–170. https://doi.org/10.1080/10715762.2017.1420905.
Crossref
[7]
W. G. Sun, W. L. Xu, H. K. Liu, et al., γ-Tocotrienol induces mitochondria-mediated apoptosis in human gastric adenocarcinoma SGC-7901 cells, J. Nutr. Biochem. 20(4) (2009) 276–284. https://doi.org/10.1016/j.jnutbio.2008.03.003.
Crossref
[8]

J. Y. Zhang, Y. L. Zhao, Y. T. Ding, et al., Relationships of lipid oxidation and protein oxidation with flavor characteristics of meat products, J. Nuclear Agri. Sci. 32(7) (2018) 1417–1424. https://doi.org/10.11869/j.issn.100-8551.2018.07.1417.
Crossref Google Scholar
[9]
A. B. Gurung, A. Bhattacharjee, Impact of tyrosine nitration at positions Tyr307 and Tyr335 on structural dynamics of lipoprotein-associated phospholipase A2–A therapeutically important cardiovascular biomarker for atherosclerosis, Int. J. Biol. Macromol. (2018) 1956–1964. https://doi.org/10.1016/j.ijbiomac.2017.10.068.
Crossref
[10]

I. Majkutewicz, E. Kurowska, M. Podlacha, et al., Age-dependent effects of dimethyl fumarate on cognitive and neuropathological features in the streptozotocin-induced rat model of Alzheimer’s disease, Brain Res. 1686 (2018) 19–33. https://doi.org/10.1016/j.brainres.2018.02.016.
Crossref Google Scholar
[11]

A. L. Bulteau, N. P. Mena, F. Auchère, et al., Dysfunction of mitochondrial Lon protease and identification of oxidized protein in mouse brain following exposure to MPTP: implications for Parkinson disease, Free Radic. Biol. Med. 108 (2017) 236–246. https://doi.org/10.1016/j.freeradbiomed.2017.03.036.
Crossref Google Scholar
[12]

Z. L. Li, Y. H. Shi, Y. Y. Ding, et al., Dietary oxidized tyrosine (O-Tyr) stimulates TGF-β1-induced extracellular matrix production via the JNK/p38 signaling pathway in rat kidneys, Amino Acids 49(2) (2017) 241–260. https://doi.org/10.1007/s00726-016-2353-6.
Crossref Google Scholar
[13]

A. H. Bryk, M. Konieczynska, P. Rostoff, et al., Plasma protein oxidation as a determinant of impaired fibrinolysis in type 2 diabetes, Thromb. Haemost. 119(2) (2019) 213–222. https://doi.org/ 10.1055/s-0038-1676609.
Crossref Google Scholar
[14]

Y. H. Yang, H. Zhang, B. Yan, et al., Health effects of dietary oxidized tyrosine and dityrosine administration in mice with nutrimetabolomic strategies, J. Agric. Food Chem. 65(32) (2017) 6957–6971. https://doi.org/10.1021/acs.jafc.7b02003.
Crossref Google Scholar
[15]

Y. Y. Ding, X. R. Cheng, Z. Q. Li, et al., Effect of dietary oxidized tyrosine products on insulin secretion via the oxidative stress-induced mitochondria damage in mice pancreas, RSC Adv. 7(43) (2017) 26809–26826. https://doi.org/10.1039/c7ra02945d.
Crossref Google Scholar
[16]

Y. Y. Ding, Z. Q. Li, X. R. Cheng, et al., Dityrosine administration induces dysfunction of insulin secretion accompanied by diminished thyroid hormones T3 function in pancreas of mice, Amino Acids 49 (2017) 1401–1414. https://doi.org/10.1007/s00726-017-2442-1.
Crossref Google Scholar
[17]

Y. Y. Ding, X. Tang, X. R. Cheng, et al., Effects of dietary oxidized tyrosine products on insulin secretion via the thyroid hormone T3-regulated TRβ1-Akt-mTOR pathway in the pancreas, RSC Adv. 7(86) (2017) 54610–54625. https://doi.org/10.1039/C7RA10435A.
Crossref Google Scholar
[18]

J. Lu, X. Y. Wang, W. Q. Zhang, et al., Comparative proteomics of milk fat globule membrane in different species reveals variations in lactation and nutrition, Food Chem. 196 (2016) 665–672. https://doi.org/10.1016/j.foodchem.2015.10.005.
Crossref Google Scholar
[19]

J. Lu, S. Zhang, L. Liu, et al., Comparative proteomics analysis of human and ruminant milk serum reveals variation in protection and nutrition, Food Chem. 261 (2018) 274–282. https://doi.org/10.1016/j.foodchem.2018.04.065.
Crossref Google Scholar
[20]

X. P. Chang, J. M. Zhang, Z. D. Liu, et al., Integrated proteomic, phosphoproteomic, and N-glycoproteomic analyses of the longissimus thoracis of yaks, Curr. Res. Food Sci. 5 (2022) 1494–1507. https://doi.org/10.1016/j.crfs.2022.09.012.
Crossref Google Scholar
[21]

J. Xiao, J. Q. Wang, R. Y. Gan, et al., Quantitative N-glycoproteome analysis of bovine milk and yogurt, Curr. Res. Food Sci. 5 (2022) 182–190. https://doi.org/10.1016/j.crfs.2022.01.003.
Crossref Google Scholar
[22]

W. K. Kim, A. Henschel, C. Winter, et al., The many faces of protein-protein interactions: a compendium of interface geometry, PLoS Comput. Biol. 2(9) (2006) e124. https://doi.org/10.1371/journal.pcbi.0020124.
Crossref Google Scholar
[23]

L. Zhang, S. Boeren, J. A. Hageman, et al., Bovine milk proteome in the first 9 days: protein interactions in maturation of the immune and digestive system of the newborn, PLoS ONE 10(2) (2015) e0116710. https://doi.org/10.1371/journal.pone.0116710.
Crossref Google Scholar
[24]

F. Mestdagh, B. Kerkaert, T. Cucu, et al., Interaction between whey proteins and lipids during light-induced oxidation, Food Chem. 126(3) (2011) 1190–1197. https://doi.org/10.1016/j.foodchem.2010.11.170.
Crossref Google Scholar
[25]

Y. H. Shao, Z. T. Gan, E. Epifanovsky, et al., Advances in molecular quantum chemistry contained in the Q-Chem 4 program package, Mol. Phys. 113(2) (2014) 184–215. https://doi.org/10.1080/00268976.2014.952696.
Crossref Google Scholar
[26]
Y. G. Cao, A. D. True, J. Chen, et al., Dual role (anti- and pro-oxidant) of gallic acid in mediating myofibrillar protein gelation and gel in vitro digestion, J. Agric. Food Chem. 64(15) (2016) 3054–3061. https://doi.org/10.1021/acs.jafc.6b00314.
Crossref
[27]

R. J. Wang, R. N. Wang, X. Y. Niu, et al., Role of astrocytes-derived D-serine in PFOS-induced neurotoxicity through NMDARs in the rat primary hippocampal neurons, Toxicology 422 (2019) 14–24. https://doi.org/10.1016/j.tox.2019.04.007.
Crossref Google Scholar
[28]

K. Kieserling, T. M. Vu, S. Drusch, et al., Impact of pectin-rich orange fibre on gel characteristics and sensory properties in lactic acid fermented yoghurt, Food Hydrocoll. 94 (2019) 152–163. https://doi.org/10.1016/j.foodhyd.2019.02.051.
Crossref Google Scholar
[29]
L. Li, L. Shi, S. D. Yang, et al., SIRT7 is a histone desuccinylase that functionally links to chromatin compaction and genome stability, Nature Commun. 7 (2016) 12235. https://doi.org/10.1038/ncomms12235.
Crossref
[30]

Y. P. Du, T. X. Cai, T. T. Li, et al., Lysine malonylation is elevated in type 2 diabetic mouse models and enriched in metabolic associated proteins, Mol. Cell. Proteomics 14(1) (2015) 227–236. https://doi.org/10.1074/mcp.M114.041947.
Crossref Google Scholar
[31]

C. Song, Y. B. Liu, R. Fontana, et al., Elimination of unaltered DNA in mixed clinical samples via nuclease-assisted minor-allele enrichment, Nucleic Acids Res. 44(19) (2016) e146. https://doi.org/ 10.1093/nar/gkw650.
Crossref Google Scholar
[32]

D. Zhao, S. W. Zou, Y. Liu, et al., Lysine-5 acetylation negatively regulates lactate dehydrogenase A and is decreased in pancreatic cancer, Cancer Cell. 23(4) (2013) 464–476. https://doi.org/10. 1016/J.CCR.2013.02.005.
Crossref Google Scholar
[33]

X. Y. Ye, X. M. Niu, L. P. Gu, et al., Desuccinylation of pyruvate kinase M2 by SIRT5 contributes to antioxidant response and tumor growth, Oncotarget 8(4) (2016) 6984–6993. https://doi.org/10.18632/oncotarget.14346.
Crossref Google Scholar
[34]

M. Chevion, E. Berenshtein, E. R. Stadtman, Human studies related to protein oxidation: protein carbonyl content as a marker of damage, Free Radic Res. 33 (2000) S99–S108.
Google Scholar
[35]
M. Hamada, S. Ishizaki, T. Nagai, Variations of SH content and kamaboko-gel forming ability of shark muscle proteins by electrolysis, 42(3) (1994) 131–135.
[36]

F. Li, B. Wang, Q. Liu, et al., Changes in myofibrillar protein gel quality of porcine longissimus muscle induced by its stuctural modification under different thawing methods, Meat Sci. 147 (2019) 108–115. https://doi.org/10.1016/j.meatsci.2018.09.003.
Crossref Google Scholar
[37]

R. Lametsch, J. Knudsen, P. Ertbjerg, et al., Therkildsen, novel method for determination of myofibril fragmentation post-mortem, Meat Sci. 75(4) (2007) 719–724. https://doi.org/10.1016/j.meatsci.2006.10.002.
Crossref Google Scholar
[38]

Z. Ceylan, G. F. U. Sengor, O. Sağdıç, et al., A novel approach to extend microbiological stability of sea bass ( Dicentrarchus labrax) fillets coated with electrospun chitosan nanofibers, LWT-Food Sci. Technol. 79 (2017) 367–375. https://doi.org/10.1016/j.lwt.2017.01.062.
Crossref Google Scholar
[39]

M. Estévez, C. J. C. R. I. F. S. Luna, Nutrition, Dietary protein oxidation: a silent threat to human health?, Crit. Rev. Food Sci. Nutr. 57(17) (2017) 3781–3793. https://doi.org/10.1080/10408398.2016.1165182.
Crossref Google Scholar
[40]
E. Çarkcioğlu, A. J. Rosenthal, K. Candoğan, Rheological and textural properties of sodium reduced salt soluble myofibrillar protein gels containing sodium tri-polyphosphate, J. Texture Stud. 2016. https://doi.org/10.1111/jtxs.12169.
Crossref
[41]

I. A. Jaffe, Adverse effects profile of sulfhydryl compounds in man, Am. J. Med. 80(3) (1986) 471–476. https://doi.org/10.1016/0002-9343(86)90722-9.
Crossref Google Scholar
[42]

F. Hatahet, L. W. Ruddock, R. Signaling, Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation, Antioxid. Redox Signal. 11(11) (2019) 2807–2850. https://doi.org/10.1089/ars.2009.2466.
Crossref Google Scholar
[43]

S. Bette, H. Breer, J. Krieger, et al., Probing a pheromone binding protein of the silkmoth Antheraea polyphemus by endogenous tryptophan fluorescence, Insect Biochem. Mol. Biol. 32(3) (2002) 241–246. https://doi.org/10.1016/S0965-1748(01)00171-0.
Crossref Google Scholar
[44]

W. Z. Sun, F. B. Zhou, D. W. Sun, et al., Effect of oxidation on the emulsifying properties of myofibrillar proteins, Jiangsu J. Agric. Sci. 14(5) (2013) 1703–1712. https://doi.org/10.1007/s11947-012-0823-8.
Crossref Google Scholar
[45]

L. Y. Cai, L. Y. Nian, G. H. Zhao, et al., Effect of herring antifreeze protein combined with chitosan magnetic nanoparticles on quality attributes in red sea bream ( Pagrosomus major), Food Bioprocess Tech. 12 (2019) 409–421. https://doi.org/10.1007/s11947-018-2220-4.
Crossref Google Scholar
[46]

C. Q. Li, Y. L. Xiong, J. Chen, et al., Oxidation-induced unfolding facilitates myosin cross-linking in myofibrillar protein by microbial transglutaminase, J. Agric. Food Chem. 60(32) (2012) 8020–8027. https://doi.org/10.1021/jf302150h.
Crossref Google Scholar
[47]

G. B. Jameson, J. J. Adams, L. K. Creamer, Flexibility, functionality and hydrophobicity of bovine β-lactoglobulin, Int. Dairy J. 12(4) (2002) 319–329. https://doi.org/10.1016/S0958-6946(02)00028-6.
Crossref Google Scholar
[48]
L. A. Sazanov, P. Hinchliffe, Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus, Science 311 (2006) 1430–1436. https://doi.org/10.1126/science.1123809.
Crossref
[49]

D. Isenberg, A. Rahman, Systemic lupus erythematosus: 2005 annus mirabilis?, Nat. Clin. Pract. Rheumatol. 2(3) (2006) 145–152. https://doi.org/10.1038/ncprheum0116.
Crossref Google Scholar
[50]

C. C. Mok, C. S. Lau, Pathogenesis of systemic lupus erythematosus, J. Clin. Pathol. 56(7) (2003) 481–490. https://doi.org/10.1136/jcp.56.7.481.
Crossref Google Scholar
[51]

H. T. Cook, M. J. N. C. P. R. Botto, Mechanisms of disease: the complement system and the pathogenesis of systemic lupus erythematosus, Nat. Clin. Pract. Rheumatol. 2(6) (2006) 330–337. https://doi.org/10.1038/ncprheum0191.
Crossref Google Scholar
[52]

A. van der Flier, A. Sonnenberg, Function and interactions of integrins, Cell Tissue Res. 305(3) (2001) 285–298. https://doi.org/10.1007/s004410100417.
Crossref Google Scholar
[53]
M. Yepes, TWEAK and Fn14 in the neurovascular unit, Front. Immunol. 4 (2013) 367. https://doi.org/10.3389/fimmu.2013.00367.
Crossref
Food Science of Animal Products
Volume 2 Issue 1,
March 2024
Article number: 9240056
DOI: 10.26599/FSAP.2024.9240056
Cite this article:
Zhang J, Zhang Y, Jing R, et al. Heat-induced oxidation and proteomic changes to yak milk protein. Food Science of Animal Products, 2024, 2(1): 9240056. https://doi.org/10.26599/FSAP.2024.9240056

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Received: 07 April 2024
Revised: 15 April 2024
Accepted: 07 May 2024
Published: 11 June 2024
© Beijing Academy of Food Sciences 2024.

Food Science of Animal Products published by Tsinghua University Press. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
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