AI Chat Paper
Note: Please note that the following content is generated by AMiner AI. SciOpen does not take any responsibility related to this content.
{{lang === 'zh_CN' ? '文章概述' : 'Summary'}}
{{lang === 'en_US' ? '中' : 'Eng'}}
Chat more with AI
PDF (2.6 MB)
Collect
Submit Manuscript AI Chat Paper
Show Outline
Outline
Show full outline
Hide outline
Outline
Show full outline
Hide outline
Research Article | Open Access

The effect of protein oxidation on the formation of advanced glycation end products after chicken myofibrillar protein glycation

Zongshuai ZhuaAnthony Pius BasseyaMing Huanga,b( )Iftikhar Ali Khanc
College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China
National R&D Center for Poultry Processing Technology, Nanjing Huangjiaoshou Food Science and Technology Co., Ltd., Nanjing 211200, China
Institution of Agricultural Products Processing, Jiangsu Academy of Agricultural Sciences, Nanjing 210095, China

Peer review under responsibility of KeAi Communications Co., Ltd.

Show Author Information

Abstract

Investigation that protein oxidation to the formation of advanced glycation end products (AGEs) after chicken myofibrillar protein glycation is limited. Models of protein oxidation induced by different concentrations of hydroxyl radicals (·OH) were developed after the chicken myofibrillar protein mild glycation (MPG). Results exhibited that levels of AGEs and surface hydrophobicity (H0) steadily increased with the addition of hydrogen peroxide (H2O2) concentration. However, levels of sulfhydryl group, free amino group, and particle size gradually decreased with the H2O2 concentration. The protein carbonyl value increased in H2O2 concentration until 10 mmol/L. Pearson's correlation indicated that MPG structure modification (unfolding and degradation) induced by protein oxidation were significantly positively correlated with AGEs concentration (P < 0.05). Finally, a mechanism was proposed to hypothesize the effect of protein oxidation on the formation of AGEs under MPG conditions.

References

[1]

X.P. Li, C.L. Liu, J.X. Wang, et al., Effect of hydroxyl radicals on biochemical and functional characteristics of myofibrillar protein from large yellow croaker (Pseudosciaena crocea), J. Food Biochem. 44(1) (2020) e13084. https://doi.org/10.1111/jfbc.13084.

[2]

D. Park, Y.L. Xiong, A.L. Alderton, Concentration effects of hydroxyl radical oxidizing systems on biochemical properties of porcine muscle myofibrillar protein, Food Chem. 101(3) (2007) 1239-1246. https://doi.org/10.1016/j.foodchem.2006.03.028.

[3]

Y.L. Xiong, S.P. Blanchard, T. Ooizumi T, et al., Hydroxyl radical and ferryl-generating systems promote gel network formation of myofibrillar protein, J. Food Sci. 75(2) (2010) 215-221. https://doi.org/10.1111/j.1750-3841.2009.01511.x.

[4]

R. Nagai R, K. Ikeda, T. Highashi, et al., Hydroxyl radical mediates Nε-(carboxymethyl)lysine formation from Amadori product, Biochem. Biophys. Res. Commun. 234(1) (1997) 167-172. https://doi.org/10.1006/bbrc.1997.6608.

[5]

L.G. Yu, M. Chai, M.M Zeng, et al., Effect of lipid oxidation on the formation of Nε-carboxymethyl-lysine and Nε-carboxyethyl-lysine in Chinese-style sausage during storage, Food Chem. 269 (2018) 466-472. https://doi.org/10.1016/j.foodchem.2018.07.051.

[6]

Z.S. Zhu, M. Huang, Y.Q. Cheng, et al., A comprehensive review of Nε-carboxymethyllysine and Nε-carboxyethyllysine in thermal processed meat products, Trends Food Sci. Tech. 98 (2020) 30-40. https://doi.org/10.1016/j.tifs.2020.01.021.

[7]

Z.S. Zhu, R. Fang, Y.Q. Cheng, et al., Content of free and protein-binding Nε-carboxymethyllysine and Nε-carboxyethyllysine in different parts of braised chicken, Food Sci. Nutr. 8(2) (2020) 767-776. https://doi.org/10.1002/fsn3.1317.

[8]

Z.S. Zhu, R. Fang, M. Huang, et al., Oxidation combined with Maillard reaction induced free and protein-bound Nε-carboxymethyllysine and Nε-carboxyethyllysine formation during braised chicken processing, Food Sci. Hum. Well. 9(4) (2020) 383-393. https://doi.org/10.1016/j.fshw.2020.05.013.

[9]

Z.S. Zhu, R. Fang, D. Zhao, et al., Nε-carboxymethyllysine and Nε-carboxyethyllysine kinetics and water loss analysis during chicken braising, J. Sci. Food Agr. 101(2) (2021) 388-397. https://doi.org/10.1002/jsfa.10528.

[10]

Z.S. Zhu, S.H. Huang, I. A. Khan, et al., The effect of oxidation and Maillard reaction on formation of Nε-carboxymethyllysine and Nε-carboxyethyllysine in prepared chicken breast, Cyta-J. Food 17(1) (2019) 685-694. https://doi.org/10.1080/19476337.2019.1636139.

[11]

Z.S. Zhu, R. Fang, D. Zhao, et al., Effect of malondialdehyde on oil-in-water emulsifying behavior and Maillard reaction of chicken sarcoplasmic protein in emulsion, Colloid. Surface B. 191 (2020) 111016. https://doi.org/10.1016/j.colsurfb.2020.111016.

[12]

Z.S. Zhu, R. Fang, I. Ali, et al., Impact of methylglyoxal modification of chicken sarcoplasmic protein emulsions on emulsifying properties, rheological behavior and advanced glycation end products, J. Sci. Food Agr. 100(11) (2020) 4208-4216. https://doi.org/10.1002/jsfa.10460.

[13]

Z.S. Zhu, Y.Q. Cheng, S.H, Huang, et al., Format ion of Nε-carboxymethyllysine and Nε-carboxyethyllysine in prepared chicken breast by pan frying, J. Food Protect. 82(12) (2019) 2154-2160. https://doi.org/10.4315/0362-028X.JFP-19-319.

[14]

Q. Wu, S.M. Tang, L. Zhang, et al., The inhibitory effect of the catechin structure on advanced glycation end product formation in alcoholic media, Food Funct. 11(6) (2020) 5396-5408. https://doi.org/10.1039/C9FO02887K.

[15]

D. Zhao, B.L. Sheng, H. L, et al., Glycation from α-dicarbonyl compounds has different effects on the heat-induced aggregation of bovine serum albumin and β-casein, Food Chem. 340 (2021) 128108. https://doi.org/10.1016/j.foodchem.2020.128108.

[16]

Z.S. Zhu, J. Yang, X.H, Zhou, et al., Comparison of two kinds of peroxyl radical pretreatment at chicken myofibrillar proteins glycation on the formation of Nε-carboxymethyllysine and Nε-carboxyethyllysine, Food Chem. 353 (2021) 129487. https://doi.org/10.1016/j.foodchem.2021.129487.

[17]

Z.L. Zhang, Z.Y. Xiong, S.F. Lu, et al., Effects of oxidative modification on the functional, conformational and gelling properties of myofibrillar proteins from Culter alburnus, Int. J. Biol. Macromol. 162 (2020) 1442-1452. https://doi.org/10.1016/j.ijbiomac.2020.08.052.

[18]

Y.J. Xu, Y.Q. Zhao, Z.X. 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.

[19]

Y.G Cao, Y.L. Xiong, Chlorogenic acid-mediated gel formation of oxidatively stressed myofibrillar protein, Food Chem. 180 (2015) 235-243. https://doi.org/10.1016/j.foodchem.2015.02.036.

[20]

C.Q. Li, Y.L. Xiong, J. Chen, 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.

[21]

G.L. Bian, S.W. Xue, Y.J. Xu, et al., Improved gelation functionalities of myofibrillar protein from pale, soft and exudative chicken breast meat by nonenzymatic glycation with glucosamine, Int. J. Food Sci. Technol. 53(8) (2018) 2006-2014. https://doi.org/10.1111/ijfs.13789.

[22]

A.G. Gornall, C. J. Bardawill, M.M. David, Determination of serum proteins by means of the biuret reaction, J. Biol. Chem. 177(2) (1949) 751-766. https://doi.org/10.1016/S0021-9258(18)57021-6.

[23]

X. Zhao, Y. Hrynets, M. Betti, Cold non-enzymatic browning of glucosamine in the presence of metmyoglobin induces glucosone and deoxymyoglobin formation, Food Chem. 305 (2020) 125504. https://doi.org/10.1016/j.foodchem.2019.125504.

[24]

P. Salvador, M.Toldrà, E.Saguer, et al., Microstructure–function relationships of heat-induced gels of porcine haemoglobin, Food Hydrocoll. 23(7) (2009) 1654-1659. https://doi.org/10.1016/j.foodhyd.2008.12.003.

[25]

K. Li, L, Fu, Y.Y. Zhao, et al., Use of high-intensity ultrasound to improve emulsifying properties of chicken myofibrillar protein and enhance the rheological properties and stability of the emulsion, Food Hydrocoll. 98 (2020) 105275. https://doi.org/10.1016/j.foodhyd.2019.105275.

[26]

Y. Zou, P.P. Xu, H.H. Wu, et al., Effects of different ultrasound power on physicochemical property and functional performance of chicken actomyosin, Int. J. Biol. Macromol. 113 (2018) 640-647. https://doi.org/10.1016/j.ijbiomac.2018.02.039.

[27]

D. Zhao, J. He, X.Y. Zou, et al., Influence of salting process on the structure and in vitro digestibility of actomyosin, J. Food Sci. Technol. 57(5) (2020) 1763-1773. https://doi.org/10.1007/s13197-019-04210-w.

[28]

L.Y. Shan, Y. Li, Q.M. Wang, et al., Profiles of gelling characteristics of myofibrillar proteins extracted from chicken breast: effects of temperatures and phosphates, LWT-Food Sci. Technol. 129 (2020) 109525. https://doi.org/10.1016/j.lwt.2020.109525.

[29]

X. Zhao, T. Xing, P. Wang, et al., Oxidative stability of isoelectric solubilization/precipitation-isolated PSE-like chicken protein, Food Chem. 283 (2019) 646-655. https://doi.org/10.1016/j.foodchem.2019.01.035.

[30]

S. Arfin, G.A. Siddiqui, A. Naeem, et al., Inhibition of advanced glycation end products by isoferulic acid and its free radical scavenging capacity: an in vitro and molecular docking study, Int. J. Biol. Macromol. 118 (2018) 1479-1487. https://doi.org/10.1016/j.ijbiomac.2018.06.182.

[31]

X.H. Sun, J.M. Tang, J. Wang, et al., Formation of advanced glycation endproducts in ground beef under pasteurisation conditions, Food Chem. 172 (2015) 802-807. https://doi.org/10.1016/j.foodchem.2014.09.129.

[32]

D. Zhao, T.T. Le, L.B. Larsen, et al., Effect of glycation derived from α-dicarbonyl compounds on the in vitro digestibility of β-casein and β-lactoglobulin: a model study with glyoxal, methylglyoxal and butanedione, Food Res. Int. 102 (2017) 313-322. https://doi.org/10.1016/j.foodres.2017.10.002.

[33]

Y.L. Xiong, D. Park, T. Ooizumi, Variation in the cross-linking pattern of porcine myofibrillar protein exposed to three oxidative environments, J. Agric. Food Chem. 57(1) (2009) 153-159. https://doi.org/10.1021/jf8024453.

[34]

X. Chen, Y.L. Xiong, X.L. Xu, High-pressure homogenization combined with sulfhydryl blockage by hydrogen peroxide enhance the thermal stability of chicken breast myofibrillar protein aqueous solution, Food Chem. 285 (2019) 31-38. https://doi.org/10.1016/j.foodchem.2019.01.131.

[35]

D. Zhao, D. X u, B.L. Sheng, et al., A pplication of preheating treatment in up- and down-regulating the glycation process of dietary proteins, Food Hydrocoll. 98 (2020) 105264. https://doi.org/10.1016/j.foodhyd.2019.105264.

[36]

B.M. Nyaisaba, S. Hatab, X.X. Liu, et al., Physicochemical changes of myofibrillar proteins of squid (Argentinus ilex) induced by hydroxyl radical generating system, Food Chem. 297 (2019) 124941. https://doi.org/10.1016/j.foodchem.2019.06.008.

[37]

X. Chen, R.Y. Zhou, X.L. Xu, et al., Structural modification by high-pressure homogenization for improved functional properties of freeze-dried myofibrillar proteins powder, Food Res. Int. 100 (2017) 193-200. https://doi.org/10.1016/j.foodres.2017.07.007.

[38]

I. Khalifa, R. Sobhy, A. Nawaz, et al., Cyanidin 3-rutinoside defibrillated bovine serum albumin under the glycation-promoting conditions: a study with multispectral, microstructural, and computational analysis, Int. J. Biol. Macromol. 162 (2020) 1195-1203. https://doi.org/10.1016/j.ijbiomac.2020.06.243.

[39]

R. Sobhy, F.C. Zhan, E. Mekawi, et al., The noncovalent conjugations of bovine serum albumin with three structurally different phytosterols exerted antiglycation effects: a study with AGEs-inhibition, multispectral, and docking investigations, Bioorg. Chem. 94 (2020) 103478. https://doi.org/10.1016/j.bioorg.2019.103478.

[40]

R. Sobhy, I. Khalifa, H.S. Liang, et al., Phytosterols disaggregate bovine serum albumin under the glycation conditions through interacting with its glycation sites and altering its secondary structure elements, Bioorg. Chem. 101 (2020) 104047. https://doi.org/10.1016/j.bioorg.2020.104047.

[41]

Y.L. Xiong, A.Q. Guo, Animal and plant protein oxidation: chemical and functional property significance, Foods 10(1) (2021) 40. https://doi.org/10.3390/foods10010040.

[42]

X. Zhao, Y.G. Zhou, L. Zhao, et al., Vacuum impregnation of fish gelatin combined with grape seed extract inhibits protein oxidation and degradation of chilled tilapia fillets, Food Chem. 294 (2019) 316-325. https://doi.org/10.1016/j.foodchem.2019.05.054.

[43]

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.

Food Science and Human Wellness
Pages 1571-1579
Cite this article:
Zhu Z, Bassey AP, Huang M, et al. The effect of protein oxidation on the formation of advanced glycation end products after chicken myofibrillar protein glycation. Food Science and Human Wellness, 2023, 12(5): 1571-1579. https://doi.org/10.1016/j.fshw.2023.02.013

686

Views

26

Downloads

11

Crossref

8

Web of Science

12

Scopus

0

CSCD

Altmetrics

Received: 23 April 2021
Revised: 06 June 2021
Accepted: 27 June 2021
Published: 21 March 2023
© 2023 Beijing Academy of Food Sciences.

This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

Return