Oxidation combined with Maillard reaction induced free and protein-bound Nε-carboxymethyllysine and Nε-carboxyethyllysine formation during braised chicken processing

Zongshuai Zhu; Rui Fang; Ming Huang; Yunji Wei; Guanghong Zhou

doi:10.1016/j.fshw.2020.05.013

Food Science and Human Wellness 2020, 9(4): 383-393 https://doi.org/10.1016/j.fshw.2020.05.013

Research Article | Issue | Published: 13 June 2020

Oxidation combined with Maillard reaction induced free and protein-bound N^ε-carboxymethyllysine and N^ε-carboxyethyllysine formation during braised chicken processing

Show Author's Information Hide Author's Information Zongshuai Zhu^{^a}, Rui Fang^{^a}, Ming Huang^{^a^,^b}(

), Yunji Wei^{^c}, Guanghong Zhou^{^a}

College of Food Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu 210095, China

Nanjing Huang jiaoshou Food Science and Technology Co., Ltd, National R & D Center For Poultry Processing Technology, Nanjing, 210095, China

Huai'an Customs, Nanjing, 210095, China

Peer review under responsibility of KeAi Communications Co., Ltd

Keywords:

Oxidation, Maillard reaction, N^ε-carboxymethyllysine, N^ε-carboxyethyllysine, Braised chicken

Cite this article:

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

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Abstract Full text About this article

Abstract

The objective of this work was to investigate the effects of oxidation and Maillard reaction on free and protein-bound N^ε-carboxymethyllysine (CML) and N^ε-carboxyethyllysine (CEL) formation during braised chicken processing. It was found that a positive correlation was observed between carbonyl, fat oxidation, Maillard reaction, CML and CEL (P < 0.05). The sulfhydryl groups could be used as potential indicators to evaluate the compounds' interaction levels between Maillard reaction and protein oxidation. Frying promoted the formation of lysine (Lys), glyoxal (GO) and methylglyoxal (MGO) (P < 0.05); Boiling enhanced the formation of GO and MGO (P < 0.05) while inhibited the levels of Lys (P < 0.05); Sterilizing blocked the formation of MGO and Lys (P < 0.01) but improved GO levels (P < 0.05). Finally, a perspective was concluded that the Maillard reaction combined with oxidation is one of the main reasons for the formation of free and protein-bound CML and CEL during braised chicken processing.

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Oxidation combined with Maillard reaction induced free and protein-bound N^ε-carboxymethyllysine and N^ε-carboxyethyllysine formation during braised chicken processing

Show Author's information Hide Author's Information Zongshuai Zhu^{^a}, Rui Fang^{^a}, Ming Huang^{^a^,^b}(

), Yunji Wei^{^c}, Guanghong Zhou^{^a}

College of Food Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu 210095, China

Nanjing Huang jiaoshou Food Science and Technology Co., Ltd, National R & D Center For Poultry Processing Technology, Nanjing, 210095, China

Huai'an Customs, Nanjing, 210095, China

Peer review under responsibility of KeAi Communications Co., Ltd

Abstract

Keywords: Oxidation, Maillard reaction, N^ε-carboxymethyllysine, N^ε-carboxyethyllysine, Braised chicken

References(32)

[1]

M.W. Poulsen, R.V. Hedegaard, J.M. Andersen, et al., Dragsted, advanced glycation endproducts in food and their effects on health, Food Chem. Toxicol. 60 (2013) 10–37, http://dx.doi.org/10.1016/j.fct.2013.06.052.

DOI Google Scholar

[2]

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

DOI Google Scholar

[3]

Z. 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, Colloids Surf. B Biointerfaces 191 (2020), 111016, http://dx.doi.org/10.1016/j.colsurfb.2020.111016.

DOI Google Scholar

[4]

L. Niu, X. Sun, J. Tang, et al., Combination effects of salts and cold storage on the formation of protein-bound N^ε-(carboxymethyl)lysine and N^ε-(carboxyethyl)lysine in raw and subsequently commercially sterilized ground pork, Food Chem. 264 (2018) 455–461, http://dx.doi.org/10.1016/j. foodchem.2018.05.054.

DOI Google Scholar

[5]

X. Sun, J. Tang, J. Wang, et al., Formation of free and protein-bound carboxymethyllysine and carboxyethyllysine in meats during commercial sterilization, Meat Sci. 116 (2016), http://dx.doi.org/10.1016/j.meatsci.2016. 01.009.

DOI Google Scholar

[6]

Y. Duan, F. Zheng, H. Chen, et al., Analysis of volatiles in Dezhou braised chicken by comprehensive two-dimensional gas chromatography/high resolution-time of flight mass spectrometry, LWT - Food Sci. Technol. 60 (2015) 1235–1242, http://dx.doi.org/10.1016/j.lwt.2014.09.006.

DOI Google Scholar

[7]

Y. Yao, Z. Peng, B. Shao, et al., Effects of frying and boiling on the formation of heterocyclic amines in braised chicken, Poultry Sci. 92 (2013) 3017–3025, http://dx.doi.org/10.3382/ps.2013-03216.

DOI Google Scholar

[8]

Z. Zhu, R. Fang, Y. Cheng, et al., Content of free and protein-binding N^ε-carboxymethyllysine and N^ε-carboxyethyllysine in different parts of braised chicken, Food Sci. Nutr. 8 (2020) 767–776, http://dx.doi.org/10.1002/fsn3.1317.

DOI Google Scholar

[9]

R. Singh, A. Barden, T. Mori, et al., Advanced glycation end-products: a review, Diabetologia 44 (2001) 129–146, http://dx.doi.org/10.1007/s001250051591.

DOI Google Scholar

[10]

I. Baskara, C. Niquet-Leridon, P. Anton, et al., Neoformed compounds from the Maillard reaction in infant formulas: a new risk factor for allergy? EMJ Allergy Immunol. 2 (2017) 87–93.

DOI Google Scholar

[11]

P. Thornalley, Dicarbonyl intermediates in the Maillard reaction, Ann. N.Y. Acad. Sci. 1043 (2005) 111–117, http://dx.doi.org/10.1196/annals.1333.014.

DOI Google Scholar

[12]

M.A. Smith, S. Taneda, P.L. Richey, et al., Advanced Maillard reaction end products are associated with Alzheimer disease pathology, Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 5710–5714, http://dx.doi.org/10.1073/pnas.91.12.5710.

DOI Google Scholar

[13]

L. Yu, Z. He, M. Zeng, et al., Effect of irradiation on N^ε-carboxymethyl-lysine and N^ε-carboxyethyl-lysine formation in cooked meat products during storage, Radiat. Phys. Chem. 120 (2016) 73–80, http://dx.doi.org/10.1016/j.radphyschem.2015.11.020.

DOI Google Scholar

[14]

L. Han, L. Li, B. Li, et al., Review of the characteristics of food-derived and endogenous N^ε-carboxymethyllysine, J. Food Protect. 76 (2013) 912–918, http://dx.doi.org/10.4315/0362-028X.JFP-12-472.

DOI Google Scholar

[15]

Z. 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. Environ. Sci. Health B (2020), http://dx.doi.org/10.1002/jsfa.10460.

DOI Google Scholar

[16]

C. Delgado-Andrade, Carboxymethyl-lysine: thirty years of investigation in the field of AGE formation, Food Funct. 7 (2015), http://dx.doi.org/10.1039/C5FO00918A.

DOI Google Scholar

[17]

X. Sun, J. Huang, T. Li, et al., Effects of preslaughter shackling on postmortem glycolysis, meat quality, changes of water distribution, and protein structures of broiler breast meat, Poultry Sci. 98 (2019), http://dx.doi.org/10.3382/ps/pez175.

DOI Google Scholar

[18]

L. Niu, X. Sun, J. Tang, et al., Free and protein-bound N^ε-carboxymethyllysine and N^ε-carboxyethyllysine in fish muscle: biological variation and effects of heat treatment, J. Food Anal. 57 (2017) 56–63, http://dx.doi.org/10.1016/j.jfca. 2016.12.017.

DOI Google Scholar

[19]

M. Pischetsrieder, Are dietary AGEs/ALEs a risk to human health and, if so, what is the mechanism of action? Mol. Nutr. Food Res. 51 (2007) 1069–1070, http://dx.doi.org/10.1002/mnfr.200790016.

DOI Google Scholar

[20]

G. Liu, Y. Xiong, D. Butterfield, Chemical, physical, and gel-forming properties of oxidized myofibrils and whey- and soy-protein isolates, J. Food Sci. 65 (2000) 811–818, http://dx.doi.org/10.1111/j.1365-2621.2000.tb13592.x.

DOI Google Scholar

[21]

S. Xue, H. Yang, R. Liu, et al., Applications of high pressure to pre-rigor rabbit muscles affect the functional properties associated with heat-induced gelation, Meat Sci. 129 (2017), http://dx.doi.org/10.1016/j.meatsci.2017.03. 006.

DOI Google Scholar

[22]

M. Utrera, D. Morcuende, M. Estévez, Fat content has a significant impact on protein oxidation occurred during frozen storage of beef patties, Lwt - Food Sci. Technol. 56 (2014) 62–68, http://dx.doi.org/10.1016/j.lwt.2013.10. 040.

DOI Google Scholar

[23]

R. Gilbert, R. Brandt, Spectrophotometric determination of methyl glyoxal with 2,4-dinitrophenylhydrazine, Anal. Chem. 47 (1976) 2418–2422, http://dx.doi.org/10.1021/ac60364a003.

DOI Google Scholar

[24]

E. Sawicki, T. Hauser, R. Wilson, A comparison of methods for spot test detection and spectrophotometric determination of glyoxal, Anal. Chem. 34 (1962), http://dx.doi.org/10.1021/ac60184a018.

DOI Google Scholar

[25]

F. Church, H. Swaisgood, D. Porter, et al., Spectrophotometric assay using O-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins1, J. Dairy. Sci. 66 (1983) 1219–1227, http://dx.doi.org/10.3168/jds. S0022-0302(83)81926-2.

DOI Google Scholar

[26]

J. Guan, A. Qiu, X. Liu, et al., Microwave improvement of soy protein isolate–saccharide graft reactions, Food Chem. 97 (2006) 577–585, http://dx.doi.org/10.1016/j.foodchem.2005.05.035.

DOI Google Scholar

[27]

Y. Xiong, S. Srinivasan, G. Liu, Modification of muscle protein functionality by antioxidants, Adv. Exp. Med. Biol. 415 (1997) 95–108, http://dx.doi.org/10.1007/978-1-4899-1792-8 7.

DOI Google Scholar

[28]

M. Yim, H. Yim, C. Lee, et al., Protein glycation: creation of catalytic sites for free radical generation, Ann. Ny. Acad. Sci. 928 (2001) 48–53.

DOI Google Scholar

[29]

P.L. Privalov, G.I. Makhatadze, Heat capacity of proteins: Ⅱ. Partial molar heat capacity of the unfolded polypeptide chain of proteins: protein unfolding effects, J. Mol. Biol. 213 (1990) 385–391, http://dx.doi.org/10.1016/S0022-2836(05)80198-6.

DOI Google Scholar

[30]

T. Hayashi, M. Namiki, Role of sugar fragmentation in early stage browning of amino-carbonyl reaction of sugar with amino acid, Agric. Biol. Chem. 50 (1986) 1965–1970, http://dx.doi.org/10.1271/bbb1961.50.1965.

DOI Google Scholar

[31]

G. Chen, J.S. Smith, Determination of advanced glycation endproducts in cooked meat products, Food Chem. 168 (2015) 190–195, http://dx.doi.org/10.1016/j.foodchem.2014.06.081.

DOI Google Scholar

[32]

M. Khan, H. Liu, J. Wang, et al., Inhibitory effect of phenolic compounds and plant extracts on the formation of advance glycation end products: a comprehensive review, Food Res. Int. 130 (2020), 108933, http://dx.doi.org/10.1016/j.foodres.2019.108933.

DOI Google Scholar

About this article

Publication history

Acknowledgements

Publication history

Received: 03 December 2019

Revised: 24 March 2020

Accepted: 26 May 2020

Published: 13 June 2020

Issue date: December 2020

Copyright

Acknowledgements

This work was supported by China Agriculture Research System (CARS-41-Z06), National Key R&D Program (2016YFD040040303), Key R&D Program (Modern Agriculture) of Jiangsu Province (BE2019308) and Nanjing Customs Scientific Research Project (No. 2020KJ24).