Effects of Oxidation and Different Ionic Environment on the Binding of Pork Myofibrillar Protein to Flavor Substances

GAN Xiao; ZHAO Ling; WU Qian; CHEN Xiwen

doi:10.13386/j.issn1002-0306.2022010139

Volume 43 Issue 23

Nov. 2022

Turn off MathJax

Article Contents

Abstract

References

Science and Technology of Food Industry > 2022 > 43(23): 35-41. > DOI: 10.13386/j.issn1002-0306.2022010139

GAN Xiao, ZHAO Ling, WU Qian, et al. Effects of Oxidation and Different Ionic Environment on the Binding of Pork Myofibrillar Protein to Flavor Substances[J]. Science and Technology of Food Industry, 2022, 43(23): 35−41. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2022010139.

Citation:

PDF (2903 KB)

Effects of Oxidation and Different Ionic Environment on the Binding of Pork Myofibrillar Protein to Flavor Substances

GAN Xiao^{1, 2,},
ZHAO Ling¹,
WU Qian^{1, 2},
CHEN Xiwen^{1, 2, ,}

1.
School of Life Science & Technology, Mianyang Teachers’ College, Mianyang 621000, China
2.
Engineering Technology Research Center of Animal Disease Control and Healthy Breeding, Mianyang 621000, China

More Information

Received Date: January 17, 2022
Available Online: October 05, 2022

Graphical Abstract

Abstract

Abstract

The changes of structure and function of pork myofibrillar protein induced by oxidation and its ability to bind flavor substances under different ionic conditions were studied. 2-methyl-butanal, 3-methyl-butanal, hexanal, octanal and nonanal were selected as volatile compounds in the experiment. The ability of myofibrillar protein to bind volatile compounds was observed by headspace combined gas chromatography. The results confirmed that the secondary structure and function of oxidized myofibrillar protein changed. Oxidized myofibrillar protein could promote the release of 2-methyl-butanal and nonanal. Moreover, the effect of oxidized myofibrillar protein on 3-methyl-butanal, hexanal and octanal was dependent on AAPH concentration. The addition of Na⁺ promoted the release of hexanal, while the addition of Na⁺, K⁺, Ca²⁺ and Mg²⁺ promoted the absorption of 2-methyl-butanal, 3-methyl-butanal, octanal and nonal. Consequently, during the processing and storage of meat and meat products, oxidation of meat protein could change its structure and function, and then affect the ability of protein to combine flavor substances. In addition, sodium chloride is partially replaced by other salts in meat products, resulting in changes in the ionic environment of proteins, resulting in changes in the ability of proteins to combine flavor substances, thus changing the flavor of meat products.
- pork,
- myofibrillar protein,
- oxidation,
- headspace sampling,
- gas chromatography

FullText(HTML)

References (34)

References

[1]	甘潇, 李洪军, 王兆明, 等. KCl部分替代NaCl对腊肉蛋白质氧化, 降解及质构的影响[J]. 食品与发酵工业,2019,45(4):167−173. [GAN X, LI H J, WANG Z M, et al. Effects of partial substitution of NaCl by KCl on protein oxidation, degradation and texture of bacon[J]. Food and Fermentation Industries,2019,45(4):167−173.
[2]	殷小钰, 刘昊天, 邹汶蓉, 等. 肌肉蛋白与挥发性风味物质的相互作用机制及影响因素研究进展[J]. 食品科学,2020,41(15):288−294. [YIN X Y, LIU H T, ZOU W R, et al. Research progress on the mechanism and influencing factors of interaction between muscle protein and volatile flavor substances[J]. Food Science,2020,41(15):288−294.
[3]	ZHOU F B, ZHAO M M, SU G W, et al. Binding of aroma compounds with myofibrillar proteins modified by a hydroxyl-radical-induced oxidative system[J]. J Agric Food Chem,2014,62(39):9544−9552. doi: 10.1021/jf502540p
[4]	WANG H T, ZHU J M, ZHANG H W, et al. Understanding interactions among aldehyde compounds and porcine myofibrillar proteins by spectroscopy and molecular dynamics simulations[J]. Journal of Molecular Liquids,2022,349:118190. doi: 10.1016/j.molliq.2021.118190
[5]	SHEN H, ZHAO M M, SUN W Z. Effect of pH on the interaction of porcine myofibrillar proteins with pyrazine compounds[J]. Food Chemistry,2019,287:93−99. doi: 10.1016/j.foodchem.2019.02.060
[6]	GU S Q, DAI W L, CHONG Y Q, et al. The binding of key fishy off-flavor compounds to silver carp proteins: A thermodynamic analysis[J]. RSC Advances,2020,10(19):11292−11299. doi: 10.1039/D0RA01365J
[7]	ZHANG J, KANG D C, ZHANG W G, et al. Recent advantage of interactions of protein-flavor in foods: Perspective of theoretical models, protein properties and extrinsic factors[J]. Trends in Food Science & Technology,2021,111:405−425.
[8]	GAN X, LI H J, WANG Z M, et al. Does protein oxidation affect proteolysis in low sodium Chinese traditional bacon processing[J]. Meat science,2019,150:14−22. doi: 10.1016/j.meatsci.2018.10.007
[9]	WANG L, ZHANG M, FANG Z X, et al. Gelation properties of myofibrillar protein under malondialdehyde-induced oxidative stress[J]. Journal of the Science of Food and Agriculture,2017,97(1):50−57. doi: 10.1002/jsfa.7680
[10]	WANG Z, HE Z F, EMARA A M, et al. Effects of malondialdehyde as a byproduct of lipid oxidation on protein oxidation in rabbit meat[J]. Food Chemistry,2019,288:405−412. doi: 10.1016/j.foodchem.2019.02.126
[11]	WANG Z M, HE Z F, GAN X, et al. Interrelationship among ferrous myoglobin, lipid and protein oxidations in rabbit meat during refrigerated and superchilled storage[J]. Meat Science,2018,146:131−139. doi: 10.1016/j.meatsci.2018.08.006
[12]	JIANG W X, HE Y F, XIONG S B, et al. Effect of mild ozone oxidation on structural changes of silver carp (Hypophthalmichthys molitrix) myosin[J]. Food and Bioprocess Technology,2017,10(2):370−378. doi: 10.1007/s11947-016-1828-5
[13]	CHELH I, GATELLIER P, SANTE-LHOUTELLIER V. A simplified procedure for myofibril hydrophobicity determination[J]. Meat Science,2006,74(4):681−683. doi: 10.1016/j.meatsci.2006.05.019
[14]	曹云刚, 马文慧, 艾娜丝, 等. 氧化强度对肌原纤维蛋白结构及凝胶性能的影响[J]. 食品科学,2019,40(20):21−27. [CAO Y G, MA W H, AI N S, et al. Effect of oxidation strength on structure and gel properties of myofibrillar protein[J]. Food Science,2019,40(20):21−27.
[15]	PEREZJUAN M, FLORES M, TOLDRA F. Model studies on the efficacy of protein homogenates from raw pork muscle and dry-cured ham in binding selected flavor compounds[J]. Journal of Agricultural and Food Chemistry,2006,54(13):4802−4808. doi: 10.1021/jf060374x
[16]	SUN W, ZHAO Q, ZHAO H, et al. Volatile compounds of Cantonese sausage released at different stages of processing and storage[J]. Food Chemistry,2010,121(2):319−325. doi: 10.1016/j.foodchem.2009.12.031
[17]	ESTEVEZ M, MORCUENDE D, VENTANAS S, et al. Analysis of volatiles in meat from Iberian pigs and lean pigs after refrigeration and cooking by using SPME-GC-MS[J]. Journal of Agricultural and Food Chemistry,2003,51(11):3429−3435. doi: 10.1021/jf026218h
[18]	BAO Z J, WU J P, CHENG Y J, et al. Effects of lipid peroxide on the structure and gel properties of ovalbumin[J]. Process Biochemistry,2017,57:124−130. doi: 10.1016/j.procbio.2017.03.009
[19]	ZHOU L, ZHANG Y, ZHAO C, et al. Structural and functional properties of rice bran protein oxidized by peroxyl radicals[J]. International Journal of Food Properties,2017,20(sup2):1456−1467.
[20]	DOMIINGUEZ R, PATEIRO M, MUNEKATA P E S, et al. Protein oxidation in muscle foods: A comprehensive review[J]. Antioxidants,2021,11(1):60. doi: 10.3390/antiox11010060
[21]	周非白. 氧化修饰对猪肉肌原纤维蛋白结构与功能特性的调控研究[D]. 广州: 华南理工大学, 2016 ZHOU F B. Effects of oxidative modification on structural and functional properties of pork myofibrin[D]. Guangzhou: South China University of Technology, 2016.
[22]	WEN R X, HU Y Y, ZHANG L, et al. Effect of NaCl substitutes on lipid and protein oxidation and flavor development of Harbin dry sausage[J]. Meat Science,2019,156:33−43. doi: 10.1016/j.meatsci.2019.05.011
[23]	马国源. 低剂量亚硝酸钠抑制牦牛肉肌红蛋白氧化的作用机制[D]. 兰州: 甘肃农业大学, 2021 MA G Y. Mechanism of low dose sodium nitrite inhibiting myoglobin oxidation in yak meat[D]. Lanzhou: Gansu Agricultural University, 2021.
[24]	BAO Y, ERTBJERG P. Effects of protein oxidation on the texture and water-holding of meat: A review[J]. Critical Reviews in Food Science and Nutrition,2019,59(22):3564−3578. doi: 10.1080/10408398.2018.1498444
[25]	DAVIES M J. Protein oxidation and peroxidation[J]. Biochemical Journal,2016,473(Pt7):805−825.
[26]	ZHANG W, XIAO S, AHN D U. Protein oxidation: Basic principles and implications for meat quality[J]. Critical Reviews in Food Science and Nutrition,2013,53(11):1191−1201. doi: 10.1080/10408398.2011.577540
[27]	ZHANG Z Y, YANG Y L, ZHOU P, et al. Effects of high pressure modification on conformation and gelation properties of myofibrillar protein[J]. Food Chemistry,2017,217:678−686. doi: 10.1016/j.foodchem.2016.09.040
[28]	WANG Z M, HE Z F, ZHANG D, et al. Effect of multiple freeze-thaw cycles on protein and lipid oxidation in rabbit meat[J]. International Journal of Food Science & Technology,2021,56(6):3004−3015.
[29]	HASSOUN A, SAHAR A, LAKHAL L, et al. Fluorescence spectroscopy as a rapid and non-destructive method for monitoring quality and authenticity of fish and meat products: Impact of different preservation conditions[J]. LWT,2019,103:279−292. doi: 10.1016/j.lwt.2019.01.021
[30]	FUENTES-LEMUS E, DORTA E, ESCOBAR E, et al. Oxidation of free, peptide and protein tryptophan residues mediated by AAPH-derived free radicals: Role of alkoxyl and peroxyl radicals[J]. RSC Adv,2016,6(63):57948−57955. doi: 10.1039/C6RA12859A
[31]	DIAO X Q, GUAN H N, ZHAO X X, et al. Physicochemical and structural properties of composite gels prepared with myofibrillar protein and lard diacylglycerols[J]. Meat Science,2016,121:333−341. doi: 10.1016/j.meatsci.2016.07.002
[32]	JIA N, WANG L T, SHAO J H, et al. Changes in the structural and gel properties of pork myofibrillar protein induced by catechin modification[J]. Meat Science,2017,127:45−50. doi: 10.1016/j.meatsci.2017.01.004
[33]	LEINISCH F, MARIOTTI M, RYKAER M, et al. Peroxyl radical-and photo-oxidation of glucose 6-phosphate dehydrogenase generates cross-links and functional changes via oxidation of tyrosine and tryptophan residues[J]. Free Radical Biology and Medicine 2017, 112: 240-252.
[34]	MARIA P J, MONICA F, FIDEL T. Effect of ionic strength of different salts on the binding of volatile compounds to porcine soluble protein extracts in model systems[J]. Food Research International,2007,40(6):687−693. doi: 10.1016/j.foodres.2006.11.013