Food and Fermentation Industries >

2023 , Vol. 49 >Issue 24: 206 - 212

DOI: https://doi.org/10.13995/j.cnki.11-1802/ts.033431

Effect of addition of non-meat proteins on properties and emulsification of myofibrillar proteins

  • HUANG Chunyang ,
  • MA Jingjing ,
  • YANG Jing ,
  • LI Chao ,
  • XU Weimin ,
  • WANG Daoying ,
  • ZOU Ye ,
  • LUO Zhang
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  • 1(College of Food Science, Tibet Academy of Agriculture and Animal Husbandry, Nyingchi 860000, China)
    2(Agricultural Products Processing Institute of Jiangsu Academy of Agricultural Sciences, Nanjing 210014, China)
    3(Nanjing Yurun Food Co.Ltd., Nanjing 210000, China)

Received date: 2022-08-25

  Revised date: 2022-10-09

  Online published: 2024-01-17

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Abstract

Spray-dried blood cells, soybean protein isolate, egg white protein, and porcine plasma protein were added to the myofibrillar protein (MP) solution, and the MP solution without non-meat protein added was used as a blank control to explore the different non-meat protein and MP action mechanism. Compared with the control group, all complexes of non-meat proteins contributed to the apparent viscosity of MP, in which the area of the thixotropic ring increased for egg white proteins and porcine plasma proteins. The results of fluorescence spectroscopy showed that the fluorescence intensity could be increased by egg white protein and porcine plasma protein, and the unfolding of MP structure was promoted by the group of hemoglobin to decrease the fluorescence intensity. Analysis of the spray-dried blood cells and porcine plasma protein samples in terms of the complex protein fraction showed a clear enhancement of the band intensity of the myosin heavy chain. Myosin heavy chain content did not change significantly in the soybean protein isolate, and egg white protein addition groups. The combined emulsification and hydrophobicity results showed that the two indexes were significantly correlated, and the total sulfhydryl group content increased by 5.17% after the addition of porcine plasma protein in addition. The particle sizes of the non-meat protein treated groups were all significantly larger than those of the control group, prompting the proteins to cross-link and aggregate, resulting in an increase in the size of their molecules. Thermal stability analysis of the complex proteins, it is known that the soybean protein isolate molecules are more sensitive to temperature. Porcine plasma protein had the most obvious effect on improving the thermal stability of MP, and comprehensive analysis of other indicators in this paper concluded that porcine plasma proteins were the best to cross-link with MP, thereby alleviating the high-temperature damage to the protein structure to some extent.

Key words： non-meat proteins; myofibrillar proteins; physicochemical indexes; interactions; emulsifying characteristics

Cite this article

HUANG Chunyang , MA Jingjing , YANG Jing , LI Chao , XU Weimin , WANG Daoying , ZOU Ye , LUO Zhang . Effect of addition of non-meat proteins on properties and emulsification of myofibrillar proteins[J]. Food and Fermentation Industries, 2023 , 49(24) : 206 -212 . DOI: 10.13995/j.cnki.11-1802/ts.033431

References

[1] ALI S, ZHANG W G, RAJPUT N, et al.Effect of multiple freeze-thaw cycles on the quality of chicken breast meat[J].Food Chemistry, 2015, 173:808-814.
[2] LAWRIE R A. Meat Science[M]. Preface to the fourth edition. Amsterdam: Elsevier, 1985: vii.
[3] UTRERA M, PARRA V, ESTÈVEZ M.Protein oxidation during frozen storage and subsequent processing of different beef muscles[J].Meat Science, 2014, 96(2):812-820.
[4] ZHOU F B, ZHAO M M, SU G W, et al.Gelation of salted myofibrillar protein under malondialdehyde-induced oxidative stress[J].Food Hydrocolloids, 2014, 40:153-162.
[5] GORNALL A G, BARDAWILL C J, DAVID M M. Determination of serum proteins by means of the biuret reaction[J]. The Journal of Biological Chemistry, 1949, 177(2):751-766.
[6] YOUSSEF M K, BARBUT S.Fat reduction in comminuted meat products-effects of beef fat, regular and pre-emulsified canola oil[J].Meat Science, 2011, 87(4):356-360.
[7] HU H, CHEUNG I W Y, PAN S Y, et al.Effect of high intensity ultrasound on physicochemical and functional properties of aggregated soybean β-conglycinin and glycinin[J].Food Hydrocolloids, 2015, 45:102-110.
[8] GUO J J, ZHOU Y H, YANG K, et al.Effect of low-frequency magnetic field on the gel properties of pork myofibrillar proteins[J].Food Chemistry, 2019, 274:775-781.
[9] 楼宵玮, 蒋娅婷, 潘道东, 等.氯化钠对肌原纤维蛋白与风味物质相互作用的影响[J].食品科学, 2017, 38(5):74-79.
LOU X W, JIANG Y T, PAN D D, et al.Effect of NaCl on the interaction of flavor compounds with myofibrillar proteins[J].Food Science, 2017, 38(5):74-79.
[10] GAO X, XIE Y R, YIN T, et al.Effect of high intensity ultrasound on gelation properties of silver carp surimi with different salt contents[J].Ultrasonics Sonochemistry, 2021, 70:105326.
[11] SHEN X, FANG T Q, GAO F, et al.Effects of ultrasound treatment on physicochemical and emulsifying properties of whey proteins pre- and post-thermal aggregation[J].Food Hydrocolloids, 2017, 63:668-676.
[12] 刘光明, 余惠琳, 黄秀秀, 等.加工处理方式对蟹类原肌球蛋白的消化稳定性和过敏原性的影响[J].中国食品学报, 2011, 11(4):14-22.
LIU G M, YU H L, HUANG X X, et al.Effects of processing methods on digestibility and allergenicity of crab tropomyosin[J].Journal of Chinese Institute of Food Science and Technology, 2011, 11(4):14-22.
[13] COFRADES S, CARECHE M, CARBALLO J, et al.Thermal gelation of chicken, pork and Hake (Merluccius merluccius, L) actomyosin[J].Meat Science, 1997, 47(1-2):157-166.
[14] ZHANG D J, YANG X, WANG Y C, et al.Proanthocyanidin B2 and transglutaminase synergistically improves gel properties of oxidized myofibrillar proteins[J].Food Chemistry, 2022, 391:133262.
[15] SHEN Q W, SWARTZ D R.Influence of salt and pyrophosphate on bovine fast and slow myosin S1 dissociation from actin[J].Meat Science, 2010, 84(3):364-370.
[16] 韩馨蕊, 李颖, 刘苗苗, 等.安石榴苷与焦磷酸钠对肌原纤维蛋白氧化稳定性及凝胶性能的影响[J].食品科学, 2022, 43(8):15-21.
HAN X R, LI Y, LIU M M, et al.Effect of punicalagin combined with sodium pyrophosphate on the oxidative stability and gel properties of myofibrilar protein[J].Food Science, 2022, 43(8):15-21.
[17] 王晓霞, 李松波, 马力通, 等.三维荧光光谱法和圆二色谱法研究氨基比林与牛血清白蛋白分子的相互作用[J].中国测试, 2017, 43(9):74-80.
WANG X X, LI S B, MA L T, et al.Study on the interaction between aminopyrine and bovine serum albumin by three-dimensional fluorescence spectrometry and circular dichroism spectrum[J].China Measurement & Test, 2017, 43(9):74-80.
[18] CAO Y G, XIONG Y L.Chlorogenic acid-mediated gel formation of oxidatively stressed myofibrillar protein[J].Food Chemistry, 2015, 180:235-243.
[19] ZOU Y, YANG H, ZHANG M H, et al.The influence of ultrasound and adenosine 5′-monophate marination on tenderness and structure of myofibrillar proteins of beef[J].Asian-Australasian Journal of Animal Sciences, 2019, 32(10):1611-1620.
[20] ZHOU C S, MA H L, YU X J, et al.Pretreatment of defatted wheat germ proteins (by-products of flour mill industry) using ultrasonic horn and bath reactors:Effect on structure and preparation of ACE-inhibitory peptides[J].Ultrasonics Sonochemistry, 2013, 20(6):1390-1400.
[21] 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.
[22] LONG Z, ZHAO M M, ZHAO Q Z, et al.Effect of homogenisation and storage time on surface and rheology properties of whipping cream[J].Food Chemistry, 2012, 131(3):748-753.
[23] LIANG Q, ZHANG J S, XU C J, et al.Influence of temperature, pH, and ionic strength on the rheological properties of oviductus ranae hydrogels[J].African Journal of Biotechnology, 2014, 13(24):2435-2444.
[24] SIKORA M, ADAMCZYK G, KRYSTYJAN M, et al.Thixotropic properties of normal potato starch depending on the degree of the granules pasting[J].Carbohydrate Polymers, 2015, 121:254-264.
[25] RAIKOS V.Effect of heat treatment on milk protein functionality at emulsion interfaces.A review[J].Food Hydrocolloids, 2010, 24(4):259-265.
[26] KATO A, NAKAI S.Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins[J].Biochimica et Biophysica Acta (BBA-Protein Structure), 1980, 624(1):13-20.
[27] XIA X F, KONG B H, XIONG Y L, et al.Decreased gelling and emulsifying properties of myofibrillar protein from repeatedly frozen-thawed porcine longissimus muscle are due to protein denaturation and susceptibility to aggregation[J].Meat Science, 2010, 85(3):481-486.
[28] LAMSAL B P, KOEGEL R G, GUNASEKARAN S.Some physicochemical and functional properties of alfalfa soluble leaf proteins[J].LWT-Food Science & Technology, 2007, 40(9):1520-1526.
[29] GALLUZZO S J, REGENSTEIN J M.Role of chicken breast muscle proteins in meat emulsion formation:Myosin, actin and synthetic actomyosin[J].Journal of Food Science, 1978, 43(6):1761-1765.
[30] NEELAKANTAN S, FRONING G W.Studies on the emulsifying characteristics of some intracellular turkey muscle proteins[J].Journal of Food Science, 1971, 36(4):613-615.
[31] SUN Y J, CHEN J H, ZHANG S W, et al.Effect of power ultrasound pre-treatment on the physical and functional properties of reconstituted milk protein concentrate[J].Journal of Food Engineering, 2014, 124:11-18.
[32] ZORBA Ö, KURT Ş, GENÇCELEP H.The effects of different levels of skim milk powder and whey powder on apparent yield stress and density of different meat emulsions[J].Food Hydrocolloids, 2005, 19(1):149-155.
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