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The influence of particle size and ionic strength on the freeze-thaw (FT) stability of emulsions stabilized by whey protein isolate (WPI) was investigated in this study. The destabilization of emulsions during the FT process could be suppressed in a way by decreasing the particle size of the initial emulsions, which was the result of retarding the coalescence between oil droplets. To further improve the FT stability of emulsions, different amounts of NaCl were added before emulsification. The emulsions with the ionic strength at 30–50 mmol/L exhibited good FT stability. Notably, the ionic strength in this range would not lower the freezing point of emulsions below the freezing temperature used in this study. Salt addition could improve the structural properties of proteins, which was available to strengthen the rigidity and thickness of interfacial layers, sequentially building up the resistance that the destruction of ice crystals to emulsions. Moreover, stronger flocculation between emulsion droplets could promote the formation of a gel-like network structure dominated by elasticity in the emulsion system, which might effectively inhibit the movement of droplets, and improve the FT stability of emulsions eventually. The result was of great significance for the preparation of emulsion-based foods with improved FT stability.


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Influence of particle size and ionic strength on the freeze-thaw stability of emulsions stabilized by whey protein isolate

Show Author's information Hao Laia,bFuchao Zhana,bYujie Weia,bAbel W.S. Zongoa,bSha Jianga,bHaomin Suia,bBin Lia,bJing Lia,b( )
College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China
Key Laboratory of Environment Correlative Dietology (Huazhong Agricultural University), Ministry of Education, Wuhan 430070, China

Abstract

The influence of particle size and ionic strength on the freeze-thaw (FT) stability of emulsions stabilized by whey protein isolate (WPI) was investigated in this study. The destabilization of emulsions during the FT process could be suppressed in a way by decreasing the particle size of the initial emulsions, which was the result of retarding the coalescence between oil droplets. To further improve the FT stability of emulsions, different amounts of NaCl were added before emulsification. The emulsions with the ionic strength at 30–50 mmol/L exhibited good FT stability. Notably, the ionic strength in this range would not lower the freezing point of emulsions below the freezing temperature used in this study. Salt addition could improve the structural properties of proteins, which was available to strengthen the rigidity and thickness of interfacial layers, sequentially building up the resistance that the destruction of ice crystals to emulsions. Moreover, stronger flocculation between emulsion droplets could promote the formation of a gel-like network structure dominated by elasticity in the emulsion system, which might effectively inhibit the movement of droplets, and improve the FT stability of emulsions eventually. The result was of great significance for the preparation of emulsion-based foods with improved FT stability.

Keywords: Particle size, Ionic strength, Emulsion, Freeze-thaw stability, Whey protein isolate

References(40)

[1]

J.N. Coupland, Crystallization in emulsions, Curr. Opin. Colloid Interface Sci. 7(5-6) (2002) 445-450. https://doi.org/10.1016/S1359-0294(02)00080-8.

[2]

G.L. Cramp, A.M. Docking, S. Ghosh, et al., On the stability of oil-in-water emulsions to freezing, Food Hydrocoll. 18(6) (2004) 899-905. https://doi.org/10.1016/j.foodhyd.2003.10.007.

[3]

B.M. Degner, C. Chung, V. Schlegel, et al., Factors influencing the freeze-thaw stability of emulsion-based foods, Compr. Rev. Food Sci. Food Saf. 13(2) (2014) 98-113. https://doi.org/10.1111/1541-4337.12050.

[4]

B. Degner, K. Olson, D. Rose, et al., Influence of freezing rate variation on the microstructure and physicochemical properties of food emulsions, J. Food Eng. 119(2) (2013) 244-253. https://doi.org/10.1016/j.jfoodeng.2013.05.034.

[5]

E. Dickinson, Milk protein interfacial layers and the relationship to emulsion stability and rheology, Colloids Surf. B. 20(3) (2001) 197-210. https://doi.org/10.1016/S0167-2991(01)82248-5.

[6]

S. Ghosh, J.N. Coupland, Factors affecting the freeze-thaw stability of emulsions, Food Hydrocoll. 22(1) (2008) 105-111. https://doi.org/10.1016/j.foodhyd.2007.04.013.

[7]
N. Zaritzky, Physical-chemical principles in freezing. In: Handbook of frozen food processing and packaging. 2nd ed, CRC Press, Boca Raton: (2011).
DOI
[8]

M. Hernández-Carrión, L. Guardeño, J. Carot, et al., Structural stability of white sauces prepared with different types of fats and thawed in a microwave oven, J. Food Eng. 104(4) (2011) 557-564. https://doi.org/10.1016/j.jfoodeng.2011.01.017.

[9]

P. Thanasukarn, R. Pongsawatmanit, D. McClements, Impact of fat and water crystallization on the stability of hydrogenated palm oil-in-water emulsions stabilized by whey protein isolate, Colloids Surf. A Physicochem. Eng. Asp. 246(1-3) (2004) 49-59. https://doi.org/10.1016/j.colsurfa.2004.07.018.

[10]
W. Norde, Colloids and interfaces in life sciences, CRC Press, Boca Raton: (2003) p. 47.
DOI
[11]
P. Walstra, Physical chemistry of foods, CRC Press, Boca Raton: (2002).
DOI
[12]

G.G. Palazolo, P.A. Sobral, J.R. Wagner, Freeze-thaw stability of oil-in-water emulsions prepared with native and thermally-denatured soybean isolates, Food Hydrocoll. 25(3) (2011) 398-409. https://doi.org/10.1016/j.foodhyd.2010.07.008.

[13]

X.F. Zhu, N. Zhang, W.F. Lin, et al., Freeze-thaw stability of pickering emulsions stabilized by soy and whey protein particles, Food Hydrocoll. 69 (2017) 173-184. https://doi.org/10.1016/j.foodhyd.2017.02.001.

[14]

D. Xu, F. Yuan, X. Wang, et al., The effect of whey protein isolate-dextran conjugates on the freeze-thaw stability of oil-in-water emulsions, J. Dispers. Sci. Technol. 32(1) (2010) 77-83. https://doi.org/10.1080/01932690903546785.

[15]

X. Zang, P. Liu, Y. Chen, et al., Improved freeze-thaw stability of O/W emulsions prepared with soybean protein isolate modified by papain and transglutaminase, LWT-Food Sci. Technol. 104 (2019) 195-201. https://doi.org/10.1016/j.lwt.2019.01.013.

[16]

X. Zang, C. Yue, M. Liu, et al., Improvement of freeze-thaw stability of oil-in-water emulsions prepared with modified soy protein isolates, LWT-Food Sci. Technol. 102 (2019) 122-130. https://doi.org/10.1016/j.lwt.2018.09.004.

[17]

X.F. Zhu, J. Zheng, F. Liu, et al., Freeze-thaw stability of Pickering emulsions stabilized by soy protein nanoparticles. Influence of ionic strength before or after emulsification, Food Hydrocoll. 74 (2018) 37-45. https://doi.org/10.1016/j.foodhyd.2017.07.017.

[18]

Y. Zhu, D.J. McClements, W. Zhou, et al., Influence of ionic strength and thermal pretreatment on the freeze-thaw stability of Pickering emulsion gels, Food Chem. 303 (2020) 125401. https://doi.org/10.1016/j.foodchem.2019.125401.

[19]

M. Destribats, M. Rouvet, C. Gehin-Delval, et al., Emulsions stabilised by whey protein microgel particles: towards food-grade Pickering emulsions, Soft Matter. 10(36) (2014) 6941-6954. https://doi.org/10.1039/c4sm00179f.

[20]

W. Xiong, C. Ren, J. Li, et al., Characterization and interfacial rheological properties of nanoparticles prepared by heat treatment of ovalbumin-carboxymethylcellulose complexes, Food Hydrocoll. 82 (2018) 355-362. https://doi.org/10.1016/j.foodhyd.2018.03.048.

[21]

W. Xiong, C. Ren, M. Tian, et al., Emulsion stability and dilatational viscoelasticity of ovalbumin/chitosan complexes at the oil-in-water interface, Food Chem. 252 (2018) 181-188. https://doi.org/10.1016/j.foodchem.2018.01.067.

[22]

A. Djoullah, Y. Djemaoune, F. Husson, et al., Native-state pea albumin and globulin behavior upon transglutaminase treatment, Process Biochem. 50(8) (2015) 1284-1292. https://doi.org/10.1016/j.procbio.2015.04.021.

[23]

W. Wang, Q. Zhong, Z. Hu, Nanoscale understanding of thermal aggregation of whey protein pretreated by transglutaminase, J. Agric. Food Chem. 61(2) (2013) 435-446. https://doi.org/10.1021/jf304506n.

[24]

K. Boode, C. Bisperink, P. Walstra, Destabilization of O/W emulsions containing fat crystals by temperature cycling, Colloids and Surf. 61 (1991) 55-74. https://doi.org/10.1016/0166-6622(91)80299-4.

[25]

O.S. Lawal, Specific ions effect on emulsions, foams, and gels of a seed protein, Food Biophys. 4(4) (2009) 347-352. https://doi.org/10.1007/s11483-009-9133-8.

[26]

M.A. Bos, T.V. Vliet, Interfacial rheological properties of adsorbed protein layers and surfactants: a review, Adv. Colloid Interface Sci. 91(3) (2001) 437-471. https://doi.org/10.1016/S0001-8686(00)00077-4.

[27]

D.J. McClements, Protein-stabilized emulsions, Curr. Opin. Colloid Interface Sci. 9(5) (2004) 305-313. https://doi.org/10.1016/j.cocis.2004.09.003.

[28]

M.A. de la Fuente, Changes in the mineral balance of milk submitted to technological treatments, Trends Food Sci Technol. 9(7) (1998) 281-288. https://doi.org/10.1016/s0924-2244(98)00052-1.

[29]

S. Ghosh, G.L. Cramp, J.N. Coupland, Effect of aqueous composition on the freeze-thaw stability of emulsions, Colloids Surf. A Physicochem. Eng. Asp. 272(1/2) (2006) 82-88. https://doi.org/10.1016/j.colsurfa.2005.07.013.

[30]

M.W. Jeong, S.G. Oh, Y.C. Kim, Effects of amine and amine oxide compounds on the zeta-potential of emulsion droplets stabilized by phosphatidylcholine, Colloids Surf. A Physicochem. Eng. Asp. 181(1) (2001) 247-253. https://doi.org/10.1016/S0927-7757(00)00796-2.

[31]

E. Fredrick, P. Walstra, K. Dewettinck, Factors governing partial coalescence in oil-in-water emulsions, Adv. Colloid Interface Sci. 153(1-2) (2010) 30-42. https://doi.org/10.1016/j.cis.2009.10.003.

[32]

O.S. Lawal, Kosmotropes and chaotropes as they affect functionality of a protein isolate, Food Chem. 95(1) (2006) 101-107. https://doi.org/10.1016/j.foodchem.2004.12.041.

[33]

Y. Zhu, X. Chen, D.J. Mcclements, et al., pH-, ion- and temperature-dependent emulsion gels: fabricated by addition of whey protein to gliadin-nanoparticle coated lipid droplets, Food Hydrocoll. 77 (2017) 870-878. https://doi.org/10.1016/j.foodhyd.2017.11.032.

[34]

E. Dickinson, Interfacial structure and stability of food emulsions as affected by protein-polysaccharide interactions, Soft Matter. 4(5) (2008) 932-942. https://doi.org/10.1039/b718319d.

[35]

A. Schroder, C. Berton-Carabin, P. Venema, et al., Interfacial properties of whey protein and whey protein hydrolysates and their influence on O/W emulsion stability, Food Hydrocoll. 73 (2017) 129-140. https://doi.org/10.1016/j.foodhyd.2017.06.001.

[36]

F. Liu, C.H. Tang, Soy glycinin as food-grade Pickering stabilizers: Part. Ⅱ. Improvement of emulsification and interfacial adsorption by electrostatic screening, Food Hydrocoll. 60 (2016) 620-630. https://doi.org/10.1016/j.foodhyd.2015.10.024.

[37]

D.R. Robinson, W.P. Jencks, The effect of compounds of the urea-guanidinium class on the activity coefficient of acetyltetraglycine ethyl ester and related compounds, J. Am. Chem. Soc. 87(11) (1965) 2462-2470.

[38]

F. Liu, D. Wang, C. Sun, et al., Utilization of interfacial engineering to improve physicochemical stability of β-carotene emulsions: Multilayer coatings formed using protein and protein-polyphenol conjugates, Food Chem. 205 (2016) 129-139. https://doi.org/10.1016/j.foodchem.2016.02.155.

[39]

Y.A. Adebowale, K.O. Adebowale, The influence of kosmotropic and chaotropic salts on the functional properties of Mucuna pruriens protein isolate, Int. J. Biol. Macromol. 40(2) (2007) 119-125. https://doi.org/10.1016/j.ijbiomac.2006.06.016.

[40]

S. Damodaran, J.E. Kinsella, Effects of ions on protein conformation and functionality, ACS Symp. Ser. 206 (1982) 327-357. https://doi.org/10.1021/bk-1982-0206.ch013.

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Publication history

Received: 18 September 2020
Revised: 10 October 2020
Accepted: 01 December 2020
Published: 28 April 2022
Issue date: July 2022

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© 2022 Beijing Academy of Food Sciences. Publishing services by Elsevier B.V. on behalf of KeAi Communications Co., Ltd.

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Acknowledgements

This work was financially supported by National Natural Science Foundation of China (31871844 & 31501530).

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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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