Viscoelastic and flow behaviour of β-lactoglobulin/lactoferrin coacervates: Influence of temperature and ionic strength

被引：0
作者：
Soussi, Rima Hachfi [1 ]
Ben Messaoud, Ghazi [1 ]
Rousseau, Florence [1 ]
Hamon, Pascaline [1 ]
Famelart, Marie-Helene [1 ]
Bouhallab, Said [1 ]
机构：
[1] INRAE, Inst Agro, STLO, 65 Rue St Brieuc, F-35042 Rennes, France
来源：
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2025年 / 292卷
关键词：
Heteroprotein complex coacervation; beta-Lactoglobulin; Lactoferrin; Rheology; Time temperature superposition; HETEROPROTEIN COMPLEX COACERVATION; LINEAR VISCOELASTICITY; RHEOLOGICAL PROPERTIES; PHASE-SEPARATION; CHARGE-DENSITY; LACTOFERRIN; LACTOTRANSFERRIN; THERMODYNAMICS; CHLORIDE); FIRMNESS;
D O I：
10.1016/j.ijbiomac.2024.139121
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Heteroprotein complex coacervation has potential for a wide range of applications. However, the sensitivity of coacervates to slight changes in physico-chemical conditions may constitute a technological barrier for their development and deserves to be better understood. In this study, the rheological properties of beta-lactoglobulin/ lactoferrin (beta LG/LF) heteroprotein complex coacervates were investigated with respect to narrow changes of temperature (5-40 degrees C) and ionic strength (0 to 10 mM added NaCl). The apparent viscosity of beta LG/LF coacervates prepared at 20 degrees C showed a high sensitivity to temperature, decreasing progressively at elevated temperatures. Frequency sweep experiments demonstrated that coacervates behave as a viscoelastic liquid throughout the investigated frequency range at T > 10 degrees C. Time-temperature superposition principle revealed that the interaction involved in the coacervation process were temperature-independent. The calculated activation energy was approximately 85 kJ/mol. The addition of NaCl (up to 10mM) prior to coacervation, resulted in an increase of the viscosity but did not show a clear trend in the evolution of viscoelastic moduli. These new insights allow a better understanding of the interactions involved in concentrated protein coacervates enabling better control over their potential uses.
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页数：13
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共 76 条
  • [31] Soussi Hachfi R., Hamon P., Rousseau F., Famelart M.-H., Bouhallab S., Ionic strength dependence of the complex coacervation between lactoferrin and β-lactoglobulin, Foods, 12, (2023)
  • [32] Tavares G.M., Croguennec T., Hamon P., Carvalho A.F., Bouhallab S., Selective coacervation between lactoferrin and the two isoforms of β-lactoglobulin, Food Hydrocoll., 48, pp. 238-247, (2015)
  • [33] Tavares G.M., Croguennec T., Hamon P., Carvalho A.F., Bouhallab S., How the presence of a small molecule affects the complex coacervation between lactoferrin and β-lactoglobulin, Int. J. Biol. Macromol., 102, pp. 192-199, (2017)
  • [34] Anema S.G., de Kruif C.G.K., Complex coacervates of lactotransferrin and β-lactoglobulin, J. Colloid Interface Sci., 430, pp. 214-220, (2014)
  • [35] Chapeau A.-L., Hamon P., Rousseau F., Croguennec T., Poncelet D., Bouhallab S., Scale-up production of vitamin loaded heteroprotein coacervates and their protective property, J. Food Eng., 206, pp. 67-76, (2017)
  • [36] Liu Y., Winter H.H., Perry S.L., Linear viscoelasticity of complex coacervates, Adv. Colloid Interf. Sci., 239, pp. 46-60, (2017)
  • [37] Goulding D.A., Bovetto L., O'Regan J., O'Brien N.M., O'Mahony J.A., Rheological and microstructural properties of heteroprotein complex coacervates formed by lactoferrin and osteopontin, Food Hydrocoll., 147, (2024)
  • [38] Zhang X., Zhang Z., Zhang T., Zhang Y., Jiang L., Sui X., Heteroprotein complex coacervates of soy protein isolate and type-A gelatin: formation mechanism, structure and rheological properties, Food Hydrocoll., 158, (2025)
  • [39] Schindelin J., Arganda-Carreras I., Frise E., Kaynig V., Longair M., Pietzsch T., Preibisch S., Rueden C., Saalfeld S., Schmid B., Tinevez J.-Y., White D.J., Hartenstein V., Eliceiri K., Tomancak P., Cardona A., Fiji: an open-source platform for biological-image analysis, Nat. Methods, 9, pp. 676-682, (2012)
  • [40] Gebhardt R., Toro-Sierra J., Kulozik U., Pressure dissociation of β-lactoglobulin oligomers near their isoelectric point, Soft Matter, 8, pp. 11654-11660, (2012)
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