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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