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Acid-induced gelation of whey protein aggregates: Kinetics, gel structure and rheological properties
Abstract
Acid-induced gelation of fractal aggregates with different sizes formed by preheating whey protein isolate solutions has been investigated in the protein concentration range 10–60 g/L as a function of the net protein charge density (α). Homogeneous gels could be formed in a range of α that depended on the heating time and temperature. Decrease of the negative charge density of the proteins increased the rate of gelation, but lowering α to less negative values than approximately −2.5 by adding HCl increased turbidity of the solutions and led to syneresis. Strong syneresis also occurred at more negative net charge densities (higher pH) if the heat treatment was too severe. The elastic modulus of homogeneous gels increased with increasing protein concentration. The heterogeneity of the gels decreased with increasing protein concentration. The temperature dependence of the gelation rate was characterized by an activation energy of 155 kJ/mol independent of the charge density, protein concentration and aggregate size. Increase of the temperature increased the gelation rate, but did not influence the elastic modulus of the gels. The present findings on acid-induced gelation are compared with gelation of the same WPI aggregates induced by adding CaCl₂ reported elsewhere.
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“Acids or alkalis crosslinking agents can trigger protein gelation via pH‐mediated modulation of protein structure and intermolecular interactions, such as GDL, HCl, and sodium hydroxide (Qin et al. 2023; Kharlamova et al. 2018; Lian et al. 2024).”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as Kharlamova et al. 2018
In the citing paper
“During the gelation process, the addition of acid shifts the protein solution toward the isoelectric point, decreasing net charge density and promoting the aggregation of protein molecules into gel‐like structure (Kharlamova et al. 2018)”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as Kharlamova et al. 2018
Citations
Cites
Bryant, C. M., & McClements, D. J. (1998) · Trends in Food Science & Technology · doi:10.1016/s0924-2244(98)00031-4 · Cited by 643
Tombs, M. P. (1974) · Faraday Discussions of the Chemical Society · doi:10.1039/dc9745700158 · Cited by 216
Research works printed but not linked: 24
- Ako, 2010, Salt-induced gelation of globular protein aggregates: Structure and kinetics, Biomacromolecules, 11, 864, 10.1021/bm9011437 · DOI
- Alting, 2003, Number of thiol groups rather than the size of the aggregates determines the hardness of cold set whey protein gels, Food Hydrocolloids, 17, 469, 10.1016/S0268-005X(03)00023-7 · DOI
- Alting, 2000, Formation of disulfide bonds in acid-induced gels of preheated whey protein isolate, Journal of Agricultural and Food Chemistry, 48, 5001, 10.1021/jf000474h · DOI
- Alting, 2003, Cold-set globular protein gels: Interactions, structure and rheology as a function of protein concentration, Journal of Agricultural and Food Chemistry, 51, 3150, 10.1021/jf0209342 · DOI
- Amin, 2014, Protein aggregation, particle formation, characterization & rheology, Current Opinion in Colloid & Interface Science, 19, 438, 10.1016/j.cocis.2014.10.002 · DOI
- Britten, 2001, Acid-induced gelation of whey protein polymers: Effects of pH and calcium concentration during polymerization, Food Hydrocolloids, 15, 609, 10.1016/S0268-005X(01)00049-2 · DOI
- Cavallieri, 2007, Whey protein interactions in acidic cold-set gels at different pH values, Le Lait, 87, 535, 10.1051/lait:2007032 · DOI
- Cavallieri, 2008, The effects of acidification rate, pH and ageing time on the acidic cold set gelation of whey proteins, Food Hydrocolloids, 22, 439, 10.1016/j.foodhyd.2007.01.001 · DOI
- De Kruif, 1997, Skim milk acidification, Journal of Colloid and Interface Science, 185, 19, 10.1006/jcis.1996.4548 · DOI
- Donato, 2011, Mixtures of whey protein microgels and soluble aggregates as building blocks to control rheology and structure of acid induced cold-set gels, Food Hydrocolloids, 25, 734, 10.1016/j.foodhyd.2010.08.020 · DOI
- Donato, 2009, Mechanism of formation of stable heat-induced β-lactoglobulin microgels, International Dairy Journal, 19, 295, 10.1016/j.idairyj.2008.11.005 · DOI
- Ju, 1998, Effects of preheating on properties of aggregates and of cold-set gels of whey protein isolate, Journal of Agricultural and Food Chemistry, 46, 3604, 10.1021/jf980392h · DOI
- Ju, 1998, Textural properties of cold-set gels induced from heat-denatured whey protein isolates, Journal of Food Science, 63, 288, 10.1111/j.1365-2621.1998.tb15728.x · DOI
- Jung, 2008, Structure of heat-induced β-lactoglobulin aggregates and their complexes with sodium-dodecyl sulfate, Biomacromolecules, 9, 2477, 10.1021/bm800502j · DOI
- Kharlamova, 2016, The effect of aggregation into fractals or microgels on the charge density and the isoionic point of globular proteins, Food Hydrocolloids, 60, 470, 10.1016/j.foodhyd.2016.04.013 · DOI
- Kharlamova, 2018, Calcium-induced gelation of whey protein aggregates: Kinetics, structure and rheological properties, Food Hydrocolloids, 79, 145, 10.1016/j.foodhyd.2017.11.049 · DOI
- Mezzenga, 2013, The self-assembly, aggregation and phase transitions of food protein systems in one, two and three dimensions, Reports on Progress in Physics, 76, 10.1088/0034-4885/76/4/046601 · DOI
- Nicolai, 2011, β-Lactoglobulin and WPI aggregates: Formation, structure and applications, Food Hydrocolloids, 25, 1945, 10.1016/j.foodhyd.2011.02.006 · DOI
- Nicolai, 2013, Controlled food protein aggregation for new functionality, Current Opinion in Colloid & Interface Science, 18, 249, 10.1016/j.cocis.2013.03.001 · DOI
- Phan-Xuan, 2011, On the crucial importance of the pH for the formation and self-stabilization of protein microgels and strands, Langmuir, 27, 15092, 10.1021/la203357p · DOI
- Rabiey, 2009, Effect of protein composition on the rheological properties of acid-induced whey protein gels, Food Hydrocolloids, 23, 973, 10.1016/j.foodhyd.2008.07.009 · DOI
- Salis, 2011, Measurements and theoretical interpretation of points of zero charge/potential of BSA protein, Langmuir, 27, 11597, 10.1021/la2024605 · DOI
- Schmitt, 2009, Multiscale characterization of individualized β-lactoglobulin microgels formed upon heat treatment under narrow pH range conditions, Langmuir, 25, 7899, 10.1021/la900501n · DOI
- van Vliet, 2004, Rheology and structure of milk protein gels, Current Opinion in Colloid & Interface Science, 9, 298, 10.1016/j.cocis.2004.09.002 · DOI
Cited by
Sorted by citations
Gelation of food protein-protein mixtures.
Nicolai, T. (2019) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2019.06.006 · Cited by 263
Self-citationCheese Whey Processing: Integrated Biorefinery Concepts and Emerging Food Applications
Lappa, I., Papadaki, A., Kachrimanidou, V., Terpou, A., Koulougliotis, D., Eriotou, E., & Kopsahelis, N. (2019) · Foods · doi:10.3390/foods8080347 · Cited by 187
“Whey protein gels can be temperature-induced by either cold- or heat-set mechanisms [175,176], acid-induced [177], or even enzyme-induced [143,156].”
BackgroundXia, W., Zhu, L., Delahaije, R., Cheng, Z., Zhou, X.-L., & Sagis, L. (2021) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2021.107376 · Cited by 111
Wu, D., Tu, M., Wang, Z., Wu, C., Yu, C., Battino, M. A., El-Seedi, H. R., & Du, M. (2019) · Biotechnology Advances · doi:10.1016/j.biotechadv.2019.107491 · Cited by 122
Protein-Based Fat Replacers: A Focus on Fabrication Methods and Fat-Mimic Mechanisms
Nourmohammadi, N., Austin, L., & Chen, D. (2023) · Foods · doi:10.3390/foods12050957 · Cited by 61
Metadata
- Authors
- Kharlamova, A., Chassenieux, C., & Nicolai, T.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Venue
- Food Hydrocolloids
- Publisher
- Elsevier BV
- Published
- 2018-08
- Volume
- 81
- Pages
- 263-272
- ISSN
- 0268-005X (ISSN-L)
- OpenAlex
- W2779487865
- Cited by
- 83
- References
- 0
- Citations by year
- 2026: 10 · 2025: 7 · 2024: 6 · 2023: 3 · 2022: 8 · 2021: 8 · 2020: 16 · 2019: 17 · 2018: 8
- FWCI
- 11.51
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Food Hydrocolloids (publishedVersion)
- HAL (submittedVersion)
- HAL Portal Artxiker (Hindustan Aeronautics Limited (India)) (submittedVersion)
- Funders
- Bba association
- Le Mans University
- Regional councils of Brittany
- Pays de la Loire
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Life Sciences › Agricultural and Biological Sciences › Food Science › Polysaccharides Composition and Applications
- Keywords
- whey protein isolate, acid-induced gelation, gelation kinetics, activation energy, syneresis, gel structure, elastic modulus, heat treatment (food and biological processing), calcium-induced gelation
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