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On the structural models of bovine casein micelles—review and possible improvements
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Outgoing claims: the papers this work cites, builds on, or argues with.
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Changes in the kappa-casein and beta-casein concentrations in human milk during lactation.
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The conformation and aggregation of bovine β‐casein A. I. Molecular aspects of thermal aggregation
inferredcites →https://doi.org/10.1007/978-1-4419-8602-3openalex-snapshot
Advanced Dairy Chemistry—1 Proteins
inferredcites →https://doi.org/10.1007/bf00180271openalex-snapshot
Structure of casein micelles studied by small-angle neutron scattering
inferredcites →https://doi.org/10.1007/bf00262002openalex-snapshot
A photon correlation spectroscopy study of size distributions of casein micelle suspensions
inferredcites →https://doi.org/10.1007/bf01469535openalex-snapshot
The effect of environmental conditions on the steric stabilization of casein micelles
inferredcites →https://doi.org/10.1007/s00249-003-0377-9openalex-snapshot
An equilibrium thermodynamic model of the sequestration of calcium phosphate by casein micelles and its application to the calculation of the partition of salts in milk
inferredcites →https://doi.org/10.1007/s00249-006-0058-6openalex-snapshot
Size distribution of pressure-decomposed casein micelles studied by dynamic light scattering and AFM
inferredcites →https://doi.org/10.1007/s00249-008-0266-3openalex-snapshot
Dynamics of well-folded and natively disordered proteins in solution: a time-of-flight neutron scattering study
inferredcites →https://doi.org/10.1016/0005-2795(71)90201-7openalex-snapshot
Use of a papain superpolymer to elucidate the structure of bovine casein micelles
inferredcites →https://doi.org/10.1016/0005-2795(73)90246-8openalex-snapshot
A model for the formation and structure of casein micelles from subunits of variable composition
inferredcites →https://doi.org/10.1016/0005-2795(81)90249-xopenalex-snapshot
Effect of chymosin action on the hydrodynamic diameter of casein micelles
inferredcites →https://doi.org/10.1016/0021-9797(86)90024-xopenalex-snapshot
Steric stabilization and casein micelle stability
inferredcites →https://doi.org/10.1016/0021-9797(88)90223-8openalex-snapshot
A geometrical model to describe the initial aggregation of partly renneted casein micelles
inferredcites →https://doi.org/10.1016/0022-2836(82)90185-1openalex-snapshot
Small-angle neutron scattering study of bovine casein micelles and sub-micelles
inferredcites →https://doi.org/10.1016/0167-4838(84)90197-3openalex-snapshot
A comprehensive study of the relationship between size and protein composition in natural bovine casein micelles
inferredcites →https://doi.org/10.1016/0304-4165(89)90061-5openalex-snapshot
Size-related differences in bovine casein micelles
inferredcites →https://doi.org/10.1016/0927-7757(96)03696-5openalex-snapshot
κ-casein as a polyelectrolyte brush on the surface of casein micelles
inferredcites →https://doi.org/10.1016/j.cocis.2005.11.004openalex-snapshot
Casein micelle structure: Models and muddles
inferredcites →https://doi.org/10.1016/j.cocis.2005.11.005openalex-snapshot
Casein micelle structure: What can be learned from milk synthesis and structural biology?
inferredcites →https://doi.org/10.1016/j.foodchem.2009.06.017openalex-snapshot
High pressure effects on the structure of casein micelles in milk as studied by cryo-transmission electron microscopy
inferredcites →https://doi.org/10.1016/j.foodhyd.2004.04.025openalex-snapshot
Particle size changes and casein solubilisation in high-pressure-treated skim milk
inferredcites →https://doi.org/10.1016/j.foodhyd.2005.08.004openalex-snapshot
Immobilization of casein micelles for probing their structure and interactions with polysaccharides using scanning electron microscopy (SEM)
inferredcites →https://doi.org/10.1016/j.idairyj.2004.04.008openalex-snapshot
A possible structure of the casein micelle based on high-resolution field-emission scanning electron microscopy
inferredcites →https://doi.org/10.1016/j.idairyj.2008.03.002openalex-snapshot
The casein micelle: Historical aspects, current concepts and significance
inferredcites →https://doi.org/10.1016/j.jcis.2007.01.021openalex-snapshot
The rennet coagulation mechanism of skim milk as observed by transmission diffusing wave spectroscopy
inferredcites →https://doi.org/10.1016/j.lwt.2006.05.012openalex-snapshot
Observations of casein micelles in skim milk concentrate by transmission electron microscopy
inferredcites →https://doi.org/10.1016/s0021-9797(02)00066-8openalex-snapshot
Association behavior of β-casein
inferredcites →https://doi.org/10.1016/s0305-0491(99)00110-8openalex-snapshot
Comparative aspects of milk caseins
inferredcites →https://doi.org/10.1016/s0927-7757(02)00518-6openalex-snapshot
Casein micelles as hard spheres: limitations of the model in acidified gel formation
inferredcites →https://doi.org/10.1016/s0927-7757(02)00520-4openalex-snapshot
Substructure of bovine casein micelles by small-angle X-ray and neutron scattering
inferredcites →https://doi.org/10.1016/s0958-6946(98)00040-5openalex-snapshot
Casein Interactions: Casting Light on the Black Boxes, the Structure in Dairy Products
inferredcites →https://doi.org/10.1016/s0958-6946(99)00058-8openalex-snapshot
Casein micelle interactions
inferredcites →https://doi.org/10.1016/s0958-6946(99)00059-xopenalex-snapshot
Casein sub-micelles: do they exist?
inferredcites →https://doi.org/10.1016/s0958-6946(99)00084-9openalex-snapshot
Adsorption behaviour of sodium and calcium caseinates in oil-in-water emulsions
inferredcites →https://doi.org/10.1017/s0022029900013327openalex-snapshot
Structure of the casein micelle. The accessibility of the subunits to various reagents
inferredcites →https://doi.org/10.1017/s0022029900017234openalex-snapshot
The voluminosity of bovine casein micelles and some of its implications
inferredcites →https://doi.org/10.1017/s0022029900017258openalex-snapshot
The determination of the zeta potential of casein micelles
inferredcites →https://doi.org/10.1017/s002202990002094xopenalex-snapshot
Binding of calcium ions to bovine αsl-casein and precipitability of the protein–calcium ion complexes
inferredcites →https://doi.org/10.1017/s0022029900021476openalex-snapshot
Binding of calcium ions to bovine β-casein
inferredcites →https://doi.org/10.1017/s0022029900023724openalex-snapshot
Measurement of electrophoretic mobilities and zeta-potentials of particles from milk using laser Doppler electrophoresis
inferredcites →https://doi.org/10.1017/s0022029900027461openalex-snapshot
Changes in milk on heating: viscosity measurements
inferredcites →https://doi.org/10.1017/s0022029900033306openalex-snapshot
pH-Induced dissociation of bovine casein micelles. I. Analysis of liberated caseins
inferredcites →https://doi.org/10.1017/s0022029903006307openalex-snapshot
The use of sedimentation field flow fractionation and photon correlation spectroscopy in the characterization of casein micelles
inferredcites →https://doi.org/10.1017/s002202999700246xopenalex-snapshot
Relationship between rheological properties and degree of κ-casein proteolysis during renneting of milk
inferredcites →https://doi.org/10.1021/jf0211783openalex-snapshot
Formation of Soluble and Micelle-Bound Protein Aggregates in Heated Milk
inferredcites →https://doi.org/10.1021/jf063242copenalex-snapshot
Acid Gelation in Heated and Unheated Milks: Interactions between Serum Protein Complexes and the Surfaces of Casein Micelles
inferredcites →https://doi.org/10.1021/jf071982vopenalex-snapshot
Impact of Casein Gel Microstructure on Self-Diffusion Coefficient of Molecular Probes Measured by 1H PFG-NMR
inferredcites →https://doi.org/10.1021/jf950832uopenalex-snapshot
Identification of Peptides Released from Casein Micelles by Limited Trypsinolysis
inferredcites →https://doi.org/10.1021/ma051294hopenalex-snapshot
Effect of Casein Concentration in Suspensions and Gels on Poly(ethylene glycol)s NMR Self-Diffusion Measurements
inferredcites →https://doi.org/10.1023/a:1022518613574openalex-snapshot
Environmental Effects on Disulfide Bonding Patterns of Bovine κ-Casein
inferredcites →https://doi.org/10.1039/ft9938902683openalex-snapshot
Caseins as rheomorphic proteins: interpretation of primary and secondary structures of the α S1 -, β- and κ-caseins
inferredcites →https://doi.org/10.1046/j.1432-1327.1998.2520073.xopenalex-snapshot
A core‐shell model of calcium phosphate nanoclusters stabilized by β‐casein phosphopeptides, derived from sedimentation equilibrium and small‐angle X‐ray and neutron‐scattering measurements
inferredcites →https://doi.org/10.1051/lait:199313openalex-snapshot
Polymorphisme de la caséine Κ de trois races bovines françaises et aptitude à la coagulation
inferredcites →https://doi.org/10.1063/1.1484379openalex-snapshot
Stability of casein micelles in milk
inferredcites →https://doi.org/10.1063/1.1800931openalex-snapshot
Structure and rheological behavior of casein micelle suspensions during ultrafiltration process
inferredcites →https://doi.org/10.1063/1.2409933openalex-snapshot
Effects of the environmental factors on the casein micelle structure studied by cryo transmission electron microscopy and small-angle x-ray scattering/ultrasmall-angle x-ray scattering
inferredcites →https://doi.org/10.1111/j.1432-1033.1981.tb05602.xopenalex-snapshot
The Coagulation of Differently Sized Casein Micelles by Rennet
inferredcites →https://doi.org/10.3168/jds.2007-0819openalex-snapshot
Supramolecular Structure of the Casein Micelle
inferredcites →https://doi.org/10.3168/jds.s0022-0302(04)73319-6openalex-snapshot
Nomenclature of the Proteins of Cows’ Milk—Sixth Revision
inferredcites →https://doi.org/10.3168/jds.s0022-0302(70)86141-0openalex-snapshot
Nomenclature of the Proteins of Cow's Milk: Third Revision
inferredcites →https://doi.org/10.3168/jds.s0022-0302(90)78875-3openalex-snapshot
On the Stability of Casein Micelles
inferredcites →https://doi.org/10.3168/jds.s0022-0302(98)75862-xopenalex-snapshot
Rethinking Casein Micelle Structure Using Electron Microscopy
inferredcites →https://doi.org/10.3168/jds.s0022-0302(98)75863-1openalex-snapshot
Casein Micelle Substructure and Calcium Phosphate Interactions Studied by Sephacryl Column Chromatography
inferredcites →https://doi.org/10.3168/jds.s0022-0302(98)75865-5openalex-snapshot
Casein Micelles as Colloids: Surface Structures and Stabilities
inferredcites →https://doi.org/10.3168/jds.s0022-0302(98)75866-7openalex-snapshot
Supra-aggregates of Casein Micelles as a Prelude to Coagulation
inferredcites →https://doi.org/10.3177/jnsv.44.447openalex-snapshot
Preparation and Characterization of Micellar Calcium Phosphate-Casein Phosphopeptide Complex.
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Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Structural changes of calcium-depleted casein micelle suspensions studied by SAXS
inferred← citeshttps://doi.org/10.1016/j.colsurfb.2012.11.032openalex-snapshot
In vitro interactions between probiotic bacteria and milk proteins probed by atomic force microscopy
inferred← citeshttps://doi.org/10.1016/j.colsurfb.2016.07.030openalex-snapshot
Heat-induced gelation of casein micelles in aqueous suspensions at different pH
inferred← citeshttps://doi.org/10.1016/j.colsurfb.2017.12.029openalex-snapshot
Specific effect of calcium ions on thermal gelation of aqueous micellar casein suspensions
inferred← citeshttps://doi.org/10.1016/j.colsurfb.2018.09.079openalex-snapshot
A comparison among β-caseins purified from milk of different species: Self-assembling behaviour and immunogenicity potential
inferred← citeshttps://doi.org/10.1016/j.colsurfb.2018.10.067openalex-snapshot
Colloidal properties of protein complexes formed in β-casein concentrate solutions as influenced by heating and cooling in the presence of different solutes
inferred← citeshttps://doi.org/10.1016/j.colsurfb.2019.03.051openalex-snapshot
Casein nanomicelle as an emerging biomaterial—A comprehensive review
inferred← citeshttps://doi.org/10.1016/j.colsurfb.2019.110363openalex-snapshot
The surface properties of milk fat globules govern their interactions with the caseins: Role of homogenization and pH probed by AFM force spectroscopy
inferred← citeshttps://doi.org/10.1016/j.colsurfb.2021.111930openalex-snapshot
Spectroscopic and docking studies of the interaction mechanisms of xylitol with α-casein and κ-casein
inferred← citeshttps://doi.org/10.1016/j.crfs.2021.02.004openalex-snapshot
Revisiting the dynamics of proteins during milk powder hydration using asymmetric flow field-flow fractionation (AF4)
inferred← citeshttps://doi.org/10.1016/j.crfs.2022.09.026openalex-snapshot
What is the impact of amino acid mutations in the primary structure of caseins on the composition and functionality of milk and dairy products?
inferred← citeshttps://doi.org/10.1016/j.fbio.2019.04.003openalex-snapshot
Study of milk coagulation induced by chymosin using atomic force microscopy
inferred← citeshttps://doi.org/10.1016/j.fbio.2022.102200openalex-snapshot
Casein nanoformulations - Potential biomaterials in theranostics
inferred← citeshttps://doi.org/10.1016/j.fbio.2024.105060openalex-snapshot
A review of camel β-casein: From purification processes, to bioactivity and techno-functionality
inferred← citeshttps://doi.org/10.1016/j.fbio.2024.105715openalex-snapshot
Innovative targeted protection of lactoferrin enriched whey increased the immunoactivity of infant formula
inferred← citeshttps://doi.org/10.1016/j.fbio.2025.106068openalex-snapshot
The composition, microstructure, interaction with polysaccharides of casein micelles and their potential application as drug delivery-a review
inferred← citeshttps://doi.org/10.1016/j.fbio.2025.106361openalex-snapshot
HIPE-gels performance: Role of sodium hyaluronate conformation and concentration in structure and 3D printing
inferred← citeshttps://doi.org/10.1016/j.fbp.2022.09.009openalex-snapshot
Review on mechanisms leading to fouling and stability issues related to heat treatment of casein-based RTD beverages
inferred← citeshttps://doi.org/10.1016/j.fbp.2022.10.012openalex-snapshot
Impact of casein demineralization on the fouling of UHT plant and the heat stability of high protein beverages: A pilot scale study
inferred← citeshttps://doi.org/10.1016/j.fhfh.2021.100014openalex-snapshot
Statistical analysis of the swelling process of casein microparticles based on single particle measurements
inferred← citeshttps://doi.org/10.1016/j.fhfh.2021.100048openalex-snapshot
Phase separation of a milk protein and guar gum: The effect of guar gum molecular weight and oil addition on the phase diagram
inferred← citeshttps://doi.org/10.1016/j.fochx.2022.100356openalex-snapshot
Impact of high hydrostatic pressure on the micellar structures and physicochemical stability of casein nanoemulsion loading quercetin
inferred← citeshttps://doi.org/10.1016/j.foodchem.2011.11.019openalex-snapshot
Heating of milk alters the binding of curcumin to casein micelles. A fluorescence spectroscopy study
inferred← citeshttps://doi.org/10.1016/j.foodchem.2012.03.053openalex-snapshot
Evaporative concentration of skimmed milk: Effect on casein micelle hydration, composition, and size
inferred← citeshttps://doi.org/10.1016/j.foodchem.2012.10.144openalex-snapshot
Binding of vitamin A with milk α- and β-caseins
inferred← citeshttps://doi.org/10.1016/j.foodchem.2013.06.130openalex-snapshot
Temperature-dependent dynamics of bovine casein micelles in the range 10–40°C
inferred← citeshttps://doi.org/10.1016/j.foodchem.2015.12.035openalex-snapshot
Interactions of milk α- and β-casein with malvidin-3-O-glucoside and their effects on the stability of grape skin anthocyanin extracts
inferred← citeshttps://doi.org/10.1016/j.foodchem.2016.04.116openalex-snapshot
Preheated milk proteins improve the stability of grape skin anthocyanins extracts
inferred← citeshttps://doi.org/10.1016/j.foodchem.2018.11.083openalex-snapshot
Solvent-mediated pressure-treated bixin-casein complexation for targeted color delivery
inferred← citeshttps://doi.org/10.1016/j.foodchem.2019.04.028openalex-snapshot
Acid and rennet-induced coagulation behavior of casein micelles with modified structure
inferred← citeshttps://doi.org/10.1016/j.foodchem.2019.125574openalex-snapshot
Biotechnological potential of a cysteine protease (CpCP3) from Calotropis procera latex for cheesemaking
inferred← citeshttps://doi.org/10.1016/j.foodchem.2019.126063openalex-snapshot
Casein-based hydrogels: A mini-review
inferred← citeshttps://doi.org/10.1016/j.foodchem.2020.126418openalex-snapshot
Fabrication of caseins nanoparticles to improve the stability of cyanidin 3-O-glucoside
inferred← citeshttps://doi.org/10.1016/j.foodchem.2020.127440openalex-snapshot
Effects of calcium chelation on the neutralization of milk protein isolate and casein micelle reassembling
inferred← citeshttps://doi.org/10.1016/j.foodchem.2021.129820openalex-snapshot
Interactions between caseins and food-derived bioactive molecules: A review
inferred← citeshttps://doi.org/10.1016/j.foodchem.2021.131935openalex-snapshot
Temperature-dependent dissociation of human micellar β-casein: Implications of its phosphorylation degrees and casein micelle structures
inferred← citeshttps://doi.org/10.1016/j.foodchem.2022.133528openalex-snapshot
Differentiating ultra-high temperature milk and reconstituted milk using an untargeted peptidomic approach with chemometrics
inferred← citeshttps://doi.org/10.1016/j.foodchem.2022.134319openalex-snapshot
Use of Calotropis procera cysteine peptidases (CpCPs) immobilized on glyoxyl-agarose for cheesemaking
inferred← citeshttps://doi.org/10.1016/j.foodchem.2023.135494openalex-snapshot
Dietary supplementation with casein/cyanidin-3-O-glucoside nanoparticles alters the gut microbiota in high-fat fed C57BL/6 mice
inferred← citeshttps://doi.org/10.1016/j.foodchem.2023.135779openalex-snapshot
Casein structures differently affect postprandial amino acid delivery through their intra-gastric clotting properties
inferred← citeshttps://doi.org/10.1016/j.foodchem.2023.136178openalex-snapshot
High-intensity ultrasound treatment on casein: Pea mixed systems: Effect on gelling properties
inferred← citeshttps://doi.org/10.1016/j.foodchem.2024.138359openalex-snapshot
Exploring the effect of high pressure in the denaturation of casein micelles by in-situ SERS
inferred← citeshttps://doi.org/10.1016/j.foodchem.2024.138956openalex-snapshot
Casein-based hydrogels: Advances and prospects
inferred← citeshttps://doi.org/10.1016/j.foodchem.2024.139369openalex-snapshot
Stabilizing interactions of casein microparticles after a thermal post-treatment
inferred← citeshttps://doi.org/10.1016/j.foodchem.2025.143114openalex-snapshot
Supramolecular recognition, fluorescence, and sensing: Two trilobal dyes and casein in milk
inferred← citeshttps://doi.org/10.1016/j.foodchem.2025.144235openalex-snapshot
Efficient and safe removal of free and casein-bound oxytetracycline from milk via pulsed electric field
inferred← citeshttps://doi.org/10.1016/j.foodchem.2026.149743openalex-snapshot
High-temperature acidification upgraded the stability of acidified milk through fibrillation of casein micelles
inferred← citeshttps://doi.org/10.1016/j.foodchem.2026.150268openalex-snapshot
Clarifying the “component-structure-function” mechanism in processed mozzarella cheese: the mechanistic role of fat, protein, and water interactions on quality and texture
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2011.05.014openalex-snapshot
Polysaccharide–protein interactions in dairy matrices, control and design of structures
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2011.11.009openalex-snapshot
31P NMR spectroscopic investigations of caseins treated with microbial transglutaminase
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2012.09.006openalex-snapshot
Interactions between casein layers adsorbed on hydrophobic surfaces from self consistent field theory: κ-casein versus para-κ-casein
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2013.01.001openalex-snapshot
Physico-chemical properties of casein micelles in unheated skim milk concentrated by osmotic stressing: Interactions and changes in the composition of the serum phase
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2013.01.004openalex-snapshot
pH-induced demineralization of casein micelles modifies their physico-chemical and foaming properties
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2013.01.010openalex-snapshot
Influence of pH value and locust bean gum concentration on the stability of sodium caseinate-stabilized emulsions
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2014.03.022openalex-snapshot
Studying the structure of β-casein-depleted bovine casein micelles using electron microscopy and fluorescent polyphenols
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2014.05.011openalex-snapshot
The effect of ultrasound treatment on the structural, physical and emulsifying properties of dairy proteins
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2014.08.005openalex-snapshot
On the cohesive properties of casein micelles in dense systems
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2015.03.016openalex-snapshot
Dissociation of native casein micelles induced by sodium caseinate
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2015.04.024openalex-snapshot
The effect of pH on the structure and phosphate mobility of casein micelles in aqueous solution
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2015.04.031openalex-snapshot
Spatial arrangement of casein micelles and whey protein aggregate in acid gels: Insight on mechanisms
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2015.10.016openalex-snapshot
Incorporation of polysaccharides into sodium caseinate-low melting point fat microparticles improves probiotic bacterial survival during simulated gastrointestinal digestion and storage
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2016.01.028openalex-snapshot
Functional properties of peptides: From single peptide solutions to a mixture of peptides in food products
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2016.05.030openalex-snapshot
Heat-induced gelation of mixtures of whey protein isolate and sodium caseinate between pH 5.8 and pH 6.6
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2016.11.041openalex-snapshot
Structure and stability of sodium-caseinate-stabilized oil-in-water emulsions as influenced by heat treatment
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2017.01.007openalex-snapshot
Probing the internal and external micelle structures of differently sized casein micelles from individual cows milk by dynamic light and small-angle X-ray scattering
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2017.03.013openalex-snapshot
Effect of the pH and NaCl on the microstructure and rheology of mixtures of whey protein isolate and casein micelles upon heating
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2017.07.005openalex-snapshot
Heat-set emulsion gels of casein micelles in mixtures with whey protein isolate
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2017.07.033openalex-snapshot
Connection between dynamic rheometry and pair interactions of casein micelles in concentrated skim milk
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2017.10.008openalex-snapshot
Review on the loading efficacy of dietary tea polyphenols with milk proteins
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2018.02.010openalex-snapshot
FTIR fingerprinting of structural changes of milk proteins induced by heat treatment, deamidation and dephosphorylation
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2018.03.043openalex-snapshot
Sulfate dodecyl sodium-induced stability of a model intrinsically disordered protein, bovine casein
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2018.09.032openalex-snapshot
Membrane-based fractionation, enzymatic dephosphorylation, and gastrointestinal digestibility of β-casein enriched serum protein ingredients
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2018.12.005openalex-snapshot
Tribo-rheology characteristics and microstructure of a protein solution with varying casein to whey protein ratios and addition of hydrocolloids
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2019.01.043openalex-snapshot
Asymmetric flow field flow fractionation for the investigation of caseins cross-linked by microbial transglutaminase
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2019.01.048openalex-snapshot
Heat-induced gelation of mixtures of casein micelles with whey protein aggregates
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2019.03.006openalex-snapshot
Elucidating the interaction mechanism of eriocitrin with β-casein by multi-spectroscopic and molecular simulation methods
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2020.106414openalex-snapshot
Improvement of vitamin C stability in vitamin gummies by encapsulation in casein gel
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2020.106511openalex-snapshot
Revisiting neutron scattering data from deuterated milk
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2021.106599openalex-snapshot
Gastric colloidal behaviour of milk protein as a tool for manipulating nutrient digestion in dairy products and protein emulsions
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2021.106653openalex-snapshot
The heterogeneous substructure of casein micelles evidenced by SAXS and NMR in demineralized samples
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2021.106718openalex-snapshot
Effects of polysaccharide charge density on the structure and stability of carboxymethylcellulose-casein nanocomplexes at pH 4.5 prepared with and without a pH-cycle
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2021.106755openalex-snapshot
Heat-induced gelation of casein micelles
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2022.107819openalex-snapshot
Turbulence-dependent reversible liquid-gel transition of micellar casein-stabilised emulsions
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2022.107863openalex-snapshot
Controlled gastrointestinal digestion of micellar casein loaded anthocyanins: The chelating and complexing effect of dextran sulfate
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2022.108295openalex-snapshot
Interfacial adsorption behavior and interaction mechanism in saponin–protein composite systems: A review
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2023.108483openalex-snapshot
Single and double Pickering emulsions stabilized by sodium caseinate: Effect of crosslinking density
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2023.108881openalex-snapshot
Casein micelle with different β-casein phenotypes: Fingerprinting pH-induced structural changes using FTIR and NMR spectroscopies
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2023.109466openalex-snapshot
Effect of enzymatic dephosphorylation on caprine casein micelle structure
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2023.109618openalex-snapshot
Evaluation on pH-dependent thermal gelation performance of chickpea, pea protein, and casein micelles
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2024.109811openalex-snapshot
Structural and compositional characterization of Ca- and β-casein enriched casein micelles
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2025.111136openalex-snapshot
Tuning the structure and coagulation behaviour of artificial casein micelles by varying the casein composition
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2025.111377openalex-snapshot
Sum-weighted casein micelle AF4-UV-SAXS data disentangled - A new method for characterization and evaluation of widely size distributed samples
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2025.111488openalex-snapshot
Phosphate salt-induced structure formation in casein suspensions
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2025.111668openalex-snapshot
Tunable self-association of partially dephosphorylated beta-casein
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2025.112182openalex-snapshot
Investigating the impact of different dietary fibres on the gastrointestinal digestion of food proteins
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2025.112258openalex-snapshot
Comparison of different strategies based on β-casein dynamics to encapsulate curcumin in casein micelles
inferred← citeshttps://doi.org/10.1016/j.foodhyd.2026.113227openalex-snapshot
Understanding the mechanism of cold gel formation in reconstituted micellar casein dispersions
inferred← citeshttps://doi.org/10.1016/j.foodres.2013.06.025openalex-snapshot
On line diffusing wave spectroscopy during rheological measurements: A new instrumental setup to measure colloidal instability and structure formation in situ
inferred← citeshttps://doi.org/10.1016/j.foodres.2018.12.015openalex-snapshot
Identification of angiotensin converting enzyme and dipeptidyl peptidase-IV inhibitory peptides derived from oilseed proteins using two integrated bioinformatic approaches
inferred← citeshttps://doi.org/10.1016/j.foodres.2019.108846openalex-snapshot
Using the USAXS technique to reveal the fat globule and casein micelle structures of bovine dairy products
inferred← citeshttps://doi.org/10.1016/j.foodres.2019.108847openalex-snapshot
The adhesion of homogenized fat globules to proteins is increased by milk heat treatment and acidic pH: Quantitative insights provided by AFM force spectroscopy
inferred← citeshttps://doi.org/10.1016/j.foodres.2021.110451openalex-snapshot
The relationship between ultra-small-angle X-ray scattering and viscosity measurements of casein micelles in skim milk concentrates
inferred← citeshttps://doi.org/10.1016/j.foodres.2021.110797openalex-snapshot
Enhanced rehydration behaviors of micellar casein powder: The effects of high hydrostatic pressure treatments on micelle structures
inferred← citeshttps://doi.org/10.1016/j.foodres.2022.110981openalex-snapshot
Temperature effects on calcium binding to caseins
inferred← citeshttps://doi.org/10.1016/j.foodres.2022.111625openalex-snapshot
Temperature effect on calcium binding to aspartate and glutamate
inferred← citeshttps://doi.org/10.1016/j.foodres.2023.112810openalex-snapshot
Application of small angle scattering (SAS) in structural characterisation of casein and casein-based products during digestion
inferred← citeshttps://doi.org/10.1016/j.foodres.2023.112862openalex-snapshot
Nanostructural changes in Polysaccharide-Casein Gel-Like structures upon in vitro gastrointestinal digestion
inferred← citeshttps://doi.org/10.1016/j.foodres.2023.113558openalex-snapshot
Gastric aggregation of micellar casein powders induced by high hydrostatic pressure: Effect of serum Ca2+ level
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