http://www.worldallergyorganizationjournal.org/article/S1939455122000448/pdf

Diagnosis and Rationale for Action against Cow's Milk Allergy (DRACMA) Guidelines update - III - Cow's milk allergens and mechanisms triggering immune activation

Investigation of an Uncommon Artifact during Reducing Capillary Electrophoresis-Sodium Dodecyl Sulfate Analysis of a Monoclonal Antibody with Dynamic Light Scattering and Reversed Phase High-Performance Liquid Chromatography

A comparative study of structural and digestive properties of bovine, goat and human α-Lactalbumin with different calcium binding levels

Abstract Whey protein emulsion gel is an ideal model food for revealing how the multilength scale food structures affect food digestion, as their structure and mechanical properties can be precisely manipulated by controlling the type and intensity of intermolecular interactions between protein molecules. However, there are still significant understanding gaps among intermolecular interactions, protein aggregation and gelation, emulsion gel formation, gel breakdown in the gastrointestinal tract (GIT), and the practical use of whey protein emulsion gels, which limits their GIT‐targeted applications. In this regard, the relationship between the structure and digestion behavior of heat‐set whey protein emulsion gels is reviewed and discussed mainly from the following aspects: (1) structural characteristics of whey protein molecules; (2) how different types of intermolecular interactions influence heat‐induced aggregation and gelation of whey protein in the aqueous solutions and the oil‐in‐water emulsions, and the mechanical properties of the final gels; (3) functions of the mouth, the stomach, and the small intestine in processing of solid foods, and how different types of intermolecular interactions influence the breakdown properties of heat‐set whey protein emulsion gels in GIT (i.e., their respective role in controlling gel digestion). Finally, the implications of knowledge derived from the formation and gastrointestinal breakdown of heat‐set whey protein emulsion gels for developing controlled delivery vehicles, human satiety enhancers, and sensory modifiers are highlighted. 

Understanding of formation, gastrointestinal breakdown, and application of whey protein emulsion gels: Insights from intermolecular interactions

Influence of heat treatment and calcium sequestering salts on in vitro protein digestion in blends of skimmed buffalo and bovine milk

Selective thermal precipitation followed by a mechanical separation step is a well described method for fractionation of the main whey proteins, α-lactalbumin (α-la) and β-lactoglobulin (β-lg). By choosing appropriate environmental conditions the thermal precipitation of either α-la or β-lg can be induced. Whereas β-lg irreversibly aggregates, the precipitated α-la can be resolubilized by a subsequent adjustment of the solution’s pH and the ionic composition. This study reports on the analytical characterization of resolubilized α-la compared to its native counterpart as a reference in order to assess whether the resolubilized α-la can be considered close to ‘native’. Turbidity and quantification by RP-HPLC of the resolubilized α-la solutions were used as a measure of solubility in aqueous environment. RP-HPLC was also applied to determine the elution time as a measure for protein’s hydrophobicity. DSC measurement was performed to determine the denaturation peak temperature of resolubilized α-la. FTIR spectroscopy provided insights in the secondary structure. The refolding of α-la achieved best results using pH 8.0 and a 3-fold stoichiometric amount of Ca2+ per α-la molecule. The results showed that the mechanism of aggregation induced by gentle thermal treatment under acidic conditions with subsequent mechanical separation is reversible to a certain extent, however, the exact native conformation was not restored.

Molecular Analytical Assessment of Thermally Precipitated α-Lactalbumin after Resolubilization.

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Molecular Analytical Assessment of Thermally Precipitated α-Lactalbumin after Resolubilization.