Improved antitumor activity and IgE/IgG–binding ability of α‐Lactalbumin/β‐lactoglobulin induced by ultrasonication prior to binding with oleic acid

Abstract

Milk whey proteins, an important source of ingredient, are used for a variety of functional applications in the food industry (Foegeding et al., 2002). It is a diverse group of proteins with different structure, such as bovine β-lactoglobulin (18.3 kDa, 162 amino acid residues)

Ultrasound Improved the Non-Covalent Interaction of β-Lactoglobulin with Luteolin: Regulating Human Intestinal Microbiota and Conformational Epitopes Reduced Allergy Risks

“…α-helix of S-LG–LUT decreased to 2.39%, and β-sheet increased to 42.37%, indicating that part of the α-helix of β-LG may be extended to β-sheet whereas β-LG binds with LUT. The change was consistent with other research results [ 25 , 26 ]. However, the secondary structure change of U-LG–LUT is the most significant in all tested samples, for instance, the α-helix content decreased from 13.24% to 0.61% and the β-sheet content increased from 29.14% to 43.66%.…”

“…The result can explain the decrease in IgG/IgE binding activity ( Figure 3 A,B) and the mediator release ( Figure 3 C,D). Similar results were achieved in the study by Liu et al [ 25 ], who proved that the changes in conformational epitopes could decrease allergenicity. Therefore, the destruction in the conformational epitopes of the β-LG–LUT complex dramatically reduced allergenicity.…”

“…Eight amino acid residues of β-LG (Trp19, Ser21, Tyr42, Glu45, Gln59, Glu158, Gln159 and His161) interacted with LUT through van der Waals bonds. Trp19, Leu156, Glu157, and His161 of β-LG, adjacent to the pocket, bind with LUT through strong hydrophobic interactions [ 25 ]. These results showed that hydrogen bonds, van der Walls bonds, and hydrophobic interactions were the major driving forces taking part in the formation of the β-LG–LUT complex.…”

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

“…54 In contrast, processing modifications like glycation, phosphorylation and acetylation reduce the allergenicity of these complexes. 55 An additional phenomenon occurring in the complex milk matrix during processing is that ALA thermally co-aggregates with the heat-sensitive lactoferrin, accompanied by an increase in bsheet content and decrease in a-helix content. 56 Dimers of ALA are found in raw milk (pdb 1F6R), but dry heating leads to extensive dimer and aggregate formation of ALA, 57 in pdb a hexameric variant is depicted (1F6R) (Fig.…”