Milk β‐casein as delivery systems for luteolin: Multi‐spectroscopic, computer simulations, and biological studies

Abstract

In recent years, there has been a lot of interest in functional food research and application. (Gao et al., 2019). The addition of bioactive substances into food is a simple way to develop new functional foods with excellent efficacy (Chen et al., 2006). However, many bioactive substances have low water solubility and poor stability. To increase the bioavailability of this kind of bioactive substances, various encapsulation techniques have been developed (Okuro et al., 2015). The solubility and bioavailability of some substances can be improved

Regulation Mechanism of Phenolic Hydroxyl Number on Self-Assembly and Interaction between Edible Dock Protein and Hydrophobic Flavonoids

“…In general, protein molecules and flavonoid molecules can undergo noncovalent interactions including hydrogen bonding and van der Waals (Δ H < 0, Δ S < 0), hydrophobic (Δ H > 0, Δ S > 0), and electrostatic interactions (Δ H < 0, Δ S > 0) . In the present experiments, the thermodynamic parameters (Δ H , Δ S , Δ G ) during the interactions of EDP and flavonoids were calculated via the Van’t Hoff equation.…”

“…38 In general, protein molecules and flavonoid molecules can undergo noncovalent interactions including hydrogen bonding and van der Waals (ΔH < 0, ΔS < 0), hydrophobic (ΔH > 0, ΔS > 0), and electrostatic interactions (ΔH < 0, ΔS > 0). 39 In the present experiments, the thermodynamic parameters (ΔH, ΔS, ΔG) during the interactions of EDP and flavonoids were calculated via the Van't Hoff equation. Table 2 exhibits that ΔH < 0 and ΔS < 0 during the combination of Gal-EDP nanomicelles, indicating that hydrogen bonding and van der Waals were the main interaction forces.…”

Characterization and biological function analysis of endogenous peptides derived from donkey colostrum proteins

“…33 As an essential functional protein in milk, casein transports essential nutrients from mother to newborn mammals. 34 Donkey milk mainly contains α S1 - and β-casein, while α S2 - and κ-casein are minor components. β-Casein accounts for up to 80% of the total casein in human milk and is also the principal protein in the casein fraction of donkey milk.…”

Interfacial Rheological Study of β-Casein/Pectin Mixtures at the Air/Water Interface

“…For the design of new products, the interactions between proteins and polysaccharides have to be deeply understood. Milk-based foods are a big slice of the food market, and the proteins from milk have been extensively investigated to create colloidal systems, emulsions, gels, and bioactive foods [12,13].…”

“…The isoelectric point is between 4.1 and 5.3 [16]. β-casein forms about 30% of the casein proteins and has a principal hydrophobic behavior even if it is recognized, among the caseins, as the most soluble, highly amphiphilic, and calcium-sensitive phosphoprotein [13,18]. β-casein is rich in prolamine and poor in cysteine; it is not able to form intramolecular covalent disulfide bonds [15] and lacks a secondary structure because of the presence of uniformly distributed prolines in the complete amino acid sequence of β-casein [19,20].…”