Effect of the non-covalent and covalent interactions between proteins and mono- or di-glucoside anthocyanins on β-lactoglobulin-digestibility. (December 2022)

• Record Type: Journal Article
• Authors: Khalifa, Ibrahim; Lorenzo, José M.; Bangar, Sneh Punia; Morsy, Osama M.; Nawaz, Asad; Walayat, Noman; Sobhy, Remah
• Is Part Of: Food hydrocolloids. Volume 133(2022)
• Publication Date: 2022-12
• Subjects: β-lactoglobulins -- Mono- and di-glucoside anthocyanins -- Covalent and non-covalent binding -- In vitro-digestion; Hydrocolloids -- Periodicals; Food additives -- Periodicals; Colloïdes -- Périodiques; Aliments -- Additifs -- Périodiques; Colloids; Food additives; Periodicals; Electronic journals; 664.06
• DOI: 10.1016/j.foodhyd.2022.107952
• Languages: English
• ISSNs: 0268-005X

Abstract

Abstract: The present study aims to affect the nature of the interaction between β-lactoglobulin (β-Lg) and cyanidin 3-glucoside (C3G) or cyanidin 3-rutinoside (C3R) on the digestibility, and antioxidant capacity. C3R and C3G were-conjugated with β-Lg by means of covalent and non-covalently interaction, and their binding ability, degree of hydrolysis, solvable proteins SDS-PAGE-bands, secondary structure, morphological clicks, and particles size were determined. Results disclosed that C3R and C3G improved the in vitro digestibility of β-Lg by amending the degree of hydrolysis, solvable peptides-parts, and declining its agglomeration. It was also found that C3R displayed better digestion-promoting effects than C3G, in which covalent interaction was more productive than the non-covalent one. Furthermore, C3G/R improved the antioxidant capacity of the digested peptides. Most notably, it was noted that C3G/R could partly unfold the β-Lg-structure via shifting their α-helix and β-sheet components. Furthermore, the binding of β-Lg-C3R/G was accountable for the modifications in the β-Lg subordinate structure. It was assumed that the partly unfolding in β-Lg-structure that was stimulated by β-Lg-C3R/G gathering might expand the availability of peptide bonds to the digestive enzymes and accelerate the ' digestibility of proteins. Graphical abstract: Image 1 Highlights: C3G and C3R aided the digestion of β-Lg proteins. C3G and C3R partially unfolded the secondary structure of β-Lg proteins. The covalent binding seems to be more efficient than the noncovalent one.