Interpolymeric Complexes Formed Between Whey Proteins and Biopolymers: Delivery Systems of Bioactive Ingredients

Abstract

Whey proteins are obtained from dairy industry waste. Studies involving the analysis of the bioactive compounds in whey show health benefits, as it is an excellent source of indispensable amino acids. Milk whey contains principally β-lactoglobulin, α-lactoglobulin, bovine serum albumin, and lactoferrin, proteins with innumerable functional and technological properties. One application of these proteins in food is the formation of interpolymer complexes, along with other proteins or anionic polysaccharides. The formation of complexes occurs mainly through electrostatic interactions between a negatively charged biopolymer and a positively charged biopolymer. This formation is influenced by factors such as pH, ionic strength, and biopolymer ratio. Because they do not use high temperatures and chemical reagents and have additional nutritional and functional value, these complexes have been used as encapsulating agents for bioactive ingredients. Recent studies on their training and applications are addressed in this review to boost new research and applications in the food industry, thus increasing opportunities for utilizing whey proteins.

A Brief Review of Edible Coating Materials for the Microencapsulation of Probiotics

“…Studies showed an increase in gelation ability and gel properties (strength, rigidity, or viscoelasticity) of β-LG when mixed with α-LA, suggesting a synergistic effect of these proteins in the gelation behaviour [171]. The calcium atom of α-LA can promote the formation of intermolecular ionic bonds, which makes this protein thermally stable and allow it to bind to other proteins [172]. Among several bio-properties attributed to α-LA, the digestion of α-LA releases small peptides that have shown antimicrobial activity against pathogenic bacteria, such as Escherichia coli, Klebsiella pneumoniae, Staphylococcus aureus, Staphylococcus epidermis, streptococci, and Candida albicans.…”

“…Among several bio-properties attributed to α-LA, the digestion of α-LA releases small peptides that have shown antimicrobial activity against pathogenic bacteria, such as Escherichia coli, Klebsiella pneumoniae, Staphylococcus aureus, Staphylococcus epidermis, streptococci, and Candida albicans. Moreover, these small peptides also exhibited the capacity to prevent enteropathogenic Escherichia coli, Salmonella typhimurium, and Shigella flexneri from adhering to intestinal cells [172,173]. Whey proteins, in its different forms, were recently explored as coating materials for the microencapsulation of probiotics [28,30,41,58,72,95,97,[102][103][104][105].…”

Comparison of low- and high-methoxyl pectin for the stabilization of whey protein isolate as carrier for lutein

“…Researchers reported the stabilization of the WPI using pectin as a layer between the protein molecules and the solvent (water). Several authors have applied J o u r n a l P r e -p r o o f this system to stabilize WPI to enrich products such as emulsions (Evans, Ratcliffe, & Williams, 2013;Neirynck, et al, 2007;Pimentel-Moral, Ochando-Pulido, Segura-Carretero, & Martinez-Ferez, 2018) as well as carriers or stabilizers of active compounds (Ozel, Cikrikci, Aydin, & Oztop, 2017;M. B. Santos, da Costa, & Garcia-Rojas, 2018;Su, Guo, Mao, Gao, & Yuan, 2018).…”

Development and Characterization of Whey Protein-Based Nano-Delivery Systems: A Review

“…As discussed earlier, whey proteins undergo conformational changes depending on the environmental conditions, such as pH and temperature. The conformational changes of whey proteins may affect not only binding of whey proteins with other molecules, such as BCs and co-delivery materials (e.g., carbohydrates), but also associations between whey protein molecules [82]. The confirmation can therefore be a crucial factor determining the physicochemical properties of NDSs, including size and surface charge.…”