Simulated gastrointestinal digestion of protein alginate complexes: effects of whey protein cross-linking and the composition and degradation of alginate

Abstract

Alginate effectively protects whey protein from gastric digestion at pH 3. Complexes dissolve under intestinal conditions (pH 7) where whey protein is degraded by trypsin and alginate can be degraded by bacterial lyases.

Whey Protein Isolate Composites as Potential Scaffolds for Cultivated Meat

“…When WPI and Alg components were mixed together, forming a complex solution, there was a noticeable increase in the shear moduli of the blend solutions. 31,57 In this study, the interactions between the aqueous solutions comprising 10% (w/v) WPI and 3% (w/v) Alg resulted in a significant increase in both G′ and G″ (p < 0.005) compared to the solutions alone (Figure 2A). Interactions were observed after the moduli of the blended solutions were compared to the summations of the constituent components by themselves.…”

“…Interactions were observed after the moduli of the blended solutions were compared to the summations of the constituent components by themselves. When WPI and Alg components were mixed together, forming a complex solution, there was a noticeable increase in the shear moduli of the blend solutions. , There was also a significant increase in G ′ and G ″ observed in the blended solution comprising 10% WPI and 3% AlgMA ( p < 0.05) (Figure B). Significant interactions were not observed in the blend comprising 10% WPI-MA and 3% AlgMA (Figure D).…”

“…The interaction between WPI and Alg in their nonmodified forms has been previously reported, and is influenced by a variety of factors, including the weight ratio of WPI to Alg, the mannuronate/guluronate ratio of the Alg, degree of Alg protonation, WPI acidic side chains present, among others. ,− We determined if the interactions were changed at our solution concentrations and postchemical modification of the polymers. Rheometry was performed on the hydrogel constituent materials and polymer blend solutions .…”

“…Whey protein, in either the concentrate (whey protein concentrateWPC, usually 70–80% protein) or isolate (whey protein isolateWPI, >90%) form, is a common food additive as a colloid or gelling agent. In its nonmodified form, WPI will self-gel when heated above 80 °C. , Despite this inherent ability to gel, the mechanical properties are less than desirable for muscle and fat tissue and lack tunability. , To vary the performance of WPI hydrogels, other biomolecules, such as alginate, chitosan, soy protein, and dextran, have been added to WPI slurries and three-dimensional (3D) printing inks; , however, these interactions were based on electrostatic interactions, thermal-gelling, and entanglement within an ionically cross-linked hydrogel. − …”

Effect of Molecules’ Physicochemical Properties on Whey Protein/Alginate Hydrogel Rheology, Microstructure and Release Profile

“…These observations seem to indicate an influence of the encapsulated compound on the behavior of the WP/ALG MP produced. The physicochemical properties of both the polymer and drug used in the formulation can be considered to be important variables influencing solution viscosity [ 15 , 16 ], microparticle formation [ 17 , 18 , 19 ] and settings like encapsulation efficiency and drug/probiotic release [ 8 , 20 , 21 , 22 ]. Encapsulation efficiency of microparticles could also be modified by microencapsulation techniques, polymer concentration, solubility of polymers in solvent, rate of solvent removal and solubility of organic solvent in water [ 23 , 24 ].…”