Food amyloid fibrils are safe nutrition ingredients based on in-vitro and in-vivo assessment.

Food protein amyloid fibrils have superior technological, nutritional, sensorial, and physical properties compared to native monomers, but there is as yet insufficient understanding of their digestive fate and safety for wide consumption. By combining SDS-PAGE, ELISA, fluorescence, AFM, MALDI-MS, CD, microfluidics, and SAXS techniques for the characterization of β-lactoglobulin and lysozyme amyloid fibrils subjected to in-vitro gastrointestinal digestion, here we show that either no noticeable conformational differences exist between amyloid aggregates and their monomer counterparts after the gastrointestinal digestion process (as in β-lactoglobulin), or that amyloid fibrils are digested significantly better than monomers (as in lysozyme). Moreover, in-vitro exposure of human cell lines and in-vivo studies with C.

Glycation of Plant Proteins Via Maillard Reaction: Reaction Chemistry, Technofunctional Properties, and Potential Food Application.

Plant proteins are being considered to become the most important protein source of the future, and to do so, they must be able to replace the animal-derived proteins currently in use as techno-functional food ingredients. This poses challenges because plant proteins are oftentimes storage proteins with a high molecular weight and low water solubility. One promising approach to overcome these limitations is the glycation of plant proteins.

Improvement of emulsifying behavior of pea proteins as plant-based emulsifiers via Maillard-induced glycation in electrospun pea protein-maltodextrin fibers.

Heat-treated electrospun pea protein isolate (PPI)-maltodextrin fibers containing glycated PPI were analyzed for their interfacial tension and emulsifying properties compared to unheated electrospun PPI-maltodextrin fibers. Interfacial tension at the oil-water-interface of the heated fibers was higher (19.2 ± 0.

Formation of Whey Protein Isolate (WPI)-Maltodextrin Conjugates in Fibers Produced by Needleless Electrospinning.

Glycation of proteins via the first stage of the Maillard reaction is capable of improving their stability but not economically feasible yet. This work reports the glycation of whey protein isolate (WPI) with maltodextrin at a high yield after heating electrospun fibers made from the reactants. Glycoconjugates were characterized by Fourier transform infrared spectroscopy (FTIR) and SDS-PAGE.