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 ß-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 ß-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. elegans and mouse models, indicate that the digested fibrils present no observable cytotoxicity, physiological abnormalities in health-span, nor accumulation of fibril-induced plaques in brain nor other organs. These extensive in-vitro and in-vivo studies together suggest that the digested food amyloids are at least equally as safe as those obtained from the digestion of corresponding native monomers, pointing to food amyloid fibrils as potential ingredients for human nutrition.

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. The covalent bonding between the proteins and different carbohydrates created via the initial stage of the Maillard reaction can improve the techno-functional characteristics of these proteins without the involvement of potentially toxic chemicals. However, compared to studies with animal-derived proteins, glycation studies on plant proteins are currently still underrepresented in literature. This review provides an overview of the existing studies on the glycation of the major groups of plant proteins with different carbohydrates using different preparation methods. Emphasis is put on the reaction conditions used for glycation as well as the modifications to physicochemical properties and techno-functionality. Different applications of these glycated plant proteins in emulsions, foams, films, and encapsulation systems are introduced. Another focus lies on the reaction chemistry of the Maillard reaction and ways to harness it for controlled glycation and to limit the formation of undesired advanced glycation products. Finally, challenges related to the controlled glycation of plant proteins to improve their properties are discussed.

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 ± 0.1 mN m-1) compared to the unheated fibers (16.3 ± 1.4 mN m-1) due to the covalently bound hydrophilic maltodextrin in the glycoconjugates. Applied in oil-in-water emulsions (10% w/w oil, 0.7% protein, 103.4 MPa, 3 passes), unheated PPI-maltodextrin fibers produced large droplets (72-259 µm) with multimodal distributions in the pH range of 2-7. The largest droplet size was at pH 4, which was around the pI of PPI. Emulsions were also prone to flocculation, which was most probably caused by a depletion flocculation mechanism due to an excess of maltodextrin in the aqueous phase. In contrast, emulsions made with heated PPI-maltodextrin fibers were monomodal (36-55 µm) at pH 2-7 and only showed a minor increase in droplet size close to the pI of PPI. The improved properties of heated PPI-maltodextrin fibers were ascribed to the enhanced steric repulsion caused by the covalently bound maltodextrin. The results indicate that Maillard-induced glycation of PPI with maltodextrin in electrospun fibers can be used as a novel method to improve the properties of PPI as a plant-based emulsifier.

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. The binding ratio between WPI and maltodextrin was assessed via the free amino groups. The molecular weight of the conjugates and the reaction yield were studied by size exclusion chromatography. The impact of different mass ratios between WPI and maltodextrin in the fibers (5:95, 10:90, 20:80, and 25:75 w/w) was investigated. With increasing WPI content, the binding ratio of maltodextrin decreased from ∼2.1 to ∼1.2. Preferably small polysaccharides (2-13 kDa) from the maltodextrin reacted. Protein specific reaction yields of up to 44.52 ± 7.46% w/w were demonstrated in all WPI-maltodextrin fibers after heating.