Does protein deamidation enhance rice protein concentrate's ability to produce and stabilize high internal phase emulsions?

Rice is one of the most consumed grains in the world. Rice protein has great nutritional value as a hypoallergenic protein and due to its high lysine content, a limiting amino acid in several other plant protein sources. However, rice protein has low solubility, hampering its use in many applications in the food industry. In this context, alkaline deamidation (0.5 h, 343 K, and pH 11) was applied to modify the protein structure of rice protein concentrate (RPC). After deamidation, two protein powders were produced: (i) one containing the whole protein fraction recovered after RPC deamidation (DT) and (ii) another containing only the soluble fraction recovered after RPC deamidation (DS). Protein dispersions were characterized by SDS-PAGE, zeta potential, solubility, surface hydrophobicity, and capacity to hold water and oil. RPC could not structure canola oil into a high internal phase emulsion (HIPE) due to its low solubility. DT and DS dispersions displayed solubility much higher than RPC and enabled the structuration of HIPEs with 75 % (w/w) canola oil and 25 % of DT or DS dispersions (2, 4, and 6 % w/w). HIPEs were characterized regarding particle size, microstructure, Turbiscan and oil loss stabilities, and rheological behavior for 60 days. Turbiscan analysis and oil loss measurements showed high stability, and the thixotropy tests showed high recovery in all HIPEs. Higher protein concentrations and DS dispersions produced HIPEs with smaller particle sizes. However, rheological measurements indicate that HIPEs produced with DT dispersions had better results, maintaining their structure over the 60 days. Furthermore, DT is cheaper to produce; therefore, DT 4 and 6 % w/w were the most promising for producing HIPEs. The HIPEs produced in this study displayed great potential as fat replacers.

Lutein bioaccessibility in casein-stabilized emulsions is influenced by the free to acylated carotenoid ratio, but not by the casein aggregation state.

Considering that carotenoids are found acylated to fatty acids in most edible fruits, the influence of the ratio of free to acylated lutein on the hydrolysis extent and bioaccessibility was evaluated by in vitro digestion. For this purpose, for the first time, esterified, free, or a mixture of both carotenoid forms was used in the lipid phase of emulsions stabilized by sodium caseinate (NaCas) and native phosphocaseinate (PPCN). Marigold petals was used as a source of lutein-rich extracts. The emulsions were characterized and the extent of ester hydrolysis, carotenoid recovery, and bioaccessibility were evaluated by LC-DAD-MS/MS. Besides low polydispersity, NaCas and PPCN stabilized emulsions exhibited a constant mean droplet diameter of about 260 and 330 nm, respectively, after 7 days. Caseins were completely digested after the gastric digestion step. Moreover, casein supramolecular structure did not significantly affect carotenoid bioaccessibility. Lutein was majorly found in its free form in all bioaccessible fractions. The carotenoid bioaccessibility increased from 3% to 40% by increasing the percentage of free carotenoids from 0.5 to 100% in the emulsions; but the carotenoid recovery and hydrolysis extent of lutein esters were not affected. In conclusion, emulsion-based systems for carotenoid delivery stabilized either by NaCas or PPCN provided similar carotenoid bioaccessibility. Furthermore, bioaccessibility was inversely dependent on the overall hydrophobicity of the carotenoid extract. Our results suggest that the low bioaccessibility of esterified carotenoids was a consequence of their limited hydrolysis extent. This study provides information that may help design emulsion-based systems stabilized by food protein as a vehicle for carotenoids.

Structural and foaming properties of whey and soy protein isolates in mixed systems before and after heat treatment.

The partial replacement of proteins from animal sources by plant proteins in formulated food products has been proposed as useful to improve sustainability aspects of the products without dramatically changing their techno-functional properties. Although several research groups have published on the gelling properties of mixed systems containing whey and soy protein isolates (WPI and SPI), their foaming properties are much less described. In this context, the main objective of this paper was to evaluate the structural and foaming properties of samples containing different mass ratios of WPI:SPI (100:0, 75:25, 50:50, 25:75 and 0:100) before and after heat treatment. The samples were evaluated according to their solubility, foaming capacity (FC), foam microstructure and foam stability (FS). Before heat treatment, mixing SPI to WPI did not affect the solubility of whey proteins, but, after heat treatment, insoluble co-aggregates were formed. Similar FC was measured for all samples despite their WPI:SPI ratio and the applied heat treatment. The partial replacement of WPI by SPI changed the microstructure of the foams and had an antagonistic effect on the FS of the samples, due to the negative effect of insoluble soy protein aggregates and/or insoluble co-aggregates on the reinforcement of the air-water interfacial film.