Plant-based proteins are increasingly recognized for their environmental, ethical, and nutritional benefits. However, their digestibility varies due to factors such as molecular structure, amino acid composition, and processing methods. This review comprehensively analyzes methods used to assess plant protein digestibility, including in vivo, in vitro, and ex vivo approaches. While in vivo studies, particularly those using pigs, are considered the gold standard, in vitro and ex vivo models offer cost-effective and reproducible alternatives for simulating digestion. Additionally, antinutritional factors present in plant proteins can hinder digestibility, necessitating processing strategies such as fermentation, enzymatic hydrolysis, and high-pressure treatments to enhance protein bioavailability. Advances in evaluation techniques, including the Digestible Indispensable Amino Acid Score (DIAAS) and dynamic digestion models, offer more precise assessments of protein quality. By systematically comparing these methods, this review aims to guide food scientists and manufacturers in selecting appropriate evaluation strategies to improve the nutritional quality of plant-based protein products. Understanding the mechanisms influencing plant protein digestibility is essential for optimizing food formulations and supporting the broader adoption of sustainable protein sources in human diets.

Chitin is one of the most abundant natural polysaccharides in the world and it is mainly used to produce chitosan by a deacetylation process. In the present study, the extraction of chitin and chitosan from the Parastacus pugnax (P. pugnax) crayfish exoskeleton was studied for the first time. Thus, the P. pugnax crayfish exoskeleton was converted to chitosan following the steps of depigmentation, deproteinization, and deacetylation. The produced chitosan (Chitosan-CGNA) was characterized in terms of the protein content, solubility, degree of deacetylation, viscosity, molecular weight, FTIR, SEM, XRD, antimicrobial, and antioxidant activity. The results showed that the obtained chitosan had a high degree of deacetylation (91.55%) and a medium molecular weight (589.43 kDa). The antibacterial activity of the chitosan was tested against bacterial strains relevant for the food industry and the lowest minimum inhibitory concentration (MIC) values were evidenced with Salmonella tiphymurium (S. typhimurium), Staphylococcus aureus (S. aureus), Enterococcus faecalis (E. faecalis) and Listeria. Monocytogenes (L. monocytogenes). Moreover, the Chitosan-CGNA showed an effect on DPPH radical scavenging activity, and its antioxidant activity was dependent on concentration and deacetylation degree. These results suggest that P. pugnax exoskeleton could be an excellent natural source for the production of chitosan with potential applications in the health system, and to prevent infections associated with pathogens strains.

Solubility and emulsifying properties are important functional properties associated with proteins. However, many plant proteins have lower techno-functional properties, which limit their functional performance in many formulations. Therefore, the objective of this study was to investigate the effect of protein hydrolysis by commercial enzymes to improve their solubility and emulsifying properties. Lupin protein isolate (LPI) was hydrolyzed by 7 commercial proteases using different E/S ratios and hydrolysis times while the solubility and emulsifying properties were evaluated. The results showed that neutral and alkaline proteases are most efficient in hydrolyzing lupin proteins than acidic proteases. Among the proteases, Protamex^® (alkaline protease) showed the highest DH values after 5 h of protein hydrolysis. Meanwhile, protein solubility of LPI hydrolysates was significantly higher (p < 0.05) than untreated LPI at all pH analyzed values. Moreover, the emulsifying capacity (EC) of undigested LPI was lower than most of the hydrolysates, except for acidic proteases, while emulsifying stability (ES) was significantly higher (p < 0.05) than most LPI hydrolysates by acidic proteases, except for LPI hydrolyzed with Acid Stable Protease with an E/S ratio of 0.04. In conclusion, the solubility, and emulsifying properties of lupin (Lupinus luteus) proteins can be improved by enzymatic hydrolysis using commercial enzymes.

In recent years, emulsions stabilized by solid particles (known as Pickering emulsions) have gained considerable attention due to their excellent stability and for being environmentally friendly compared to the emulsions stabilized by synthetic surfactants. In this context, edible Pickering stabilizers from agri-food byproducts have attracted much interest because of their noteworthy benefits, such as easy preparation, excellent biocompatibility, and unique interfacial properties. Consequently, different food-grade particles have been reported in recent publications with distinct raw materials and preparation methods. Moreover, emulsions stabilized by solid particles can be applied in a wide range of industrial fields, such as food, biomedicine, cosmetics, and fine chemical synthesis. Therefore, this review aims to provide a comprehensive overview of Pickering emulsions stabilized by a diverse range of edible solid particles, specifically agri-food byproducts, including legumes, oil seeds, and fruit byproducts. Moreover, this review summarizes some aspects related to the factors that influence the stabilization and physicochemical properties of Pickering emulsions. In addition, the current research trends in applications of edible Pickering emulsions are documented. Consequently, this review will detail the latest progress and new trends in the field of edible Pickering emulsions for readers.