Faba beans are emerging as sustainable quality plant protein sources, with the potential to help meet the growing global demand for more nutritious and healthy foods. The faba bean, in addition to its high protein content and well-balanced amino acid profile, contains bioactive constituents with health-enhancing properties, including bioactive peptides, phenolic compounds, GABA, and L-DOPA. Faba bean peptides released after gastrointestinal digestion have shown antioxidant, antidiabetic, antihypertensive, cholesterol-lowering, and anti-inflammatory effects, indicating a strong potential for this legume crop to be used as a functional food to help face the increasing incidences of non-communicable diseases. This paper provides a comprehensive review of the current body of knowledge on the nutritional and biofunctional qualities of faba beans, with a particular focus on protein-derived bioactive peptides and how they are affected by food processing. It further covers the adverse health effects of faba beans associated with the presence of anti-nutrients and potential allergens, and it outlines research gaps and needs.

Faba beans are a promising emerging plant-based protein source to be used as a quality alternative to peas and soy. In this study, the potential health beneficial activities of three Canadian faba bean varieties (Fabelle, Malik and Snowbird) were investigated after in vitro gastrointestinal digestion and compared to two commonly used legumes (peas and soy). The results revealed that the faba beans had a higher antioxidant activity than peas when assessed with the 2,2-diphenyl-1-picrylhydrazyl (DPPH) and the 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid (ABTS) assays, except for the Fabelle variety. In the oxygen radical absorbance capacity (ORAC) and the iron chelating assays, the faba beans had a lower antioxidant activity than soy. Interestingly, Fabelle and Snowbird showed a higher antioxidant effect than the peas and soy at the cellular level. The antihypertensive properties of Fabelle and Malik varieties were significantly higher than peas but lower than soy. The in vitro antidiabetic activity was higher for soy, but no differences were found at the cellular level. The faba bean peptides were further fractionated and sequenced by mass spectrometry. Eleven peptides with in silico predicted bioactivities were successfully identified in the faba bean digestate and support validating the health-promoting properties of peptides. The results demonstrate the bioactive potential of faba beans as a health-promoting food ingredient against non-communicable diseases.

Glabrous canaryseeds were recently approved for human consumption as a novel cereal grain in Canada and the United States. Previously, canaryseeds were exclusively used as birdseed due to the presence of carcinogenic silica fibers; therefore the nutritional value of the seeds has been seriously overlooked. Two cultivars of glabrous canaryseeds (yellow and brown) were created from the hairy varieties. They are high in protein compared to other cereal grains, and contain high amounts of tryptophan, an amino acid normally lacking in cereals, and are gluten-free. Bioactive peptides of canaryseeds produced by in vitro gastrointestinal digestion have shown antioxidant, antidiabetic, and antihypertensive activity. The seeds contain other constituents with health promoting effects, including unsaturated fatty acids, minerals, and phytochemicals. Anti-nutritional components in the seeds are comparable to other cereal grains. Because of their beneficial health effects, canaryseeds should be regarded as a healthy food and have immense potential as a functional food and ingredient. Further research is required to determine additional bioactive peptide activity and capacity, as well as differences between the yellow and brown cultivars.

Currently, information on the allergens profiles of different mustard varieties is rather scarce. Therefore, the objective of this study was to assess protein profiles and immunoglobulin E (IgE)-binding patterns of selected Canadian mustard varieties. Optimization of a non-denaturing protein extraction from the seeds of selected mustard varieties was first undertaken, and the various extracts were quantitatively and qualitatively analyzed by means of protein recovery determination and protein profiling. The IgE-binding patterns of selected mustard seeds extracts were assessed by immunoblotting using sera from mustard sensitized and allergic individuals. In addition to the known mustard allergens—Sin a 2 (11S globulins), Sin a 1, and Bra j 1 (2S albumins)—the presence of other new IgE-binding protein bands was revealed from both Sinapis alba and Brassica juncea varieties. Mass spectrometry (MS) analysis of the in-gel digested IgE-reactive bands identified the unknown ones as being oleosin, β-glucosidase, enolase, and glutathione-S transferase proteins. A bioinformatic comparison of the amino acid sequence of the new IgE-binding mustard proteins with those of know allergens revealed a number of strong homologies that are highly relevant for potential allergic cross-reactivity. Moreover, it was found that Sin a 1, Bra j 1, and cruciferin polypeptides exhibited a stronger IgE reactivity under non-reducing conditions in comparison to reducing conditions, demonstrating the recognition of conformational epitopes. These results further support the utilization of non-denaturing extraction and analysis conditions, as denaturing conditions may lead to failure in the detection of important immunoreactive epitopes.