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Faba bean is an ancient legume that is regaining interest due to its environmental and nutritional benefits. Very little is known on the protein quality of the new faba bean varieties. In this study, the digestibility and the Digestible Indispensable Amino Acid Score (DIAAS) of the protein quality of three Canadian faba bean varieties (Fabelle, Malik and Snowbird) were compared to pea and soy using the harmonized in vitro digestion procedure developed by the International Network of Excellence on the Fate of Food in the Gastrointestinal Tract (INFOGEST). The impact of boiling on the nutritional quality of faba bean flours was also ascertained. Protein content in faba bean (28.7-32.5%) was lower than defatted soy (56.6%) but higher than pea (24.2%). Total phenolics and phytate content were higher (p < 0.05) in faba bean (2.1-2.4 mg/g and 11.5-16.4 mg/g respectively) and soy (2.4 mg/g and 19.8 mg/g respectively) comparatively to pea (1.3 mg/g and 8.9 mg/g). Trypsin inhibitor activity was significantly higher (p < 0.05) in soy (15.4 mg/g) comparatively to pea (0.7 mg/g) and faba bean (0.8-1.1 mg/g). The digestibility of free amino acids of raw faba bean flours ranged from 31 to 39% while the digestibility of total amino acids ranged from 38 to 39%. The in vitro Digestible Indispensable Amino Acid Score (IV-DIAAS) of raw faba bean flours ranged from 13 to 16 (when calculated based on free amino acid digestibility) to 32-38 (when calculated based on total amino acid digestibility) and was in a similar range to pea (13-31) and soy (11-40). Boiling modified the protein electrophoretic profile and decreased trypsin inhibitor activity (30-86% reduction), while total phenolics and phytate content were unaffected. The IV-DIAAS significantly decreased in all boiled legumes, possibly due to an increased protein aggregation leading into a lower protein digestibility (18-32% reduction). After boiling, the nutritional quality of faba bean was significantly lower (p < 0.05) than soy, but higher than pea. Our results demonstrate that faba bean has a comparable protein quality than other legumes and could be used in similar food applications., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Crown Copyright © 2023. Published by Elsevier Ltd. All rights reserved.)

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 canary seed (Phalaris canariensis L.) is a novel true cereal grain produced primarily in Western Canada which has been approved for human consumption by the U.S. Food and Drug Administration and Health Canada in 2016. Due to its high protein content (22%), this new edible grain is emerging as an alternative source of plant proteins. In the present work, protein extractability from four novel glabrous (2 yellow and 2 brown) canary seeds varieties was improved based on the selection of optimal pH of protein solubilisation and precipitation. Solubilisation at pH 12 followed by acid precipitation at pH 5 were retained as optimal conditions. Scale up of the protein optimized wet fractionation process resulted in highly purified canary seed protein isolates (purity of 91 to 93%) with protein recovery yield of 65 to 69%. In parallel, for the others canary seed components, a good recovery yields were obtained for the oil fraction (6.1-6.7 g/100 g flour), starch fraction (48.1-54 g/100 g flour), and crude fiber fraction (15.1-19.7 g/100 g flour). The study of the functional properties of the obtained canary protein isolates revealed, higher solubility at acidic than alkaline region; enhanced fat and water holding capacities and notably higher foaming and emulsifying capacities than control soy protein isolate. With growing global demand for protein, glabrous canary seed has high potential in the food industry, particularly as a good source of functional gluten free cereal proteins., (Copyright © 2020. Published by Elsevier Ltd.)

Peanut allergic individuals can be both co-sensitized and co-allergic to peanut and tree nuts. At the moment, standard diagnostic approaches do not always allow differentiation between clinically relevant sensitization and nonsignificant cross-reactions, and the responsibility of each allergen remains unclear. The objective of this study was therefore to determine a peanut sensitization profile in a cohort of Canadian peanut allergic children and assess the immunoglobulin E (IgE) molecular cross-reactivity between peanut, almond, hazelnut and pistachio. The specific IgE (sIgE) levels of each patient serum were determined by ImmunoCAP, indirect ELISA and immunoblot to examine their sIgE-binding levels and profiles to peanut proteins. Reciprocal inhibition ELISA and immunoblotting were used to study sIgE cross-reactions between peanut and the selected tree nuts using an adjusted and representative serum pool of the nine allergic patients. The results showed that the prepared peanut and tree nut protein extracts allowed for the detection of the majority of peanut and selected tree nut known allergens. The reciprocal inhibition ELISA experiments showed limited sIgE cross-reactivities between peanut and the studied tree nuts, with peanut being most likely the sensitizing allergen and tree nuts the cross-reactive ones. In the case of hazelnut and pistachio, a coexisting primary sensitization to hazelnut and pistachio was also demonstrated in the serum pool. Reciprocal inhibition immunoblotting further revealed that storage proteins (2S albumin, 7S vicilin and 11S legumin) could possibly account for the observed IgE-cross-reactions between peanut and the studied tree nuts in this cohort of allergic individuals. It also demonstrated the importance of conformational epitopes in the exhibited cross-reactions.

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., Competing Interests: The authors declare no conflict of interest.