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Protein rich meal is a valuable co-product of canola/rapeseed oil extraction. Seed storage proteins that include cruciferin (11S) and napin (2S) dominate the protein complement of canola while oleosins, lipid transfer proteins and other minor proteins of non-storage nature are also found. Although oil-free canola meal contains 36–40% protein on a dry weight basis, non-protein components including fibre, polymeric phenolics, phytates and sinapine, etc. of the seed coat and cellular components make protein less suitable for food use. Separation of canola protein from non-protein components is a technical challenge but necessary to obtain full nutritional and functional potential of protein. Process conditions of raw material and protein preparation are critical of nutritional and functional value of the final protein product. The storage proteins of canola can satisfy many nutritional and functional requirements for food applications. Protein macromolecules of canola also provide functionalities required in applications beyond edible uses; there exists substantial potential as a source of plant protein and a renewable biopolymer. Available information at present is mostly based on the protein products that can be obtained as mixtures of storage protein types and other chemical constituents of the seed; therefore, full potential of canola storage proteins is yet to be revealed.

At present, canola meal is primarily streamlined into the animal feed market where it is a competitive animal feed source owing to its high protein value. Beyond animal feed lies a potential game-changer with regards to the value of canola meal, and its opportunity as a high quality food protein source. An economic and sustainable source of protein with high bioavailability and digestibility is essential to human health and well-being. Population pressures, ecological considerations, and production efficiency underscore the importance of highly bioavailable plant proteins, both for the developed and developing world. Despite decades of research, several technologies being developed, and products being brought to large scale production, there are still no commercially available canola protein products. The workshop entitled “Canola/Rapeseed Protein—Future Opportunities and Directions” that was held on 8 July 2015 during the 14th International Rapeseed Congress (IRC 2015) addressed the current situation and issues surrounding canola meal protein from the technological, nutritional, regulatory and genomics/breeding perspective. Discussions with participants and experts in the field helped to identify economic barriers and research gaps that need to be addressed in both the short and long term for the benefit of canola industry.

The two major storage proteins identified in Brassica napus (canola) were isolated and studied for their molecular composition, structural characteristics and the responses of structural features to the changes in pH and temperature. Cruciferin, a complex of six monomers, has a predominantly β-sheet-containing secondary structure. This protein showed low pH unstable tertiary structure, and distinctly different solubility behaviour with pH when intact in the seed cellular matrix. Cruciferin structure unfolds at pH 3 even at ambient temperature. Temperature-induced structure unfolding was observed above the maximum denaturation temperature of cruciferin. Napin was soluble in a wider pH range than cruciferin and has α-helices dominating secondary structure. Structural features of napin showed less sensitivity to the changes in medium pH and temperature. The surface hydrophobicity (S0) and intrinsic fluorescence of tryptophan residue appear to be good indicators of cruciferin unfolding, however they were not the best to demonstrate structural changes of napin. These two storage proteins of B. napus have distinct molecular characteristics, therefore properties and functionalities they provide are contrasting rather than complementary.

In the last decade, various foods have been reformulated with plant protein ingredients to enhance plant-based food intake in our diet. Pulses are in the forefront as protein-rich sources to aid in providing sufficient daily protein intake and may be used as binders to reduce meat protein in product formulations. Pulses are seen as clean-label ingredients that bring benefits to meat products beyond protein content. Pulse flours may need pre-treatments because their endogenous bioactive components may not always be beneficial to meat products. Infrared (IR) treatment is a highly energy-efficient and environmentally friendly method of heating foods, creating diversity in plant-based ingredient functionality. This review discusses using IR-heating technology to modify the properties of pulses and their usefulness in comminuted meat products, with a major emphasis on lentils. IR heating enhances liquid-binding and emulsifying properties, inactivates oxidative enzymes, reduces antinutritional factors, and protects antioxidative properties of pulses. Meat products benefit from IR-treated pulse ingredients, showing improvements in product yields, oxidative stability, and nutrient availability while maintaining desired texture. IR-treated lentil-based ingredients, in particular, also enhance the raw color stability of beef burgers. Therefore, developing pulse-enriched meat products will be a viable approach toward the sustainable production of meat products.

Synchrotron radiation (SR) provides a wide spectrum of bright light that can be tailored to test myriad research questions. SR provides avenues to illuminate structure and composition across scales, making it ideally suited to the study of plants and seeds. Here, we present an array of methodologies and the data outputs available at a light source facility. Datasets feature seed and grain from a range of crop species including sp. (watermelon), sp. (canola), (pea), and (wheat), to demonstrate the power of SR for advancing plant science. The application of SR micro-computed tomography (SR-µCT) imaging revealed internal seed microstructures and their three-dimensional morphologies in exquisite detail, without the need for destructive sectioning. Spectroscopy in the infrared spectrum probed sample biochemistry, detailing the spatial distribution of seed macronutrients such as lipid, protein and carbohydrate in the embryo, endosperm and seed coat. Methods using synchrotron X-rays, including X-ray absorption spectroscopy (XAS) and X-ray fluorescence (XRF) imaging revealed elemental distributions, to spatially map micronutrients in seed subcompartments and to determine their speciation. Synchrotron spectromicroscopy (SM) allowed chemical composition to be resolved at the nano-scale level. Diverse crop seed datasets showcase the range of structural and chemical insights provided by five beamlines at the Canadian Light Source, and the potential for synchrotron imaging for informing plant and agricultural research.

Seeds of six commercially produced Brassica juncea, Brassica napus and Sinapis alba varieties representing high-glucosinolate condiment-type and low-glucosinolate canola-type were studied for solubility characteristics of the predominant seed storage proteins (SSPs). The non-protein nitrogen components such as glucosinolates, nucleic acids, betaine, choline and sinapine contributed 3.1–5.2% and 7.9–10.8% for the total N content of low- and high-glucosinolate meals, respectively. The cruciferin and napin which are the predominant SSPs of crucifers were purified from these seeds and used to confirm soluble protein types under the conditions provided. The napins were soluble between pH 2 and 4 but not the cruciferins. Strong alkaline pH brought both cruciferin and napin into solution. In general, the SSP solubility was increased due to the presence of NaCl or CaCl2 salts in the medium. The effect of CaCl2 on solubility was more positive than NaCl for all the seed types except S. alba at neutral and alkaline pH. Presence of salts indeed reduced solubility of S. alba SSPs at alkaline pH. The medium pH and salt ions and their ionic strength can be manipulated to achieve selective solubility of napin and cruciferin of Brassicaceae seed meals.

Indigenous and traditional foods of Sri Lanka inherit a long history and unique traditions continued from several thousands of years. Sri Lankan food tradition is strongly inter-wound with the nutritional, health-related, and therapeutic reasoning of the food ingredients and the methods of preparation. The diverse culinary traditions and preparations reflect multipurpose objectives combining in-depth knowledge of flora and fauna in relation to human well-being and therapeutic health benefits. Trans-generational knowledge dissemination related to indigenous and traditional food is now limited due to changing lifestyles, dwindling number of knowledge holders, and shrinking floral and faunal resources. Awareness on the relationship between non-communicable diseases and the diet has garnered the focus on traditional ingredients and foods by the consumers and major food producers in Sri Lanka. This review presents concise details on the indigenous and traditional foods of Sri Lanka, with scientific analysis when possible.