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Canola is the second-largest cultivated oilseed crop in the world and produces meal consisting of about 35–40% proteins. Despite this, less than 1% of the global plant-based protein market is taken up by canola protein. The reason behind such underutilization of canola protein and its rapeseed counterpart could be the harsh conditions of the industrial oil extraction process, the dark colour of the meal, the presence of various antinutrients, the variability in the protein composition based on the source, and the different properties of the two major protein components. Although academic research has shown immense potential for the use of canola protein and its rapeseed counterpart in emulsion development and stabilization, there is still a vast knowledge gap in efficiently utilizing canola proteins as an effective emulsifier in the development of various emulsion-based foods and beverages. In this context, this review paper summarizes the last 15 years of research on canola and rapeseed proteins as food emulsifiers. It discusses the protein extraction methods, modifications made to improve emulsification, emulsion composition, preparation protocols, and emulsion stability results. The need for further improvement in the scope of the research and reducing the knowledge gap is also highlighted, which could be useful for the food industry to rationally select canola proteins and optimize the processing parameters to obtain products with desirable attributes. [ABSTRACT FROM AUTHOR]

Globally, there is an increasing demand for sources of plant‐based protein. While Brassica napus L. is an important oilseed crop worldwide, there is also interest in improving its ability to serve as a valuable source of plant‐based protein. Cruciferin, a seed storage protein that makes up 60% of the protein found in mature seeds of B. napus, is of interest for human consumption as a source of protein and as an ingredient in food products due to its functional properties. Existing methods for quantification of cruciferin protein are often time consuming and destroy the seed. This study explored the potential for the measurement of cruciferin protein content in whole seeds of B. napus by near‐infrared spectroscopy (NIRS), to allow for efficient and non‐destructive screening of breeding material. An enzyme‐linked immunosorbent assay (ELISA)‐based reference method was utilized to assess cruciferin content in a diverse population of B. napus. Scanning of whole seed samples produced spectra that were used to develop NIRS calibration equations. Statistical analysis of the calibration results indicated that the NIRS equations developed are poorly suited for prediction of cruciferin content. [ABSTRACT FROM AUTHOR]

The objective of this work was to assess the potential of Cruciferin/Calcium (Cru/Ca) and Cruciferin/Chitosan (Cru/Cs) nanoparticles for oral drug delivery. For this purpose, Cru/Ca and Cru/Cs nanoparticles were developed through cold gelation of Cruciferin, a major canola protein, and in interaction with calcium and chitosan, respectively. The extent and rate of particle uptake in Caco-2 cells and Caco-2/HT29 co-culture was then evaluated by fluorescence spectroscopy as well as flow cytometry. Through pre-incubation of Caco-2 cell monolayer with specific endocytosis inhibitors, the mechanism of cell uptake was investigated. Our results showed that the uptake of negatively-charged Cru/Ca particles to be ∼3 times higher than positively-charged Cru/Cs ones by Caco-2 cells. Presence of mucus secreted by HT29 cells in their co-culture with Caco-2 had negligible influence on the uptake and transport of both particles. In contrast to Cru/Ca particles which were dissociated in the simulated gastrointestinal conditions, digestion of Cru/Cs particles resulted in 6- and 2-fold increase in the cellular uptake and transport of encapsulated coumarin in the latter particles, respectively. While the presence of mucus in Caco-2/HT29 co-culture caused 40–50% decrease of cellular uptake and transport for coumarin encapsulated in digested Cru/Cs particles, it had no significant effect on the cell uptake and transport of coumarin associated with Cru/Ca particles after digestion. Energy-dependent mechanisms were the dominant mechanism for uptake of both undigested and digested particles. Therefore, in Caco-2/HT29 co-culture which closely simulated intestinal epithelial cells, undigested Cru/Ca and Cru/Cs particles had the ability to penetrate mucus layers, while digested Cru/Cs particles showed mucoadhesive property, and digested Cru/Ca particles were dissociated. Our results points to a potential for cruciferin based nanoparticles for oral drug delivery. Statement of Significance The long-term objective of this research is to investigate the potential of edible and safe biopolymer in enhanced oral delivery of drugs and/or vaccines. Here, we investigated the potential application of nanoparticles based on a protein extracted from Canola seeds, i.e., cruciferin, for oral delivery of a model small molecule, i.e., coumarin, through cells representing gastrointestinal epithelium, Caco-2 and Caco-2/HT29 cell monolayer. This study was completed for intact cruciferin nanoparticles and cruciferin coated chitosan nanoparticles, before and after digestion with gastric or intestine simulating fluids. This comparison was useful to understand the fate the cruciferin based particles in digestive mucosal tissues and their potential mucoadhesive and/or mucus-penetrating property. [ABSTRACT FROM AUTHOR]

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.

Canola proteins are known to have great potential for use in food and non-food applications due to their nutritional, biological and functional properties. However, canola protein extraction remains a challenge, due mainly to the complexity of canola proteins and the presence a variety of undesirable compounds. An integrated method, including acidic washing (pH 4), alkaline extraction (pH 12.5), isoelectric precipitation (pH 4), and ultrafiltration, was proposed to isolate two main canola proteins: cruciferin and napin. The protein content and yield of cruciferin and napin were 91 g/100 g and 38.6%, 82 g/100 g and 12.5%, respectively. The contents of phytic acid and phenolics were 1.5 g/100 g and 1.8 g/100 g, and 0.9 g/100 g and 0.6 g/100 g, respectively, for cruciferin and napin. The emulsifying and foaming properties of cruciferin and napin were favorably comparable to previous results. The development of a simple and scalable method of canola protein isolation will facilitate further research on their food and non-food applications. [ABSTRACT FROM AUTHOR]

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 CaCl salts in the medium. The effect of CaCl 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. [ABSTRACT FROM AUTHOR]

Among the commercially cultivated Brassicaceae (Cruciferae) plants, Brassica juncea, Brassica napus, Brassica rapa, and Sinapis alba store significant amounts of oil and protein in the seed. At present, Brassica seed proteins are primarily used for livestock feeding based on the nutritional value. The point of curiosity is whether the present knowledge on the protein structure, biochemical characteristics, nutritive value, and the recovery processes are inadequate to develop Brassica proteins into a usable plant protein source or these proteins are of substandard for uses beyond animal nutrition applications. Cruciferin (11S) and napin (2S) are the predominant storage proteins of Brassicaceae seeds that contribute to different properties and functions. A gamut of information is available on the chemistry, nutritional value, as well as the functionality in foods, and associated non-protein components of canola/rapeseed storage proteins. The intention of this article is to critically review what is known about the predominant storage proteins of commercially produced Brassicaceae seeds relative to the above aspects and identify the knowledge gaps. [ABSTRACT FROM AUTHOR]

Canola is an economically important farm-gate crop in Canada. To further explore the potential of canola protein as value-added food and nutraceutical ingredients, a better understanding of fundamental properties of 2 major canola proteins is necessary. Two major protein components, cruciferin and napin, were isolated from defatted canola meal by Sephacryl S-300 gel filtration chromatography. SDS-PAGE showed that cruciferin consists of more than 10 polypeptides, and noncovalent links are more important than disulphide bonds in stabilizing the structural conformation. Napin consists of 2 polypeptides and is stabilized primarily by disulphide bonds. Purified cruciferin showed 1 major endothermic peak at 91 °C compared with that of 110 °C for napin. Emulsion prepared by cruciferin showed significant higher specific surface area and lower particle size than that of napin. The study indicated that the presence of napin could detrimentally affect the emulsion stability of canola protein isolates. Hydrolysates from cruciferin and napin showed potent angiotensin I-converting enzyme inhibitory activity (IC50: 0.035 and 0.029 mg/mL, respectively), but weaker than that of canola protein isolate hydrolysate (IC50: 0.015 mg/mL). [ABSTRACT FROM AUTHOR]