Polypeptide composition of major oilseed proteins and functional properties of extracted protein products: A concise review

Oilseeds are grown mainly for their oil content but the residues (meals) that remain after defatting are excellent sources of plant protein ingredients. However, to serve as useful ingredients, the extracted proteins must meet industry expectations in terms of functional performance. Protein functionality is influenced by structural conformation, amino acid composition, type of polypeptides, presence of non-protein materials (carbohydrates, lipids, and polyphenols), which in turn can be modified by the extraction method. Defatted oilseed meals are extracted mostly through the pH shift method, which involves alkaline solubilization followed by acid-induced protein precipitation at the isoelectric point. A less popular method is called the protein micellar mass whereby the oilseed meal proteins are extracted with a NaCl solution, which is later diluted to reduce the ionic strength to a level where the proteins are no longer soluble and hence precipitate. A third method utilizes carbohydrases and phytases to first digest non-protein materials from the oilseed meal into smaller units that are then removed by membrane ultrafiltration to leave behind a protein-rich extract. These methods produce mainly two types of isolated oilseed proteins, concentrates (60%-89% protein content) and isolates (& GE;90% protein content), which can differ in terms of their protein conformation, solubility, and functionality as food ingredients. Therefore, this review provides an overview of the extraction and isolation as well as structural and functional properties of soybean, peanut, canola, hemp seed, sunflower, and sesame seed proteins.