CONCLUSIONS
Microstructural features of camelina seeds confirmed the organization of oil bodies and protein-rich areas (storage vacuoles) in cotyledon cells as being typical of crucifer oilseeds, implying that similar oil extraction and meal co-product processing approaches are applicable. Seed coat mucilage, which is an impediment to recovering proteins from oil-free meal, can be removed/reduced using seed pre-treatments, such as treatment with polysaccharide-degrading enzymes. Several isoforms of both cruciferin and napin comprise the primary SSPs, while minor proteins, such as vicilins, OBPs and LEA proteins, make up the remainder of the meal protein. The OBPs are primarily of oleosins, but other types occur. Camelina cruciferin and napin exhibit structural characteristics and pH and temperature stabilities that correspond to those of proteins from B. napus . The composition and properties of camelina seed protein indicate its value as a plant-derived protein with somewhat unique characteristics compared to other plant proteins. This study shows that camelina SSPs have close similarity to Brassica napus(canola/rapeseed) proteins with some subtle differences