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