Adhesion properties of camelina protein fractions isolated with different methods

• Albumin, glutelin, and globulin were isolated from camelina meal.
• The globulin fraction showed better adhesion performance than glutelin.
• The glutelin fraction had higher protein aggregation than globulin, as indicated by higher crystallinity, higher thermal stability, and dense protein aggregate.
• The compact structure of glutelin contributed to lower adhesion strength than globulin.

The objective of this research was to investigate the effects of protein extraction methods on the adhesion performance of different camelina protein fractions. Physicochemical properties were also studied, including the electrophoresis profile; rheological, thermal, and morphological properties; and crystallization. Two camelina protein fractions, globulin and glutelins, were isolated from defatted camelina meal using three different methods resulting in total of six protein fractions including globulin 0–2 and glutelin 0–2. Dry adhesion strength of camelina protein adhesives exhibited nearly 100% wood cohesive failure at the curing temperatures of 150–190 °C, except glutelin 2 and globulin 0. The overall adhesion performance of globulin fraction behaved better than glutelin fraction. The greatest wet shear strength of globulin 1 and 2 was around 3.3 MPa, curing at 190 °C. The wet shear strength of glutelin 2 was inferior to glutelin 1 due to the negative effects of NaCl. Glutelin had higher protein aggregation than globulin, as indicated by higher crystallinity, higher thermal stability, and dense protein aggregation. The compact structure of glutelins may partially contribute to their lower adhesion strength.