2025 AOCS Annual Meeting & Expo.
Protein and Co-Products
Karandeep Singh Sodhi
Masters student
University of Saskatchewan
Saskatoon, Saskatchewan, Canada
Supratim Ghosh, PhD (he/him/his)
Professor
University of Saskatchewan
Saskatoon, Saskatchewan, Canada
Jianping Wu
Professor
University of Alberta, Canada
ajay dalai
professor
University of Saskatchewan
saskatoon, Saskatchewan, Canada
This study aimed to valorize desolventized toasted canola meal using sub-critical water extraction, to recover functional hydrolyzed proteins with optimal interfacial tension (IFT), degree of hydrolysis (DH) and emulsion stabilization property. A central composite design was used to optimize extraction conditions of temperature (200–250°C), time (20–30 min), and feed concentration (5–20%) at 4.03 MPa. The extracted proteins displayed an IFT ranging from 11.6 mN/m to a minimum of 4.0 mN/m, while the DH varied from 2.3% to 14.1%. Based on the DH, two sets of extracts containing hydrolyzed proteins were chosen for emulsion development: set-1 with a low DH (2-5%) and set-2 with a high DH (9-15%). Both sets of emulsions destabilized over 1-week storage, with a significant increase in droplet size and cream layer separation, due to the inability of the hydrolyzed proteins to remain at the droplet interface and form a stable, elastic interface to resist droplet coalescence. Therefore, the most unstable emulsion (T225-t25-FC12.5) with the largest increase in droplet size was selected for bilayer formation around the oil droplets by adding chitosan at different pH (2-7) values. The bilayer improved emulsion stability by creating a more elastic interface. Bilayer emulsions at pH 2, 4, 5, and 6 retained droplet sizes (0.56–0.65 µm) over 4 weeks and displayed no visual creaming, in contrast to the primary emulsion showing extensive coalescence, with droplet size increasing from 0.59 to 2.09 µm. The bilayer emulsions also displayed a high positive zeta potential ranging from 56.7 mV to 32.17 mV. However, emulsion at pH 7, with low zeta potential (15.3 mV) displayed a rapid destabilization. Overall, this research provides valuable insights into stabilizing the hydrolyzed protein-stabilized emulsions using a bilayer formation approach by creating a more elastic interface, which can stabilize the emulsions against coalescence.