No abstract

Currently, the predominant process for soy protein concentrate (SPC) production is aqueous ethanol washing of hexane-extracted soy meal. However, the use of hexane is less desired, which explains the increased interest in cold pressing for oil removal. In this study, cold-pressed soy meal was used as the starting material, and a range of water/ethanol ratios was applied for the washing process to produce SPCs. Washing enriched the protein content for the SPCs, regardless of the solvent used. However, we conclude that washing with water (0% ethanol) or solvents with a high water/ethanol ratio (60% and above) can be more advantageous. Washing with a high water/ethanol ratio resulted in the highest yield, and SPCs with the highest protein solubility and water holding capacity. The water-only washed SPC showed the highest viscosity, and formed gels with the highest gel strength and hardness among all the SPCs at a similar protein concentration. The variations in the functionality among the SPCs were attributed to protein changes, although the effects of non-protein constituents such as sugar and oil might also be important. Overall, the aqueous ethanol washing process combined with cold-pressed soy meal created SPCs comparable to commercial SPC in terms of composition, but with varied functionalities that are relevant for novel soy-food developments.

No abstract

Exploitation of plant proteins as an alternative to animal proteins currently presents an important challenge for food industries. In this contribution, total sunflower protein isolate from cold press meal was used as a starting material for the generation of highly soluble and functional hydrolysates that could be used in various food formulations. To do this, a rational and complete approach of controlled hydrolysis was implemented using the individual Alcalase and Prolyve enzymes. The method of stopping the hydrolysis reaction was also evaluated. The influence of operating conditions on hydrolysis kinetics and enzymatic mechanism was studied to identify the appropriate hydrolysis conditions. The gain of the solubility was then analyzed and compared to that of the initial proteins. Finally, the emulsifying and foaming properties (capacities and stabilities) of the resulting hydrolysates were also assessed. As a result, controlled enzymatic proteolysis significantly improved the sunflower protein solubility at neutral pH (twofold increase) and generated highly soluble hydrolysates. The limited proteolysis also maintained the good foam capacities and allowed an improvement in the initial foam stabilities and emulsifying capacities and stabilities of sunflower proteins. This contribution can greatly increase the value of sunflower meal and help in the development of sunflower protein products in the future.