No abstract

Lupin meal presents great potential as an alternative plant-based source of proteins for human nutrition. In the present work, different conditions of extraction and purification were evaluated for production of lupin protein isolates. The results showed that the protein extraction yield was comparable at acidic and conventionally used alkaline extraction pH (37% vs. 40–45%, respectively). Proteins extracted were principally composed of globulins. The ionic strength negatively impacted the protein extractability at pH 2, whereas no significant differences were observed between extractions at 20 to 50 °C. The selected extraction conditions (pH 2 and 7) combined with purification by isoelectric precipitation or ultrafiltration process generated the isolate-grade products. Interestingly, further characterization revealed a partial denaturation of proteins extracted at pH 2 resulting in loss of protein solubility at pH 6 and 7 (10–50%), modifications in secondary structure, lower thermal stability, and formation of protein aggregates. However, foaming and emulsifying properties were generally similar for almost all lupin isolates. Further investigation might be of interest with regard to the extraction behaviours and structural and functional properties of specific lupin protein fractions.

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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.