Emerging Camelina Protein: Extraction, Modification, and Structural/Functional Characterization

Camelina sativa, a sustainable oilseed crop, is a novel source of plant protein. The aim of this work was to evaluate two protein extraction approaches, alkaline and salt extraction, and determine their impact on the structural and functional properties of camelina protein. Protein yield, content, structural characteristics, and functional properties of the produced camelina protein concentrates (CPC, 70-80% protein) and camelina protein hydrolysates were assessed and compared to reference proteins, whey protein isolate and soy protein isolate (SPI). Compared to alkaline pH extraction, data showed that salt extraction produces less denatured and more functional CPC, composed mainly of cruciferin and napin proteins. The functionality of the salt-extracted CPC was comparable and sometimes better than that of SPI. Specifically, the solubility (similar to 70%) of the salt-extracted CPC at pH 3.4 was significantly (P < 0.05) higher than that (similar to 50%) of SPI. Additionally, salt-extracted CPC had significantly higher emulsification capacity and foaming capacity than SPI. On the other hand, the gelation property of CPC was inferior to that of SPI, an observation attributed to the molecular size of camelina protein compared to soy protein. Upon hydrolysis of CPC with Aspergillus oryzae protease, a limited benefit to solubility was noted at pH 7 postthermal treatment. Overall, results revealed the potential of camelina as a novel source of functional plant protein that might gain a position in the protein market place, and possibly compete with soy protein for several applications targeting the use of plant proteins.