Pulse proteins (PP) are gaining popularity as compared to animal proteins due to perceived sustainably, allergen-free, gluten-free, low cost and increasing vegan population. The post-translational processing and variations in agronomic as well as environmental factors caused variations in physicochemical and functional properties of PP. These proteins have lower digestibility that can be improved by hydrolyzing into peptides and amino acids. Though absorption and utilization of hydrolyzed protein products in the presence of anti-nutritional factors is reduced and mechanism is unrevealed. The amount of these factors can be reduced or eliminated by altering their biosynthesis pathways and adopting appropriate processing methods. Germination and fermentation of pulses reduce the content of antinutritional factors leading to improved protein digestibility. Emulsification properties of protein depend on the distinct amino acid order and composition as well as surface hydrophobicity. Efforts are also being made to improve functional properties such as emulsification, solubility etc. by forming Maillard conjugates. Undesirable beany odor in the pulses also restricts their applications in food products. The reduction in beany odor by fermenting pulses using appropriate microbial consortia has been suggested. Aquafaba, a viscous liquid from cooked pulses has potential to develop vegan products.
The value of pulse grain has been drastically increased by manufacturing it to pulse storage protein isolates. The utilization of pulse proteins is highly dependent on the composition, functional and structural properties. Therefore, the current study was conducted to investigated the structural and functional attributes, as well as the aroma profile of major fractions of pulse storage proteins isolated from green pea and chickpea including globulin, legumin, and vicilin. Alkaline extraction-isoelectric precipitation in conjunction with a modified salt dissolution-precipitation method was developed to produce abovementioned protein fractions in a large scale. Results showed that purity of globulin, legumin and vicilin fractions reached more than 90%, 80%, and 90%, respectively. Regarding the functionality of protein fractions, protein compositions had significant impacts on the structural and functional properties of proteins. In general, vicilin fractions had higher solubility, and foaming and emulsification properties but lower thermal properties compared to legumin fractions because of its lower molecular weight, less rigid conformational structure, and lower disulfide bond content. However, aromatic compound profile of protein fractions was strongly affected by pulse types as both lipid and lipoxygenase contents varied depending on the type of pulses. Overall, chickpea protein fractions contained higher typical beany aromatic compounds (e.g., 1-pentanol, 1-ocetn-3-ol, and hexanal) than green pea protein fractions. These results can greatly extend the knowledge for better understanding the structural and functional properties of pulse proteins.
Source: NarpinderSinghParmeetKaurMehakKatyal “Challenges and Strategies for Utilization of Pulse Proteins” sciencedirect.com/science/article/pii/B9780128239605000159