Skip to main content
ARS Home » Plains Area » Fargo, North Dakota » Edward T. Schafer Agricultural Research Center » Small Grain and Food Crops Quality Research » Research » Publications at this Location » Publication #385419
Research Project: Identification and Characterization of Quality Parameters for Enhancement of Marketability of Hard Spring Wheat, Durum, and Oat

Location: Small Grain and Food Crops Quality Research

Title: Plant proteins from green pea and chickpea: Extraction, fractionation, structural characterization, and functional properties

Author
item CHANG, LIUYI - North Dakota State University
item LAN, YANG - North Dakota State University
item BANDILLO, NONOY - North Dakota State University
item Ohm, Jae-Bom
item CHEN, BINGCAN - North Dakota State University
item RAO, JIAJIA - North Dakota State University

Submitted to: Food Hydrocolloids
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 8/29/2021
Publication Date: 9/1/2021
Citation: Chang, L., Lan, Y., Bandillo, N., Ohm, J., Chen, B., Rao, J. 2022. Plant proteins from green pea and chickpea: Extraction, fractionation, structural characterization, and functional properties. Food Hydrocolloids. 123. Article 107165. https://doi.org/10.1016/j.foodhyd.2021.107165.
DOI: https://doi.org/10.1016/j.foodhyd.2021.107165

Interpretive Summary: The utilization of plant proteins from pulse grains is on the rise because of their high nutritional properties and the competitive price in the food sector. However, there have only been a few systematic studies on structural and functional characteristics of protein fractions in different pulse grains. Therefore, this research studied the structural and functional attributes, as well as the aroma profile of major protein fractions extracted from green pea and chickpea grains. A large-scale procedure was established to extract protein fractions from green pea and chickpea grains. Results showed that the new procedure improved purity of protein fractions. We also found that the extracted protein fractions were significantly different in important protein composition, structure, and functional properties. Green pea and chickpea were significantly different in aromatic profile of protein fractions. Overall, chickpea protein fractions contained higher typical off-flavor aromatic compounds than green pea protein fractions. These findings will be useful information to pulse ingredient manufacturers to formulate appropriate pulse protein products with premium characteristics.

Technical Abstract: Currently, there is a lack of systematic study on structural and functional relationship among protein fractions from different pulse resources. As such, we researched the structural and functional attributes, as well as the aroma profiles of major fractions of pulse storage proteins from green pea and chickpea including globulin, legumin, and vicilin fractions. 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.