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Isolation and Characterization of Protein Fractions Isolated from Camelina Meal

Published by the American Society of Agricultural and Biological Engineers, St. Joseph, Michigan

Citation:  Transactions of the ASABE. 57(1): 169-178. (doi: 10.13031/trans.57.10455) @2014
Authors:   Ningbo Li, Guangyan Qi, Xiuzhi Susan Sun, Donghai Wang, Scott Bean, Deidre Blackwell
Keywords:   Albumin, Amino acid profiles, Camelina protein, FTIR, Globulin, Glutelin, Molecular weight, SEC, TEM, TGA.

Camelina is a new oil crop in North America. Camelina meal, a by-product of the camelina oil extraction process, typically contains 10% to 15% residual oil and 40% crude protein. As camelina oil demand increases, utilization of camelina protein for value-added products is critical to food and biotechnology industries; however, few studies have been conducted on camelina proteins. In this study, camelina protein fractions (albumin, globulins, and glutelins) were isolated from camelina meal based on their solubility using three different sequences: method 0 (S0), method 1 (S1), and method 2 (S2). The proteins’ physicochemical properties, including solubility, amino acid profiles, molecular weight, and thermal and morphological properties, were also characterized. Results showed that S1 harvested more protein (88.20%) than S0 (84.05%) and S2 (76.52%). Glutelin was the major fraction (64.64%) in camelina, followed by globulin (17.67%), and albumin (10.54%). Essential amino acids accounted for approximately 40% of the total amino acids in camelina protein. High molecular weight aggregates stabilized by covalent bonds in the glutelin and albumin fractions, as shown in size-exclusion chromatography (SEC), are closely related to larger-size protein aggregates observed in TEM images.

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