Li, NingboQi, GuangyanSun, Xiuzhi S.Wang, DonghaiBean, Scott R.Blackwell, Deidre2014-06-172014-06-172014-07-01http://hdl.handle.net/2097/17862Camelina 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.en-USThis Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s).AlbuminAmino acid profilesCamelina proteinFTIRGlobulinGlutelinMolecular weightSECTEMTGAArticle (publisher version)