Profiling and characterization of Camelina sativa (L.) Crantz meal proteins. (5th August 2022)

• Record Type: Journal Article
• Authors: Perera, Suneru P.; McIntosh, Tara; Coutu, Cathy; Tyler, Robert T.; Hegedus, Dwayne D.; Wanasundara, Janitha P. D.
• Is Part Of: Journal of the American Oil Chemists' Society. Volume 99:Number 10(2022)
• Page Start: 873
• Page End: 889
• Publication Date: 2022-08-05
• Subjects: Camelina sativa -- cruciferin -- meal -- napin -- oil body protein; Oils and fats -- Periodicals; Soap -- Periodicals; Fats -- Periodicals; Food-Processing Industry -- Periodicals; Acides gras -- Périodiques; Aliments -- Industrie et commerce -- Périodiques; Huiles et graisses -- Périodiques; Savon -- Périodiques; Oliën; Chemie; Oils and fats; Soap; Periodicals; 547.77
• DOI: 10.1002/aocs.12634
• Languages: English
• ISSNs: 0003-021X

Abstract

Abstract: Protein from camelina seed is a valuable co‐product that can be derived from the meal remaining after oil extraction. The current study describes the types and physicochemical properties of the major proteins present in camelina meal. Seed coat mucilage, which interferes with protein extraction, was removed from whole seeds by digestion with Viscozyme® and lipids were removed with hexane to obtain demucilaged/defatted meal. Protein comprised 51.3% of meal dry matter and the eight essential amino acids comprised 40.8% of total amino acids. The meal polypeptide profile showed bands originating from cruciferin (~44.1 and 51.7 kDa), napin (~14 kDa) and oil body proteins (OBP; ~15–20 kDa) resembling that of other crucifers. Cruciferins (11 isoforms) were the predominant proteins, while vicilins (6 isoforms) also were identified among the proteins soluble at pH 8.5. Among the proteins soluble at pH 3, napins (5 isoforms) comprised the majority, though late embryogenesis abundant proteins also were found. Camelina cruciferin and napin were confirmed to possess predominantly β‐sheet and α‐helix secondary structures, respectively. Camelina cruciferin structure was highly sensitive to changes in pH of the medium and underwent acid‐induced denaturation at pH 3, but exhibited high thermal stability (>80°C) at neutral and alkaline pHs. The structure of camelina napins was less sensitive to pH. The major proteins associated with oil bodies were oleosins (6 isoforms). Identification and characterization of the properties of camelina meal proteins will enable strategic paths for co‐product valorization such as developing plant protein ingredients.