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Profiling and characterization of Camelina sativa (L.) Crantz meal proteins
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  • Janitha Wanasundara,
  • Tara McIntosh,
  • Dwayne Hegedus,
  • Suneru Perera,
  • Robert Tyler,
  • Cathy Coutu
Janitha Wanasundara
Agriculture and Agri-Food Canada

Corresponding Author:[email protected]

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Tara McIntosh
Agriculture and Agri-Food Canada
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Dwayne Hegedus
Agriculture and Agri-Food Canada
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Suneru Perera
University of Saskatchewan College of Agriculture and Bioresources
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Robert Tyler
University of Saskatchewan
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Cathy Coutu
Agriculture and Agri-Food Canada
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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 medium pH 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.
06 Jan 2022Submitted to Journal of the American Oil Chemists' Society
06 Jan 2022Submission Checks Completed
06 Jan 2022Assigned to Editor
24 Jan 2022Reviewer(s) Assigned
03 Apr 2022Review(s) Completed, Editorial Evaluation Pending
04 Apr 2022Editorial Decision: Revise Minor
31 May 20221st Revision Received
14 Jun 2022Submission Checks Completed
14 Jun 2022Assigned to Editor
23 Jun 2022Review(s) Completed, Editorial Evaluation Pending
28 Jun 2022Editorial Decision: Revise Minor
09 Jul 20222nd Revision Received
11 Jul 2022Submission Checks Completed
11 Jul 2022Assigned to Editor
13 Jul 2022Review(s) Completed, Editorial Evaluation Pending
15 Jul 2022Editorial Decision: Accept