ARS | Publication request: Extraction of proteins from pennycress

Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: November 15, 2010
Publication Date: March 31, 2011
Citation: Selling, G.W., Evangelista, R.L., Isbell, T., Hojillaevangelist, M.P. 2011. Extraction of Proteins from Pennycress. Meeting Abstract. #.

Technical Abstract: Pennycress (Thlaspi arvense L.)has recently been found to have value as a source of biodiesel. Not only does it provide a high yield of quality oil, but perhaps more importantly, it can be planted after the harvest of traditional crops. It will grow through the winter (on days warmer than 0 C) and can be harvested before the normal planting season of conventional crops. In order to reach its full economic potential, as much of the pennycress seed as possible should be utilized. Due to the presence of glucosinolates, pennycress products cannot be readily used in food applications. Therefore, efforts are being employed to utilize possible co-products in non-food applications. Pennycress seed contains approximately 20% protein; little is known about these proteins. Pennycress ground seed and press cake (after the oil has been removed) were extracted under a variety of conditions in order to obtain available protein. Solvents used included water, saline, 70% ethanol/water, 60% acetic acid, and 0.1 N NaOH/water. The use of water as the extracting agent provided the most material extracted from both the press cake and seed, however, the protein content of this material was around 35%. While the material obtained after saline extraction had the highest protein content (83%) the total amount of material extracted was rather low. By SDS-PAGE, there were differences between that which was extracted from the seed and cake when water and acetic acid were used as solvent. When saline was used, the magnitudes of some bands were different, but the same band pattern was present. The apparent molecular weights of the protein varied from 6 to >200 kDa in the presence of a reducing agent. When the reducing agent was not present, the minimum molecular weight protein was on the order of 12 kDa. Differences in the IR spectra were observed, but it was difficult to make specific conclusions given the complex composition.