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ARS Home » Plains Area » Manhattan, Kansas » Center for Grain and Animal Health Research » Grain Quality and Structure Research » Research » Research Project #414694


Location: Grain Quality and Structure Research

2012 Annual Report

1a. Objectives (from AD-416):
1) Determine the adhesive properties of sorghum proteins isolated from DDGS, bran and flour, 2) Determine the chemical properties of sorghum proteins related to adhesive and bio-plastic quality, and 3) Improve the quality of sorghum protein based adhesives and bio-plastics.

1b. Approach (from AD-416):
Optimize the isolation of sorghum proteins from DDGS, bran, and/or sorghum flour and characterize the chemical properties of the isolated proteins and their functional properties in adhesives and bio-plastic production. Isolate proteins from sorghum grains with known attributes (e.g. hardness) to determine the factors that influence the quality of sorghum based adhesives and bio-plastics.

3. Progress Report:
Use of coproducts generated during fermentation is important to the overall economics of biofuel production. The main coproduct from grain-based ethanol production is distillers dried grains with solubles (DDGS). High in protein, DDGS is a potential source of protein for many bioindustrial applications such as adhesives and resins. The objective of the first phase of this research was to characterize the composition as well as chemical and physical properties of kafirin proteins from sorghum DDGS with various extraction methods including use of acetic acid, HCl-ethanol and NaOH-ethanol under reducing conditions. Extraction conditions affected purity and thermal properties of the extracted kafirin proteins. Extraction yields of 44.2, 24.2, and 56.8% were achieved by using acetic acid, HCl-ethanol and NaOH-ethanol, respectively. Acetic acid and NaOH-ethanol produced protein with higher purity than kafirins extracted with the HCl-ethanol protocol. The acetic acid extraction protocol produced protein with the highest purity, 98.9%. Several techniques were used to evaluate structural, molecular and thermal properties of kairin extracts. FTIR showed alpha-helix dominated in all three samples, with only a small portion of ß-sheet present. Electrophoresis results showed R1, R2 band and ß kafirins were present in all three extracts. Glass transition peaks of the extracts were shown by DSC to be approximately 230 degrees Celsius. Kafirin degraded at 270-290 degrees Celsius. Size exclusion chromatography revealed that the acetic acid and HCl-ethanol based extraction methods tended to extract more high molecular weight protein than the NaOH-ethanol based method. Reversed phase high-performance liquid chromatography showed that the gamma-kafirins were found only in extracts from the NaOH-ethanol extraction method. The objective of the second phase of this research was to compare the adhesive performance of three types of sorghum proteins: acetic acid-extracted sorghum protein from DDGS (PI), aqueous ethanol-extracted sorghum protein from DDGS (PII) and acetic acid-extracted sorghum protein from sorghum flour (PF). Physicochemical properties including amino acid composition, and rheological, thermal and morphological properties also were characterized. Results showed that PI had the best adhesion performance in terms of dry, wet and soak adhesion strength, followed by PF and PII. The wet strength of PI at a concentration of 12% protein assembled at 150 °C was 3.15 MPa, compared to 2.17 MPa and 2.59 MPa for PII and PF, respectively. DSC thermograms indicated that the PF protein isolates contained higher levels of carbohydrates than PI and PII; such non-protein contaminants in the PF isolate could be the reason for its lower adhesion strength than PI. In addition, PI might have more hydrophobic amino acids aligned at the protein-wood interface than PII, which could explain the better water resistance of PI. The optimum sorghum protein concentration and pressing temperature for maximum adhesion strength was 12% and 150 °C. PI had a significantly higher wet strength (3.15 MPa) than unmodified soy protein (1.63 MPa for soy protein). The high percentage of hydrophobic amino acids in PI (57%) was likely a key factor in the increased water resistance of PI compared with soy protein (36% hydrophobic amino acids). These results indicated that sorghum protein has huge potential as an alternative to petroleum-based adhesives.

4. Accomplishments