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Optimizing extraction methods to improve utilization of wheat gluten in bio-product manufacturing

Optimizing extraction methods to improve utilization of wheat gluten in bio-product manufacturing. Project Title:. By: Shannon Williamson. Mentors: Dr. Andrew Ross Dr. Kaichang Li Crop and Soil Science Wood Science Oregon State University Oregon State University.

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Optimizing extraction methods to improve utilization of wheat gluten in bio-product manufacturing

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  1. Optimizing extraction methods to improve utilization of wheat gluten in bio-product manufacturing Project Title: By: Shannon Williamson Mentors: Dr. Andrew Ross Dr. Kaichang Li Crop and Soil Science Wood Science Oregon State University Oregon State University

  2. Temporary wet strength resins (TWSR) • When paper/paper products become wet their tensile strength decreases dramatically. Therefore, resins are added to these products to increase wet strength for a duration of time. • Two types of resins: Temporary and permanent that can provide either short or long lasting wet strength. • Ren and Li (2005) developed a temporary wet-strength additive from wheat gluten for use in the paper and paperboard industry.

  3. Why wheat gluten? • Wheat gluten is widely available, inexpensive and bio-degradable. • Currently the paper industry uses glyoxal-polyacrylamide (GPA) which is manufactured from petro-chemicals. • Wheat gluten is a renewable resource • The new temporary wet-strength additive could be used in the industry if the wheat gluten extraction process was refined.

  4. Wheat endosperm protein composition • Albumins and Globulins~15-20% (Not useful for TWSR) • Gliadins and Glutenins~75-80% • This new additive has been made with only the gliadins • only using about half of the available protein.

  5. Gliadins vs. Glutenins • Gliadins are soluble in 70% ethanol • Glutenin • is the residue leftover from the extraction of gliadin. • Glutenin subunits are not soluble... • due to the large size of the protein subunits. • due to inter-subunit disulfide bonds

  6. Approach Chemical Modification of wheat gluten • Gluten becomes soluble in a variety of chemicals: soaps, detergents, hydrochloric acid, sodium hydroxide, 70% ethanol are just a few possibilities. • Solubilization by deamidation is also used; this can be in acidic or basic solutions. Removal of the amide group of glutamine results in a change in the potential ionic charge on the protein. • Enzymatic modification is a process that hydrolyzes peptide bonds and increases the solubility of gluten.

  7. Outline of reaction scheme • Measure protein content of gluten with LECO and perform HPLC analysis of existing proteins • 8% (w/v) ratio of gluten in aqueous solution • Addition of enzyme to modify gluten protein • The fractions will be separated by centrifugation • Remeasure protein content and examine HPLC • Sonication of existing residues (insoluble fraction)

  8. Enzymes • Two enzymes utilized 1. Bacterial protease from Bacillus licheniformis( Subtilisin A)2. Fungal protease from Aspergillus oryzae • Both are endoproteases with broad specificity toward native and denatured proteins • Both perform best in an environment pH= 6.0-9.0

  9. Chromatogram for untreated gluten • Gluten – sonicated 1 min (black) • Gluten- sonicated 3 min (green) • Gluten – sonicated 5 min (blue) Glutenin Peak Gliadin Peak

  10. SE-HPLC Data for Run 1-1 and 1-2 • Red- 1 minute sonication of gluten • Blue- No sonication of gluten • Black-Run - Fungal protease - 1 hr. treatment • Green-Run - Fungal protease - 30 minute treatment

  11. Results of Enzymatic Treatment • ~100% of protein was soluble in water • Solubilized protein has a considerably reduced mass due to hydrolysis • With the protein in solution the TWSR was then made according the Ren and Li (2005)

  12. Resin From Hydrolyzed Gluten Protein • Hydrolyzed protein was modified with glycidyltrimethylammonium chloride (GTA) • GTA modified protein underwent another reaction with glyoxal to create a GTA-gluten protein-glyoxal resin. • When this last reaction was performed between GTA-gliadin and glyoxal, a significant change in viscosity was observed. • In the case of my enzymatic treated protein, no change in viscosity was observed.

  13. Conclusions and Future goals • Total solubilization of gluten protein is possible with enzymatic treatment. • Resin made from low molecular weight gluten proteins failed to yield a usable product. • Future approaches • Hydrolyze less to keep MW closer to the MW of gliadin • Separate gliadin from glutenin, followed by hydrolysis of glutenin and then recombining with gliadin

  14. Acknowledgments • Ernest and Pauline Jaworski Fund for Summer Research Experiences for Underserved Undergraduates in Plant Science • Howard Hughes Medical Institute • Dr. Andrew Ross and Dr. Jae Ohm • Dr. Kaichang Li • Crop and Soil & Wood Science Department at Oregon State University

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