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Published on: October 24, 2016
Utilizing protein-lean coproducts from corn containing recombinant pharmaceutical proteins for ethanol production
Ilankovan Paraman1, Lorena Moeller, M Paul Scott
1Department of Food Science and Human Nutrition, Center for Crops Utilization Research, Iowa State University, Ames, Iowa 50011, USA.
Fuel ethanol production from transgenic corn is feasible, as residual recombinant proteins do not impact yield. Most proteins are inactivated during processing, ensuring safe distillers dry grains with solubles (DDGS) production.
Area of Science:
- Biotechnology
- Agricultural Science
- Biofuel Production
Background:
- Corn (maize) is a primary feedstock for fuel ethanol production.
- Transgenic crops offer potential for producing valuable recombinant proteins.
- Assessing the impact of recombinant proteins on ethanol production and coproduct safety is crucial.
Purpose of the Study:
- To evaluate protein-lean corn fractions with recombinant proteins as a feedstock for fuel ethanol.
- To determine residual recombinant protein levels in distillers dry grains with solubles (DDGS).
- To assess the impact of recombinant proteins on ethanol yield and the safety of DDGS.
Main Methods:
- Utilized transgenic corn lines expressing recombinant green fluorescence protein (r-GFP), recombinant Escherichia coli enterotoxin subunit vaccine (r-LTB), and recombinant human collagen (r-CIα1).
- Fermented whole ground kernels and fractionated corn (germ-removed) for ethanol production.
- Analyzed residual r-proteins in DDGS using biochemical assays and fermentation inactivation studies.
Main Results:
- Ethanol concentrations were comparable between transgenic and normal corn feedstocks (127-155 g/L).
- Recombinant protein extraction and germ removal did not negatively affect fermentation efficiency.
- Most r-proteins were inactivated during mashing; residual r-CIα1 was detected but fully hydrolyzed by protease treatment.
Conclusions:
- Transgenic corn containing recombinant proteins can be effectively used for fuel ethanol production without compromising yield.
- The mashing process significantly inactivates most recombinant proteins, enhancing the safety of the DDGS coproduct.
- Specific event-based safety evaluations are necessary for DDGS intended for applications where residual proteins are a concern, though protease treatment ensures complete hydrolysis.
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