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Utilizing protein-lean coproducts from corn containing recombinant pharmaceutical proteins for ethanol production.
Paraman, Ilankovan; Moeller, Lorena; Scott, M Paul; Wang, Kan; Glatz, Charles E; Johnson, Lawrence A.
Afiliação
  • Paraman I; Department of Food Science and Human Nutrition, Center for Crops Utilization Research, Iowa State University, Ames, Iowa 50011, USA.
J Agric Food Chem ; 58(19): 10419-25, 2010 Oct 13.
Article em En | MEDLINE | ID: mdl-20809624
ABSTRACT
Protein-lean fractions of corn (maize) containing recombinant (r) pharmaceutical proteins were evaluated as a potential feedstock to produce fuel ethanol. The levels of residual r-proteins in the coproduct, distillers dry grains with solubles (DDGS), were determined. Transgenic corn lines containing recombinant green fluorescence protein (r-GFP) and a recombinant subunit vaccine of Escherichia coli enterotoxin (r-LTB), primarily expressed in endosperm, and another two corn lines containing recombinant human collagen (r-CIα1) and r-GFP, primarily expressed in germ, were used as model systems. The kernels were either ground and used for fermentation or dry fractionated to recover germ-rich fractions prior to grinding for fermentation. The finished beers of whole ground kernels and r-protein-spent endosperm solids contained 127-139 and 138-155 g/L ethanol concentrations, respectively. The ethanol levels did not differ among transgenic and normal corn feedstocks, indicating the residual r-proteins did not negatively affect ethanol production. r-Protein extraction and germ removal also did not negatively affect fermentation of the remaining mass. Most r-proteins were inactivated during the mashing process used to prepare corn for fermentation. No functionally active r-GFP or r-LTB proteins were found after fermentation of the r-protein-spent solids; however, a small quantity of residual r-CIα1 was detected in DDGS, indicating that the safety of DDGS produced from transgenic grain for r-protein production needs to be evaluated for each event. Protease treatment during fermentation completely hydrolyzed the residual r-CIα1, and no residual r-proteins were detectable in DDGS.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas Recombinantes / Plantas Geneticamente Modificadas / Zea mays / Etanol Idioma: En Ano de publicação: 2010 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas Recombinantes / Plantas Geneticamente Modificadas / Zea mays / Etanol Idioma: En Ano de publicação: 2010 Tipo de documento: Article