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ARS Home » Research » Publications at this Location » Publication #151335


item Gembeh, Shirley
item Farrell Jr, Harold
item Taylor, Maryann
item Brown, Eleanor - Ellie
item Marmer, William

Submitted to: Journal of the Science of Food and Agriculture
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 6/23/2004
Publication Date: 11/8/2004
Citation: Gembeh, S.V., Farrell Jr, H.M., Taylor, M.M., Brown, E.M., Marmer, W.N. 2004. Application of transglutaminase to derivatize proteins. 1. studies on soluble proteins and preliminary results on wool. Journal of the Science of Food and Agriculture. 85:418-424.

Interpretive Summary: Although wool burns more slowly than most other fibers, enhancing its flame retardance is still a commercial objective. Functional properties can be added to wool through chemical reaction, but enzymatic alternatives are favored for their safety, mildness, and environmental responsibility. To probe an enzymatic process to impact flame retardance to wool, a protein fiber, we investigated the enzymatic addition of a potential flame retardant, O-phosphorylethanolamine, to soluble proteins. After obtaining positive results we carried out the reaction on wool fabric. Our results indicate that we successfully fixed the retardant onto wool enzymatically. This will offer the industry alternative methods for enhancing the safety of wool, and will inspire further research on the enzymatic modification of the natural fiber.

Technical Abstract: The use of enzymes in chemical processing is gaining favor because of the reduction of hazardous chemicals and it is considered to be environmentally safe. The acyl transfer reaction between primary amines and glutamine residues in proteins is catalyzed by the enzyme transglutaminase. The efficiency of microbial transglutaminase to attach functional amines and catalyze inter- and intra-molecular crosslinks was investigated using reduced carboxymethylated kappa-casein, gelatin and wool. Model systems used in this research gave evidence of both cross-linking of the protein and covalent binding of the primary amine O-phosphorylethanolamine to the protein. These data agree with earlier publications that show transglutaminase catalyzes the formation of covalent cross-links between the gamma-carboxyamide group of glutamine and the epsilon-amino group of lysine and also the incorporation of primary amines into proteins. Preliminary analysis of treated wool indicated the covalent bonding of the functional amine to the protein. Our goal is to increase the value of wool by enzymatic addition of functional groups to the wool fiber.