Abstract
AbstractThe use of enzymes in chemical processing is gaining favour due to the reduction of hazardous chemicals and because it is considered to be environmentally safe. The acyl transfer reaction between primary amines and glutamine residues in proteins is catalysed by the enzyme transglutaminase. The efficiency of microbial transglutaminase to attach functional amines and catalyse inter‐ and intra‐molecular crosslinks was investigated using reduced carboxymethylated κ‐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 catalyses the formation of covalent cross‐links between the γ‐carboxyamide group of glutamine and the ε‐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 fibre. Published in 2004 for SCI by John Wiley & Sons, Ltd.
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