This article is a US Government work and is in the public domain in the USA
Article first published online: 8 NOV 2004
This article is a US Government work and is in the public domain in the USA. Published in 2004 for SCI by John Wiley & Sons, Ltd.
Journal of the Science of Food and Agriculture
Volume 85, Issue 3, pages 418–424, February 2005
How to Cite
Gembeh, S. V., Farrell, H. M., Taylor, M. M., Brown, E. M. and Marmer, W. N. (2005), Application of transglutaminase to derivatize proteins: 1. Studies on soluble proteins and preliminary results on wool. J. Sci. Food Agric., 85: 418–424. doi: 10.1002/jsfa.1999
Mention of brand or firm names does not constitute an endorsement by the US Department of Agriculture over others of similar nature not mentioned.
- Issue published online: 4 JAN 2005
- Article first published online: 8 NOV 2004
- Manuscript Accepted: 23 JUN 2004
- Manuscript Revised: 2 APR 2004
- Manuscript Received: 14 OCT 2003
- gelatin Blooms
The 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.