Transglutaminases as tanning agents for the leather industry

Russell Collighan, Santiago Clara, Xiaoling Li, James Parry, Martin Griffin

Research output: Contribution to journalArticlepeer-review


This study was aimed at determining whether the protein crosslinking enzymes, transglutaminases, had the potential to be used as tanning agents, using native bovine hide and purified soluble rat tail collagen as real and model substrates, respectively. We demonstrate that transglutaminases (TGs) were capable of covalently crosslinking collagen molecules together such that on average every collagen molecule contained at least one epsilon(gamma-glutamyl)lysine crosslink. However, transglutaminase-mediated crosslinking did not affect the denaturation temperature of either native bovine hide or soluble rat tail collagens when used in isolation or together with other proteins and bifunctional diamines as crosslinking facilitators. In an initial study into the effect of TG-mediated crosslinking on the tensile strength of chrome-tanned bovine hide, such crosslinking led to a 30 per cent decrease in tensile strength. Despite a change in the gel melting point mediated by epsilon(gamma-glutamyl)lysine crosslinking, the use of transglutaminases as alternative tanning agents seems unlikely given the present data.
Original languageEnglish
Pages (from-to)293-302
Number of pages10
JournalJournal of the American Leather Chemists Association
Issue number7
Publication statusPublished - Jul 2004


  • protein crosslinking enzymes
  • transglutaminases
  • tanning agents
  • native bovine hide
  • purified soluble rat tail collagen
  • crosslinking collagen molecules
  • epsilon(gamma-glutamyl)lysine


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