Transglutaminase Reactivity with Gelatine: Perspective Applications in Tissue Engineering

• DOI: 10.1007/s10529-006-9046-2
• Publication Date: 2006-05-23T03:47:18Z
• Authors: F. Bertoni; N. Barbani; P. Giusti; G. Ciardelli
• Keywords: 0301 basic medicine; Transglutaminases; Tissue Engineering; Swine; Glutamine; Lysine; Polysaccharides, Bacterial; Biocompatible Materials; Fibroblasts; 03 medical and health sciences; Cross-Linking Reagents; Polysaccharides; Spectroscopy, Fourier Transform Infrared; Cell Adhesion; Animals; Gelatin; Biotechnology

Gelatine was crosslinked by means of an enzymatic treatment using tissue transglutaminase (tTGase) (Sigma) and microbial transglutaminase (mTGase) (Ajinomoto) which catalyses the formation of isopeptide bonds between the gamma-carbonyl group of a glutamine residue and the epsilon-amino group of a lysine residue. The reaction is an interesting alternative to the traditional glutaraldehyde crosslinking, which has several drawbacks (e.g., in medical application) due to the toxicity of the chemical reagent. To further investigate the possibility to utilize the modified protein for tissue engineering application, TGase crosslinked gelatine was incorporated in a gellan matrix, a polysaccharide, to enhance the stability in aqueous media. Films obtained by casting were characterized by thermal analysis, chemical imaging, swelling behaviour and cell adhesion.