Characterization of collagen matrices crosslinked using microbial transglutaminase

Ray Neng Chen, Hsiu O. Ho, Ming Thau Sheu

Research output: Contribution to journalArticlepeer-review

113 Citations (Scopus)


In search of a new approach for crosslinking collagen-based biomaterials, we examined the effect of microbial transglutaminase (MTGases) as a crosslinking reagent on collagenous matrices made from porcine type I collagen. As the results revealed, MTGase exhibited a crosslinking action that raised the viscosity of the collagen solution. Matrices crosslinked with MTGase at the low pH values of pH 3 and 4 exhibited higher tensile strengths than those at high pH values. In comparison with untreated matrices, the denaturation temperatures of the corresponding matrices shifted toward higher temperatures. These enzyme-catalyzed crosslinked matrices were proven by MTT assay to be non-cytotoxic. In conclusion, this enzymatic method of using MTGase provides an alternative potential way for crosslinking collagen-based matrices.

Original languageEnglish
Pages (from-to)4229-4235
Number of pages7
Issue number20
Publication statusPublished - Jul 2005


  • Biomaterials
  • Collagen
  • Crosslinking
  • Enzyme
  • Matrix
  • Transglutaminase

ASJC Scopus subject areas

  • Mechanics of Materials
  • Ceramics and Composites
  • Bioengineering
  • Biophysics
  • Biomaterials


Dive into the research topics of 'Characterization of collagen matrices crosslinked using microbial transglutaminase'. Together they form a unique fingerprint.

Cite this