Characterization of collagen matrices crosslinked using microbial transglutaminase

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

Research output: Contribution to journalArticle

81 Citations (Scopus)

Abstract

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
JournalBiomaterials
Volume26
Issue number20
DOIs
Publication statusPublished - Jul 2005

Fingerprint

Transglutaminases
Collagen
Crosslinking
Cross-Linking Reagents
Denaturation
Temperature
Tensile Strength
Biocompatible Materials
Collagen Type I
Viscosity
Assays
Tensile strength
Swine
Biomaterials
Enzymes

Keywords

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

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biomedical Engineering

Cite this

Characterization of collagen matrices crosslinked using microbial transglutaminase. / Chen, Ray Neng; Ho, Hsiu O.; Sheu, Ming Thau.

In: Biomaterials, Vol. 26, No. 20, 07.2005, p. 4229-4235.

Research output: Contribution to journalArticle

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