Enzyme immobilization on fibrin

Biotechnol Bioeng. 1976 Jan;18(1):133-9. doi: 10.1002/bit.260180112.


The following conclusions can be drawn concerning the utilization of fibrin to immobilized enzyme systems. Fibrin can be used both as a powder or membrane, to covalently immobilize trypsin with retention of activity. Carbon-14 labeled trypsin can be used to estimate the amount of immobilized enzyme on a proteinaceous support. Significant amounts of noncovalently coupled (adsorbed) enzyme are present on the surface of the support. Esterase activity of the immobilized labeled trypsin was inversely proportional to the amount of attached enzyme. Optimum TAME hydrolysis occurred at pH 8-8.4. The storage stability of trypsin was enhanced. Inhibition of trypsin esterase activity occurred at substrate concentrations greater than 30mM.

MeSH terms

  • Adsorption
  • Drug Storage
  • Fibrin* / metabolism
  • Hydrogen-Ion Concentration
  • Kinetics
  • Protein Binding
  • Trypsin* / metabolism


  • Fibrin
  • Trypsin