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Rheological characterization and dissolution kinetics of fibrin gels crosslinked by a microbial transglutaminase
Author(s) -
Sun Yan,
Giraudier Olivier,
Garde Véronique Larreta
Publication year - 2005
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20177
Subject(s) - tissue transglutaminase , chemistry , rheology , covalent bond , fibrin , kinetics , viscoelasticity , dissolution , chemical engineering , fibronectin , polymer chemistry , chromatography , enzyme , biochemistry , organic chemistry , extracellular matrix , materials science , physics , quantum mechanics , engineering , immunology , composite material , biology
Various fibrin gels were prepared with a microbial transglutaminase under miscellaneous conditions. The gels were characterized through their rheological properties. The influence of fibronectin addition and that of covalent bonding on the viscoelastic characteristics were evaluated. Gel elasticity is proportional to fibrinogen concentration but shows a nonlinear dependence on transglutaminase concentration. Additional crosslink of fibronectin in fibrin gels has no effect on the rheological character of the matrix. Dissolution kinetics in concentrated urea solutions evidences the role of covalent bonds on gel stability. The rheological properties and gel stability are discussed in relation with the enzyme‐catalyzed covalent bonding. The microbial enzyme reactions are compared to those of FXIII and tissue transglutaminases. © 2005 Wiley Periodicals, Inc. Biopolymers, 2005