Biocompatible Hydrogel Formation of Gelatin from Cold Water Fish via Enzymatic Networking

Abstract

Biocompatible hydrogel formation of gelatin from cold water fish skin has been examined using enzyme catalyst. Due to the large number of functional groups in the side chain, gelatin readily undergoes chemical crosslinking, which is important for its possible use as biomaterial. In addition, transglutaminase (TGase) provides an alternative method for creating a gelatin gel and may offer interesting opportunities as injectable material for various applications. The aim of this study was to investigate the effect of the reaction conditions on rheological and mechanical properties of the hydrogels in the enzymatic curing of gelatin from cold water fish skin. The rheological measurements showed that TGase catalyzed the transformation of gelatin solutions into hydrogels, and the gel points were between 3.3 and 144 min depending on the concentration of gelatin and TGase. Furthermore, the buffer pH strongly affected the rheological properties. Mechanical tests of the resulting hydrogels exhibited that the elastic modulus ranged from 21 to 292 kPa, which were influenced by the concentrations of gelatin and TGase. The rheological and mechanical properties of the gelatin gels were closely related to the degree of the crosslinking.