Immobilisation of catalase on the surface of biodegradable starch-based polymers as a way to change its surface...

In this study, a specific enzyme catalase was immobilised onto the surface of two different biodegradable materials, starch cellulose acetate (SCA) and starch polycrapolactone (SPCL) blends. This immobilisation was achieved by several different routes, mainly by covalent binding and an adsorption method using as activation agents epichlorohydrin, cyanogen bromide (CNBr), and aminopropyltriethoxysilane. The effect of the coupling pH of the enzyme-support reaction was determined in terms of activity recovery (%). The catalase immobilised on SCA showed higher activity recovery (%) for all the methods used as compared with results obtained with SPCL. The immobilisation process using epichlorohydrin as an activation agent and polyethylenimine as a spacer-arm enhanced the stability and the half-lives at pH 7.0, 30 degrees C, for immobilised catalase on both SCA and SPCL. The half-lives were respectively, 1162 and 870 h compared with other treatments and free enzyme (480 h). The free glycerol present in the immobilisation medium was also a factor that contributed toward the better performance regarding the long-term stability at 30 degrees C and neutral pH. The extension of the morphological modifications on the surface of the materials was observed by scanning electron microscopy. In general, the results indicated that the chemical modification with epichlorohydrin could provide a simple and rather efficient technique to modify the starch-based materials' surface that might be useful in several biomedical applications.