INMOVILIZACIÓN DE CELULASA SOBRE UNA MATRIZ DE QUITINA-QUITOSANA
Abstract
Cellulase from Biochemika were inmovililized for physics absorption and covalent bond with glutaraldehyde in the support chitin-chitosan. The optimal concentration of glutaraldehyde for bond enzyme to the support was 0,25 % with reaction time ½ hour. The best conditions for the physics absorption were: pH= 4,5, protein concentration = 170 μ/mL and incubation time= 4 hours. Various
characteristics of immobilized cellulases such as the pH optimum , thermal stability, and reuse were evaluated. The modification process increased the thermostability of enzymes after physics adsorption on support and covalent attachement respectively. The pH optimum of enzymes change for the acid region for modification. The cellulase immobilized by covalent attachment to the chitosan-coated chitin support, retained about 60 % of its initial activity after 15 cycles of reuse.
Keywords: cellulase, immobilized, covalent bond, physics absorption, chitin-chitosan.
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