IMMOBILIZATION OF INULINASE FROM ASPERGILLUS KAWACHII ON CHITOSAN FOR ITS APPLICATTION IN INULIN HYDROLISIS

CHESINI M;; CAVELLO IA;; ROJAS NL;; CAVALITTO SF;

Foz de Iguazú, Paraná

Simposio; XIX SIMPÓSIO NACIONAL DE BIOPROCESSOS X SIMPÓSIO DE HIDRÓLISE ENZIMÁTICA DE BIOMASSAS; 2013

Asociación Brasileña de Ingeniería Química (ABEQ)

ABSTRACT Crude inulinase from Aspergillus kawachii was immobilized using chitosan beads. Some parameters of this immobilization procedure were studied: the production of the chitosan beads (in terms of glutaraldehyde concentration and activation time) was optimized using factorial design and surface response techniques. Once the immobilization procedure was established, enzyme characteristics such as optimal pH, temperature stability, and reuse of the enzyme were determined in order to be compared to those of the free enzyme. Optimal pH was found to be 4,5; 28 % of the enzyme activity remnants after 30 min of incubation at 70°C and a five times reutilization of the enzyme was determined. The immobilization procedure proposed here confers to the enzyme some characteristics which could make it a robust biocatalyst for the hydrolysis of inulin in a continuous procedure.