This experiment studied the immobilization of inulinase from Kluyveromyces marxianus in different supports to bioconvert the inulin from Helianthus tuberosus. Inulin was extracted from H. tuberosus tubers, desproteinized and concentrated to 25% total reducing sugars. Inulinase from K. marxianus was concentrated in a rotative evaporator and immobilized onto chitin (with and without glutaraldehyde), sodium alginate (2 and 4%), pectin, a dialysis membrane or controlled-porosity silicate. On chitin, with or without glutaraldehyde, the imobilization rate was 73 and 48 U g-1 respectively. However the hydrolysys of 1g L-1 inulin was very low in both treatments (2.4 % per hour). In sodium alginate gel of 2% and 4% concentration, the conversion was 12% and 26% per hour, respectively. Immobilization onto pectin was not possible due to a high activity pectinase in the enzyme extract. Binding of the enzyme onto dialysis membrane provided recovery of 50% total reducing sugars (42g) in 6h of operation. The controlled-porosity silicate showed an imobilization rate of 43 U g-1 silicate, hydrolyzing 43% of substrate per hour. This activity was, however, exhausted quickly during the process.
Helianthus tuberosus; enzyme; inulinase; inulin
