Immobilization of Cassava Linamarase on Kankara Kaolinite Clay

Abstract

The enzyme, linamarase was successfully extracted and immobilized on pretreated Kankara kaolinite clay, serving as substitute for other expensive catalysts supports. Acid treatment of the clay was observed to affect the activity of linamarase. The activity of the enzyme was higher in the cortex compared with both in the stem and the leaves. Enzyme activity was observed to increase with increase in the silica contents of the treated clay. Operational stability/activity of the immobilized enzyme was found to reduce by about 50% after 18days at room temperature, following first order denaturation reaction, with rate constant k obtained to be 0.03day^-1 with R² 0.957. The K_m and V_max were determined to 0.1986mM^-1 and 10.01mM/min respectively, which is an indication of the enzyme’s affinity to the support used. The specific surface area and pore size of kaolin were also found to decrease with rate of enzyme anchoring, pointing to occupation and/or blockage of the available pore. Kankara kaolinite clay is a promising cheaper support material for linamarase immobilization.

Keywords: linamarase, immobilization, kaolinite clay, cassava, metakaolin, cyanogen