Immobilization of chitinases from Streptomyces griseus and Paenibacillus illinoisensis on chitosan beads

► Chitinases of S. griseus and P. illinoisensis KJA-424 used for enzyme immobilization. ► For stability, total chitinase activity of S. griseus was 1.4 units/2 mL in the absence of glutaraldehyde. ► Enzyme immobilization with glutaraldehyde 10% was the highest activity level for hypha degradation of R. solani. To investigate the enzyme activity of the chitosan beads immobilized with chitinases this study was carried out. Protein content of the Streptomyces griseus enzyme in supernatant was not detected in test tubes including chitosan beads treated with GA 1, 2, 3, 4, 5, and 10% at 6 h after the reaction except for glutaraldehyde (GA) 0%. Also, chitinase activity of the supernatant was highest (2.68 unit/mL), in GA 0%. Regarding enzyme stability of S. griseus, total chitinase activities were 1.4, 0.4, and 0.3 units/2 mL in GA 0%, 3%, and 5%, respectively, at the initial reaction time. The supernatant protein from Paenibacillus illinoisensis KJA-424 was bound at the highest level of 42% in chitosan beads treated with GA 10% after reaction at 4 °C for 24 h. Immobilized enzyme with GA 10% showed the highest activity level for degradation of hypha from Rhizoctonia solani.