Yamasaki Y, Fukumoto I, Kumagai N, Ohta Y, Nakagawa T, Kawamukai M, Matsuda H
Applied Biological Sciences, Faculty of Agriculture, Shimane University, Matsue, Japan.
Biosci Biotechnol Biochem. 1992 Oct;56(10):1546-51. doi: 10.1271/bbb.56.1546.
Chitosanolytic enzymes from Enterobacter sp. G-1 were immobilized on various carriers to continuously hydrolyze chitosan. Four different carriers were tested: FE-3901 (strong basic anion exchange resin, ionic binding), glutaraldehyde-treated FE-4612 (weak basic anion exchange resin, cross-linking), Chitopearl (chitosan beads), and alginate calcium. Glutaraldehyde-treated FE-4612 and Chitopearl immobilized more protein than the others. The enzyme immobilized on FE-3901 had the greatest activity. The activity of enzyme immobilized on FE-3901 decreased rapidly when exposed to a continuous flow of 1% chitosan. The enzyme immobilized with Chitopearl retained more than 50% of its original activity after 17 days, and the activity was fully restored by re-immobilization.
