Continuous Chitosan Hydrolyzate Production by Immobilized Chitosanolytic Enzyme from<i>Enterobacter</i>sp. G-1

Yukikazu Yamasaki, Ikuo Fukumoto, Naoki Kumagai, Yukari Ohta, Tsuyoshi Nakagawa, Makoto Kawamukai, Hideyuki Matsuda

Bioscience Biotechnology and Biochemistry · 1992 · 25 citations · 0 references

Concepts

Abstract

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.