| Literature DB >> 1369055 |
Y Yamasaki1, I Fukumoto, N Kumagai, Y Ohta, T Nakagawa, M Kawamukai, H Matsuda.
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.Entities:
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Year: 1992 PMID: 1369055 DOI: 10.1271/bbb.56.1546
Source DB: PubMed Journal: Biosci Biotechnol Biochem ISSN: 0916-8451 Impact factor: 2.043