Immobilization of invertase via carbohydrate moiety on chitosan to enhance its thermal stability
Journal
Biotechnology Letters
Journal Volume
22
Journal Issue
18
Pages
1459-1464
Date Issued
2000
Author(s)
Abstract
A new technique using chitosan as support for covalent coupling of invertase via carbohydrate moiety improved the activity and thermal stability of immobilized invertase. The best preparation of immobilized invertase retained 91% of original specific activity (412 U mg -1). The half-life at 60°C was increased from 2.3 h (tree invertase) to 7.2 h (immobilized invertase). In contrast, the immobilization of invertase via protein moiety on chitosan or using Sepharose as support resulted in less thermostable preparations. Additionally, immobilization of invertase on both supports caused the optimal reaction pH to shift from 4.5 to 2.5 and the substrate (sucrose) concentration for maximum activity to increase from 0.5 M to 1.0 M.
SDGs
Type
journal article