ISSN:
1573-6776
Keywords:
chitosan
;
immobilization
;
invertase
;
thermal stability
Source:
Springer Online Journal Archives 1860-2000
Topics:
Process Engineering, Biotechnology, Nutrition Technology
Notes:
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 (free 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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1005602812037
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