Biotechnology Letters

, Volume 22, Issue 18, pp 1459–1464 | Cite as

Immobilization of invertase via carbohydrate moiety on chitosan to enhance its thermal stability

  • Hsyue-Jen Hsieh
  • Po-Chih Liu
  • Wan-Jun Liao

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.

chitosan immobilization invertase thermal stability 

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Copyright information

© Kluwer Academic Publishers 2000

Authors and Affiliations

  • Hsyue-Jen Hsieh
    • 1
  • Po-Chih Liu
    • 1
  • Wan-Jun Liao
    • 1
  1. 1.Department of Chemical EngineeringNational Taiwan UniversityTaipei, Taiwan Republic of China

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