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

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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.

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Authors and Affiliations

  1. Department of Chemical Engineering, National Taiwan University, Taipei, Taiwan , 10617, Republic of China

    Hsyue-Jen Hsieh, Po-Chih Liu & Wan-Jun Liao

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  1. Hsyue-Jen Hsieh
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  2. Po-Chih Liu
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  3. Wan-Jun Liao
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Hsieh, HJ., Liu, PC. & Liao, WJ. Immobilization of invertase via carbohydrate moiety on chitosan to enhance its thermal stability. Biotechnology Letters 22, 1459–1464 (2000). https://doi.org/10.1023/A:1005602812037

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  • DOI: https://doi.org/10.1023/A:1005602812037

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