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Immobilization of glucoamylase onto novel porous polymer supports of vinylene carbonate and 2-hydroxyethyl methacrylate

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Abstract

Glucoamylase was immobilized onto novel porous polymer supports. The properties of immobilized glucoamylase and the relationship between the activity of immobilized enzyme and the properties of porous polymer supports were investigated. Compared with the native enzyme, the temperature profile of immobilized glucoamylase was widened, and the optimum pH was also changed. The optimum substrate concentration of immobilized glucoamylase was higher than that of native enzyme. After storage for 23 d, the immobilized glucoamylase still maintained about 84% of its initial activity, whereas the native enzyme only maintained about 58% of the initial activity. Moreover, after using repeatedly seven times, the immobilized enzyme maintained about 85% of its initial activity. Furthermore, the properties of porous polymer supports had an effect on the activity of the immobilized glucoamylase.

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  1. Yanli Huo

    Present address: Institute of Advanced Materials, Fudan University, 200433, Shanghai, P. R. China

Authors and Affiliations

  1. Department of Chemistry, The State Key Laboratory of Functional Polymer Materials for Adsorption and Separation, Nankai University, 300071, Tianjin, P.R. China

    Yanli Huo, Yue Li, Zhi Yuan & Jiaxian Huang

Authors
  1. Yanli Huo
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  2. Yue Li
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  3. Zhi Yuan
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  4. Jiaxian Huang
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Correspondence to Yanli Huo.

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Huo, Y., Li, Y., Yuan, Z. et al. Immobilization of glucoamylase onto novel porous polymer supports of vinylene carbonate and 2-hydroxyethyl methacrylate. Appl Biochem Biotechnol 119, 121–131 (2004). https://doi.org/10.1385/ABAB:119:2:121

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  • DOI: https://doi.org/10.1385/ABAB:119:2:121

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