Immobilization of .ALPHA.-amylase on glycolchitosan.

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  • Kusaoke Hideo
    Department of Environment and Safety Engineering, Fukui Institute of Technology
  • Kasaba Keigi
    Department of Environment and Safety Engineering, Fukui Institute of Technology
  • Sakurai Takehisa
    Department of Environment and Safety Engineering, Fukui Institute of Technology

Bibliographic Information

Other Title
  • グリコールキトサン上へのα-アミラーゼの固定化
  • グリコールキトサン上へのα-アミラーゼの固定化〔英文〕
  • グリコールキトサンジョウ ヘ ノ アルファ アミラーゼ ノ コテイカ エイブン

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Abstract

As noble solid supports for enzyme immobilization, partly glycolated chitosans were prepared from chitosan. α-Amylase was immobilized on a glycolchitosan with the aid of cross-linking agent glutaraldehyde. The maximum activity yield of enzyme immobilized on glycolchitosan with a degree of substitution of glycol groups of 0.78 was 28%, compared with that on chitosan of 20%.<br>The optimum pH for the conversion of starch to reducing sugars by the immobilized enzyme on glycolchitosan was approximately 6. This was lower than that for the conversion with free enzyme. The optimum temperature for the conversion using immobilized enzyme was 60°C, similar to that for the conversion with free enzyme. Immobilized α-amylase on glycolchitosan retained about 80% of the maximum enzyme activity after repeated use of 6 times.

Journal

  • Sen'i Gakkaishi

    Sen'i Gakkaishi 43 (9), 495-498, 1987

    The Society of Fiber Science and Technology, Japan

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