Immobilization of<i>Bacillus licheniformis</i><scp>L</scp>-Arabinose Isomerase for Semi-Continuous<scp>L</scp>-Ribulose Production

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  • ZHANG Ye-Wang
    Department of Chemical Engineering, Konkuk University
  • PRABHU Ponnandy
    Department of Bioscience and Biotechnology, Konkuk University
  • LEE Jung-Kul
    Department of Chemical Engineering, Konkuk University Institute of Biomedical Science and Technology, Konkuk University

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  • Immobilization of Bacillus licheniformis L-Arabinose Isomerase for Semi-Continuous L-Ribulose Production

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Bacillus licheniformis L-arabinose isomerase (BLAI) with a broad pH range, high substrate specificity, and high catalytic efficiency for L-arabinose was immobilized on various supports. Eupergit C, activated-carboxymethylcellulose, CNBr-activated agarose, chitosan, and alginate were tested as supports, and Eupergit C was selected as the most effective. After determination of the optimum enzyme concentration, the effects of pH and temperature were investigated using a response surface methodology. The immobilized BLAI enzyme retained 86.4% of the activity of the free enzyme. The optimal pH for the immobilized BLAI was 8.0, and immobilization improved the optimal temperature from 50 °C (free enzyme) to a range between 55 and 65 °C. The half life improved from 2 at 50 °C to 212 h at 55 °C following immobilization. The immobilized BLAI was used for semi-continuous production of L-ribulose. After 8 batch cycles, 95.1% of the BLAI activity was retained. This simple immobilization procedure and the high stability of the final immobilized BLAI on Eupergit C provide a promising solution for large-scale production of L-ribulose from an inexpensive L-arabinose precursor.

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