Bioconversion of xylose to xylonic acid via co-immobilized dehydrogenases for conjunct cofactor regeneration

Karolina Bachosz, Karol Synoradzki, Maciej Staszak, Manuel Pinelo, Anne S. Meyer, Jakub Zdarta*, Teofil Jesionowski

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review


Enzymatic cofactor-dependent conversion of monosaccharides can be used in the bioproduction of value-added compounds. In this study, we demonstrate co-immobilization of xylose dehydrogenase (XDH, EC and alcohol dehydrogenase (ADH, EC using magnetite-silica core-shell particles for simultaneous conversion of xylose into xylonic acid (XA) and in situ cofactor regeneration. The reaction conditions were optimized by factorial design, and were found to be: XDH:ADH ratio 2:1, temperature 25 °C, pH 7, and process duration 60 min. Under these conditions enzymatic production of xylonic acid exceeded 4.1 mM and was more than 25% higher than in the case of a free enzymes system. Moreover, the pH and temperature tolerance as well as the thermo- and storage stability of the co-immobilized enzymes were significantly enhanced. Co-immobilized XDH and ADH make it possible to obtain higher xylonic acid concentration over broad ranges of pH (6-8) and temperature (15-35 °C) as compared to free enzymes, and retained over 60% of their initial activity after 20 days of storage. In addition, the half-life of the co-immobilized system was 4.5 times longer, and the inactivation constant (kD= 0.0141 1/min) four times smaller, than those of the free biocatalysts (kD= 0.0046 1/min). Furthermore, after five reaction cycles, immobilized XDH and ADH retained over 65% of their initial properties, with a final biocatalytic productivity of 1.65 mM of xylonic acid per 1 U of co-immobilized XDH. The results demonstrate the advantages of the use of co-immobilized enzymes over a free enzyme system in terms of enhanced activity and stability.
Original languageEnglish
Article number102747
JournalBioorganic Chemistry
Number of pages10
Publication statusPublished - 2019


  • Alcohol dehydrogenase
  • Cofactor regeneration system
  • Enzyme co-immobilization
  • Enzyme stability
  • NADH
  • Xylose conversion
  • Xylose dehydrogenase


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