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

Research output: Contribution to journalJournal article – Annual report year: 2019Researchpeer-review

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Bioconversion of xylose to xylonic acid via co-immobilized dehydrogenases for conjunct cofactor regeneration. / Bachosz, Karolina; Synoradzki, Karol; Staszak, Maciej; Pinelo, Manuel; Meyer, Anne S.; Zdarta, Jakub; Jesionowski, Teofil.

In: Bioorganic Chemistry, 2019.

Research output: Contribution to journalJournal article – Annual report year: 2019Researchpeer-review

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Bachosz, Karolina ; Synoradzki, Karol ; Staszak, Maciej ; Pinelo, Manuel ; Meyer, Anne S. ; Zdarta, Jakub ; Jesionowski, Teofil. / Bioconversion of xylose to xylonic acid via co-immobilized dehydrogenases for conjunct cofactor regeneration. In: Bioorganic Chemistry. 2019.

Bibtex

@article{2d36f2ac93d44409894b8dc9ab3e1836,
title = "Bioconversion of xylose to xylonic acid via co-immobilized dehydrogenases for conjunct cofactor regeneration",
abstract = "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 1.1.1.175) and alcohol dehydrogenase (ADH, EC 1.1.1.1) 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.",
keywords = "Alcohol dehydrogenase, Cofactor regeneration system, Enzyme co-immobilization, Enzyme stability, NADH, Xylose conversion, Xylose dehydrogenase",
author = "Karolina Bachosz and Karol Synoradzki and Maciej Staszak and Manuel Pinelo and Meyer, {Anne S.} and Jakub Zdarta and Teofil Jesionowski",
year = "2019",
doi = "10.1016/j.bioorg.2019.01.043",
language = "English",
journal = "Bioorganic Chemistry",
issn = "0045-2068",
publisher = "Academic Press",

}

RIS

TY - JOUR

T1 - Bioconversion of xylose to xylonic acid via co-immobilized dehydrogenases for conjunct cofactor regeneration

AU - Bachosz, Karolina

AU - Synoradzki, Karol

AU - Staszak, Maciej

AU - Pinelo, Manuel

AU - Meyer, Anne S.

AU - Zdarta, Jakub

AU - Jesionowski, Teofil

PY - 2019

Y1 - 2019

N2 - 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 1.1.1.175) and alcohol dehydrogenase (ADH, EC 1.1.1.1) 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.

AB - 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 1.1.1.175) and alcohol dehydrogenase (ADH, EC 1.1.1.1) 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.

KW - Alcohol dehydrogenase

KW - Cofactor regeneration system

KW - Enzyme co-immobilization

KW - Enzyme stability

KW - NADH

KW - Xylose conversion

KW - Xylose dehydrogenase

U2 - 10.1016/j.bioorg.2019.01.043

DO - 10.1016/j.bioorg.2019.01.043

M3 - Journal article

JO - Bioorganic Chemistry

JF - Bioorganic Chemistry

SN - 0045-2068

ER -