Enhanced In Vitro Cascade Catalysis of Glycerol into Pyruvate and Acetoin by Integration with Dihydroxy Acid Dehydratase from <i>Paralcaligenes ureilyticus</i>
Recently, an in vitro enzymatic cascade was constructed to transform glycerol into the high-value platform chemical pyruvate. However, the low activity of dihydroxy acid dehydratase from <i>Sulfolobus solfataricus</i> (SsDHAD) limited the efficiency. In this study, the enzymatic reductio...
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| Autores principales: | , , , , , , |
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| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
MDPI AG
2021
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| Materias: | |
| Acceso en línea: | https://doaj.org/article/7ea5f4d9381049088e3d6a41b6d43ddb |
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| Sumario: | Recently, an in vitro enzymatic cascade was constructed to transform glycerol into the high-value platform chemical pyruvate. However, the low activity of dihydroxy acid dehydratase from <i>Sulfolobus solfataricus</i> (SsDHAD) limited the efficiency. In this study, the enzymatic reduction of pyruvate catalyzed by <span style="font-variant: small-caps;">d</span>-lactate dehydrogenase from <i>Pseudomonas aeruginosa</i> PAO1 was used to assay the activities of dihydroxy acid dehydratases. Dihydroxy acid dehydratase from <i>Paralcaligenes ureilyticus</i> (PuDHT) was identified as the most efficient candidate for glycerate dehydration. After the optimization of the catalytic temperature for the enzymatic cascade, comprising alditol oxidase from <i>Streptomyces coelicolor</i> A3, PuDHT, and catalase from <i>Aspergillus niger</i>, 20.50 ± 0.27 mM of glycerol was consumed in 4 h to produce 18.95 ± 0.97 mM of pyruvate with a productivity 12.15-fold higher than the previous report using SsDHAD. The enzymatic cascade was further coupled with the pyruvate decarboxylase from <i>Zymomonas mobile</i> for the production of another platform compound, acetoin. Acetoin at a concentration of 8.52 ± 0.12 mM was produced from 21.62 ± 0.19 mM of glycerol with a productivity of 1.42 ± 0.02 mM h<sup>−1</sup>. |
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