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:	Shiting Guo, Xiaoxu Tan, Yuxian Wang, Kai Li, Chuanjuan Lü, Cuiqing Ma, Chao Gao
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	glycerol pyruvate acetoin in vitro enzymatic cascade dihydroxy acid dehydratase Chemical technology TP1-1185 Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/7ea5f4d9381049088e3d6a41b6d43ddb
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spelling	oai:doaj.org-article:7ea5f4d9381049088e3d6a41b6d43ddb2021-11-25T17:05:25ZEnhanced In Vitro Cascade Catalysis of Glycerol into Pyruvate and Acetoin by Integration with Dihydroxy Acid Dehydratase from <i>Paralcaligenes ureilyticus</i>10.3390/catal111112822073-4344https://doaj.org/article/7ea5f4d9381049088e3d6a41b6d43ddb2021-10-01T00:00:00Zhttps://www.mdpi.com/2073-4344/11/11/1282https://doaj.org/toc/2073-4344Recently, 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>.Shiting GuoXiaoxu TanYuxian WangKai LiChuanjuan LüCuiqing MaChao GaoMDPI AGarticleglycerolpyruvateacetoinin vitro enzymatic cascadedihydroxy acid dehydrataseChemical technologyTP1-1185ChemistryQD1-999ENCatalysts, Vol 11, Iss 1282, p 1282 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	glycerol pyruvate acetoin in vitro enzymatic cascade dihydroxy acid dehydratase Chemical technology TP1-1185 Chemistry QD1-999
spellingShingle	glycerol pyruvate acetoin in vitro enzymatic cascade dihydroxy acid dehydratase Chemical technology TP1-1185 Chemistry QD1-999 Shiting Guo Xiaoxu Tan Yuxian Wang Kai Li Chuanjuan Lü Cuiqing Ma Chao Gao Enhanced In Vitro Cascade Catalysis of Glycerol into Pyruvate and Acetoin by Integration with Dihydroxy Acid Dehydratase from <i>Paralcaligenes ureilyticus</i>
description	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>.
format	article
author	Shiting Guo Xiaoxu Tan Yuxian Wang Kai Li Chuanjuan Lü Cuiqing Ma Chao Gao
author_facet	Shiting Guo Xiaoxu Tan Yuxian Wang Kai Li Chuanjuan Lü Cuiqing Ma Chao Gao
author_sort	Shiting Guo
title	Enhanced In Vitro Cascade Catalysis of Glycerol into Pyruvate and Acetoin by Integration with Dihydroxy Acid Dehydratase from <i>Paralcaligenes ureilyticus</i>
title_short	Enhanced In Vitro Cascade Catalysis of Glycerol into Pyruvate and Acetoin by Integration with Dihydroxy Acid Dehydratase from <i>Paralcaligenes ureilyticus</i>
title_full	Enhanced In Vitro Cascade Catalysis of Glycerol into Pyruvate and Acetoin by Integration with Dihydroxy Acid Dehydratase from <i>Paralcaligenes ureilyticus</i>
title_fullStr	Enhanced In Vitro Cascade Catalysis of Glycerol into Pyruvate and Acetoin by Integration with Dihydroxy Acid Dehydratase from <i>Paralcaligenes ureilyticus</i>
title_full_unstemmed	Enhanced In Vitro Cascade Catalysis of Glycerol into Pyruvate and Acetoin by Integration with Dihydroxy Acid Dehydratase from <i>Paralcaligenes ureilyticus</i>
title_sort	enhanced in vitro cascade catalysis of glycerol into pyruvate and acetoin by integration with dihydroxy acid dehydratase from <i>paralcaligenes ureilyticus</i>
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/7ea5f4d9381049088e3d6a41b6d43ddb
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Enhanced In Vitro Cascade Catalysis of Glycerol into Pyruvate and Acetoin by Integration with Dihydroxy Acid Dehydratase from <i>Paralcaligenes ureilyticus</i>

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