Ene-reductase transformation of massoia lactone to δ-decalactone in a continuous-flow reactor

Abstract The demand for natural food flavorings increases every year. Biotransformation has become an attractive approach to obtain natural products. In this work, enantiomerically pure (R)-(+)-δ-decalactone was obtained by reduction of the C=C double bond of natural massoia lactone in a continuous-...

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Autores principales:	Ewa Szczepańska, Danilo Colombo, Francesca Tentori, Teresa Olejniczak, Elisabetta Brenna, Daniela Monti, Filip Boratyński
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/0b131d15a6a9471099c8e1068f64326f
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spelling	oai:doaj.org-article:0b131d15a6a9471099c8e1068f64326f2021-12-02T18:14:00ZEne-reductase transformation of massoia lactone to δ-decalactone in a continuous-flow reactor10.1038/s41598-021-97585-w2045-2322https://doaj.org/article/0b131d15a6a9471099c8e1068f64326f2021-09-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-97585-whttps://doaj.org/toc/2045-2322Abstract The demand for natural food flavorings increases every year. Biotransformation has become an attractive approach to obtain natural products. In this work, enantiomerically pure (R)-(+)-δ-decalactone was obtained by reduction of the C=C double bond of natural massoia lactone in a continuous-flow reactor. Of 13 different ene-reductases isolated, purified and tested, OYE3 was found to be the most efficient biocatalyst. The selected biocatalyst, either in the form of purified enzyme, cell lysate, whole cells or immobilized cells, was tested in the batch system as well as in the packed-bed flow bioreactor. The biotransformation performed in batch mode, using Ca2+-alginate immobilized cells of Escherichia coli BL21(DE3)/pET30a-OYE3, furnished the desired product with complete conversion in 30 min. The process was intensified using a continuous-flow reactor-membrane filtration system (flow 0.1 mL/min, substrate concentration 10 mM, pH 7, 24 °C) with cell lysate as biocatalyst combined with a cofactor regeneration system, which allowed obtaining > 99% bioconversion of massoia lactone.Ewa SzczepańskaDanilo ColomboFrancesca TentoriTeresa OlejniczakElisabetta BrennaDaniela MontiFilip BoratyńskiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-9 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Ewa Szczepańska Danilo Colombo Francesca Tentori Teresa Olejniczak Elisabetta Brenna Daniela Monti Filip Boratyński Ene-reductase transformation of massoia lactone to δ-decalactone in a continuous-flow reactor
description	Abstract The demand for natural food flavorings increases every year. Biotransformation has become an attractive approach to obtain natural products. In this work, enantiomerically pure (R)-(+)-δ-decalactone was obtained by reduction of the C=C double bond of natural massoia lactone in a continuous-flow reactor. Of 13 different ene-reductases isolated, purified and tested, OYE3 was found to be the most efficient biocatalyst. The selected biocatalyst, either in the form of purified enzyme, cell lysate, whole cells or immobilized cells, was tested in the batch system as well as in the packed-bed flow bioreactor. The biotransformation performed in batch mode, using Ca2+-alginate immobilized cells of Escherichia coli BL21(DE3)/pET30a-OYE3, furnished the desired product with complete conversion in 30 min. The process was intensified using a continuous-flow reactor-membrane filtration system (flow 0.1 mL/min, substrate concentration 10 mM, pH 7, 24 °C) with cell lysate as biocatalyst combined with a cofactor regeneration system, which allowed obtaining > 99% bioconversion of massoia lactone.
format	article
author	Ewa Szczepańska Danilo Colombo Francesca Tentori Teresa Olejniczak Elisabetta Brenna Daniela Monti Filip Boratyński
author_facet	Ewa Szczepańska Danilo Colombo Francesca Tentori Teresa Olejniczak Elisabetta Brenna Daniela Monti Filip Boratyński
author_sort	Ewa Szczepańska
title	Ene-reductase transformation of massoia lactone to δ-decalactone in a continuous-flow reactor
title_short	Ene-reductase transformation of massoia lactone to δ-decalactone in a continuous-flow reactor
title_full	Ene-reductase transformation of massoia lactone to δ-decalactone in a continuous-flow reactor
title_fullStr	Ene-reductase transformation of massoia lactone to δ-decalactone in a continuous-flow reactor
title_full_unstemmed	Ene-reductase transformation of massoia lactone to δ-decalactone in a continuous-flow reactor
title_sort	ene-reductase transformation of massoia lactone to δ-decalactone in a continuous-flow reactor
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/0b131d15a6a9471099c8e1068f64326f
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Ene-reductase transformation of massoia lactone to δ-decalactone in a continuous-flow reactor

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