Ethyl acetate production by the elusive alcohol acetyltransferase from yeast

Alex Kruis*, Mark Levisson, Astrid E. Mars, Max van der Ploeg, Fernando Garcés Daza, Valeria Ellena, Servé W.M. Kengen, John van der Oost, Ruud A. Weusthuis

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

28 Citations (Scopus)

Abstract

Ethyl acetate is an industrially relevant ester that is currently produced exclusively through unsustainable processes. Many yeasts are able to produce ethyl acetate, but the main responsible enzyme has remained elusive, hampering the engineering of novel production strains. Here we describe the discovery of a new enzyme (Eat1) from the yeast Wickerhamomyces anomalus that resulted in high ethyl acetate production when expressed in Saccharomyces cerevisiae and Escherichia coli. Purified Eat1 showed alcohol acetyltransferase activity with ethanol and acetyl-CoA. Homologs of eat1 are responsible for most ethyl acetate synthesis in known ethyl acetate-producing yeasts, including S. cerevisiae, and are only distantly related to known alcohol acetyltransferases. Eat1 is therefore proposed to compose a novel alcohol acetyltransferase family within the α/β hydrolase superfamily. The discovery of this novel enzyme family is a crucial step towards the development of biobased ethyl acetate production and will also help in selecting improved S. cerevisiae brewing strains.
Original languageEnglish
Pages (from-to)92-101
JournalMetabolic Engineering
Volume41
DOIs
Publication statusPublished - 2017

Fingerprint

Acetyltransferases
Yeast
Alcohols
Yeasts
Saccharomyces cerevisiae
Enzymes
Brewing
Hydrolases
Acetyl Coenzyme A
Escherichia coli
ethyl acetate
Esters
Ethanol

Keywords

  • Alcohol acetyltransferase
  • Escherichia coli
  • Ethyl acetate
  • Saccharomyces cerevisiae
  • yeast
  • α/β hydrolase

Cite this

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title = "Ethyl acetate production by the elusive alcohol acetyltransferase from yeast",
abstract = "Ethyl acetate is an industrially relevant ester that is currently produced exclusively through unsustainable processes. Many yeasts are able to produce ethyl acetate, but the main responsible enzyme has remained elusive, hampering the engineering of novel production strains. Here we describe the discovery of a new enzyme (Eat1) from the yeast Wickerhamomyces anomalus that resulted in high ethyl acetate production when expressed in Saccharomyces cerevisiae and Escherichia coli. Purified Eat1 showed alcohol acetyltransferase activity with ethanol and acetyl-CoA. Homologs of eat1 are responsible for most ethyl acetate synthesis in known ethyl acetate-producing yeasts, including S. cerevisiae, and are only distantly related to known alcohol acetyltransferases. Eat1 is therefore proposed to compose a novel alcohol acetyltransferase family within the α/β hydrolase superfamily. The discovery of this novel enzyme family is a crucial step towards the development of biobased ethyl acetate production and will also help in selecting improved S. cerevisiae brewing strains.",
keywords = "Alcohol acetyltransferase, Escherichia coli, Ethyl acetate, Saccharomyces cerevisiae, yeast, α/β hydrolase",
author = "Alex Kruis and Mark Levisson and Mars, {Astrid E.} and {van der Ploeg}, Max and {Garc{\'e}s Daza}, Fernando and Valeria Ellena and Kengen, {Serv{\'e} W.M.} and {van der Oost}, John and Weusthuis, {Ruud A.}",
year = "2017",
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language = "English",
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pages = "92--101",
journal = "Metabolic Engineering",
issn = "1096-7176",
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Ethyl acetate production by the elusive alcohol acetyltransferase from yeast. / Kruis, Alex; Levisson, Mark; Mars, Astrid E.; van der Ploeg, Max; Garcés Daza, Fernando; Ellena, Valeria; Kengen, Servé W.M.; van der Oost, John; Weusthuis, Ruud A.

In: Metabolic Engineering, Vol. 41, 2017, p. 92-101.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Ethyl acetate production by the elusive alcohol acetyltransferase from yeast

AU - Kruis, Alex

AU - Levisson, Mark

AU - Mars, Astrid E.

AU - van der Ploeg, Max

AU - Garcés Daza, Fernando

AU - Ellena, Valeria

AU - Kengen, Servé W.M.

AU - van der Oost, John

AU - Weusthuis, Ruud A.

PY - 2017

Y1 - 2017

N2 - Ethyl acetate is an industrially relevant ester that is currently produced exclusively through unsustainable processes. Many yeasts are able to produce ethyl acetate, but the main responsible enzyme has remained elusive, hampering the engineering of novel production strains. Here we describe the discovery of a new enzyme (Eat1) from the yeast Wickerhamomyces anomalus that resulted in high ethyl acetate production when expressed in Saccharomyces cerevisiae and Escherichia coli. Purified Eat1 showed alcohol acetyltransferase activity with ethanol and acetyl-CoA. Homologs of eat1 are responsible for most ethyl acetate synthesis in known ethyl acetate-producing yeasts, including S. cerevisiae, and are only distantly related to known alcohol acetyltransferases. Eat1 is therefore proposed to compose a novel alcohol acetyltransferase family within the α/β hydrolase superfamily. The discovery of this novel enzyme family is a crucial step towards the development of biobased ethyl acetate production and will also help in selecting improved S. cerevisiae brewing strains.

AB - Ethyl acetate is an industrially relevant ester that is currently produced exclusively through unsustainable processes. Many yeasts are able to produce ethyl acetate, but the main responsible enzyme has remained elusive, hampering the engineering of novel production strains. Here we describe the discovery of a new enzyme (Eat1) from the yeast Wickerhamomyces anomalus that resulted in high ethyl acetate production when expressed in Saccharomyces cerevisiae and Escherichia coli. Purified Eat1 showed alcohol acetyltransferase activity with ethanol and acetyl-CoA. Homologs of eat1 are responsible for most ethyl acetate synthesis in known ethyl acetate-producing yeasts, including S. cerevisiae, and are only distantly related to known alcohol acetyltransferases. Eat1 is therefore proposed to compose a novel alcohol acetyltransferase family within the α/β hydrolase superfamily. The discovery of this novel enzyme family is a crucial step towards the development of biobased ethyl acetate production and will also help in selecting improved S. cerevisiae brewing strains.

KW - Alcohol acetyltransferase

KW - Escherichia coli

KW - Ethyl acetate

KW - Saccharomyces cerevisiae

KW - yeast

KW - α/β hydrolase

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