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Information on EC 2.3.1.84 - alcohol O-acetyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P40353
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EC Tree
2.3.1.84 alcohol O-acetyltransferaseIUBMB Comments
Acts on a range of short-chain aliphatic alcohols, including methanol and ethanol
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Word Map
- 2.3.1.84
-
isoamyl
-
sake
- fruity
-
kyokai
- tatase
-
2-phenylethyl
- uvarum
-
wickerhamomyces
- l-asp
-
self-cloning
- synthesis
- hanseniaspora
-
acetate-producing
-
brewery
- biotechnology
- nutrition
- analysis
- food industry
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
aatase, alcohol acetyltransferase, lg-atf1, alcohol acetyltransferase atf1, phcfat, aatfase, cfat1, coniferyl alcohol acetyltransferase, alcohol acetyl transferase i, rhaat, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetyltransferase, alcohol
-
-
-
-
alcohol acetyltransferase
ATF1
alcohol acetyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:alcohol O-acetyltransferase
Acts on a range of short-chain aliphatic alcohols, including methanol and ethanol
CAS REGISTRY NUMBER
COMMENTARY
80237-89-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + (Z)-11-tetradecen-1-ol
CoA + (Z)-11-tetradecenyl acetate
-
-
-
?
acetyl-CoA + (Z)-9-dodecen-1-ol
CoA + (Z)-9-dodecenyl acetate
-
-
-
?
acetyl-CoA + (Z)-9-hexadecen-1-ol
CoA + (Z)-9-hexadecenyl acetate
-
-
-
?
acetyl-CoA + (Z)-9-tetradecen-1-ol
CoA + (Z)-9-tetradecenyl acetate
-
-
-
?
acetyl-CoA + indole-3-ethanol
CoA + indole-3-ethanol acetate
-
-
-
-
?
isoamylalcohol + acetyl-CoA
isoamyl acetate + CoA
-
-
-
-
?
isoamylalcohol + acetyl-CoA
isoamyl acetate + CoA
-
slightly higher activity with straight-chain alcohols than with branched-chain alcohols, activity with straight-chain alcohols in descending order: pentanol, butanol, propanol, very low activity with ethanol, activity with branched-chain alcohols in descending order of carbon number: C5, C4, C3
-
?
isoamylalcohol + acetyl-CoA
isoamyl acetate + CoA
-
alcohol acetyltransferase 2 is probably the key enzyme in a steroid detoxification mechanism, alcohol acetyltransferase 1 accounts for 80% of isoamyl acetate production and 30% of ethyl acetate production and might be involved in fatty acid metabolism
-
?
additional information
?
-
isoform ATF1 is capable of acetylating moth pheromone fatty alcohols with chain lengths from 10 to 18 carbons with up to 27- and 10-fold higher in vivo and in vitro efficiency, respectiviely, compared to plant-derived diacylglycerol acetyltransferase EaDAcT, EC 2.3.1.20
-
-
?
additional information
?
-
-
isoform ATF1 is capable of acetylating moth pheromone fatty alcohols with chain lengths from 10 to 18 carbons with up to 27- and 10-fold higher in vivo and in vitro efficiency, respectiviely, compared to plant-derived diacylglycerol acetyltransferase EaDAcT, EC 2.3.1.20
-
-
?
additional information
?
-
-
alcohol acetyl transferase gene ATF1 is a target of the cAMP/PKA and FGM nutrient-signalling pathways, ATF1 is repressed by heat and ethanol stress
-
-
?
additional information
?
-
expression levels of the yeast alcohol acetyltransferase genes ATF1, Lg-ATF1, and ATF2 control the formation of a broad range of volatile esters
-
-
?
additional information
?
-
-
expression levels of the yeast alcohol acetyltransferase genes ATF1, Lg-ATF1, and ATF2 control the formation of a broad range of volatile esters
-
-
?
additional information
?
-
-
localization of Atf1p in lipid particles may indicate that Atf1p has a specific role in the lipid and/or sterol metabolism that takes place in these particles
-
-
?
additional information
?
-
-
Atf1 uses acetyl-CoA to synthesize acetate esters from all of the alcohols tested. Atf1 is specific for acetyl-CoA. Additionally, Atf1 can hydrolyse all of the acyl-CoA substrates tested, with a clear preference for C8 chain lengths
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + indole-3-ethanol
CoA + indole-3-ethanol acetate
-
-
-
-
?
isoamylalcohol + acetyl-CoA
isoamyl acetate + CoA
-
alcohol acetyltransferase 2 is probably the key enzyme in a steroid detoxification mechanism, alcohol acetyltransferase 1 accounts for 80% of isoamyl acetate production and 30% of ethyl acetate production and might be involved in fatty acid metabolism
-
?
additional information
?
-
-
alcohol acetyl transferase gene ATF1 is a target of the cAMP/PKA and FGM nutrient-signalling pathways, ATF1 is repressed by heat and ethanol stress
-
-
?
additional information
?
-
expression levels of the yeast alcohol acetyltransferase genes ATF1, Lg-ATF1, and ATF2 control the formation of a broad range of volatile esters
-
-
?
additional information
?
-
-
expression levels of the yeast alcohol acetyltransferase genes ATF1, Lg-ATF1, and ATF2 control the formation of a broad range of volatile esters
-
-
?
additional information
?
-
-
localization of Atf1p in lipid particles may indicate that Atf1p has a specific role in the lipid and/or sterol metabolism that takes place in these particles
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
oxygen
-
inhibits activity to a greater extent for isoamylacetate production than for ethyl acetate production
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
sequence of strain S288c which is about 99% homologous to strain 38
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
AATase for ethyl acetate peaks at the beginning of the exponential growth phase and that for isoamylacetate at its end
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
alcohol acetyltransferase 1 is located within the cellular vacuoles
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the sequence of Saccharomyces cerevisiae strain S288c is about 99% homologous to Saccharomyces cerevisiae strain 38
physiological function
alcohol acetyltransferase (AATFase) extensively catalyzes the reactions of alcohols to acetic esters in microorganisms and plants
physiological function
-
after 5 days of fermentation, the concentrations of ethyl acetate, isoamyl acetate, and isobutyl acetate in yellow rice wines fermented with yeasts overexpressing isoform ATF2 increase to 137.79 mg/L (an approximate 4.9fold increase relative to the parent cell), 26.68 mg/L, and 7.60 mg/L, respectively
additional information
additional information
-
method development for quantification of the activity of AATFase using a SnO2-based sensor of electronic nose, which is determined on the basis of its higher sensitivity for the reducing alcohol compared to the oxidizing ester, e-nose measurements method, overview
additional information
method development for quantification of the activity of AATFase using a SnO2-based sensor of electronic nose, which is determined on the basis of its higher sensitivity for the reducing alcohol compared to the oxidizing ester, e-nose measurements method, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
140000
-
gel filtration, protein-detergent complex comprising an Atf1 monomer of 65 kDa associated with the Thesit micelle
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E509A/E512A/E513A
-
mutation in isoform Atf1, mutated protein shows 84% localization to lipid droplets
L511A/L514A/Y518A/L512A
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mutation in isoform Atf1, loss of membrane association
R22A/R23A/R36A
-
mutation in isoform Atf2, protein is localized in the cytoplasm
W518A/F521/I529A/F532A R36A
-
mutation in isoform Atf2, protein is localized in the cytoplasm
additional information
additional information
-
truncation of amphipathic helices within the N- and C-terminal domains of isoform Atf1 (residues 24-41 and 508-525) impair endoplasmic reticulum localization and membrane association. Mutations of the basic or hydrophobic residues in the N-terminal helix and hydrophobic residues in the C-terminal helix of Atf1 disrupt ER association and subsequent sorting from the ER to lipid droplets. Similar amphipathic helices are found at both ends of isoform Atf2, enabling ER and lipid droplet association. Mutations to the N- and C-terminal helices of Atf2 prevent membrane association
additional information
-
reconstruction of the engineered pathways for production of indole-3-ethanol and indole-3-ethanol acetate from glucose in Escherichia coli strain MG1655, enzyme ATF1 is included catalyzing the formation of indole-3-ethanol acetate from indole-3-ethanol, pathway and method evaluation, overview
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
30
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PBE 94 column, DEAE-cellulose, Toypearl HW60, hydroxyapatite, octyl Sepharose
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a pPTB construct is used, expression experiments are performed in Escherichia coli cells
-
cloned from the VIN13 commercial wine yeast strain, and placed under the constitutive control of the PGK1 regulatory sequences to generate plasmids pATF2-s. Overexpression of ATF2 in vine yeast increased the concentrations of ethyl acetate and isoamyl acetate to a lesser degree than overexpression of ATF1
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cloned from the VIN13 commercial wine yeast strain, and placed under the constitutive control of the PGK1 regulatory sequences. Overexpression of ATF1 in vine yeast significantly increased the concentrations of ethyl acetate, isoamyl acetate, 2-phenylethyl acetate and ethyl caproate
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cloning of ATF1 gene encoding alcohol acetyltransferase, expression in Saccharomyces cerevisiae
-
cloning of the ATF1 gene encoding alcohol acetyltransferase 1 from wine yeast
-
expression in Escherichia coli and in Clostridium acetobutylicum, alcohol acetyltransferase AFT2
-
gene atf1, recombinant coexpression of the enzyme with genes YjgB, KDC, ARO8, SerA, ARoG, and TrpABCD from Saccharomyces cerevisiae strain YPH499 in Escherichia coli strain MG1655 to establish the production of indole-3-ethanol and indole-3-ethanol acetate from glucose, method, overview. Subcloning in Escherichia coli strain DH1013
-
into the pBAD-TOPO vector, furthermore a pTRC construct is used, expression experiments are performed in Escherichia coli cells
-
overexpression of ATF1p-GFP fusion protein in Sacharomyces cerevisiae
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
analysis
method to quantify the activity of alcohol acetyltransferase using a SnO2-based sensor of electronic nose, on the basis of its higher sensitivity to the reducing alcohol than the oxidizing ester. The method has been successfully applied to determine the alcohol acetyltransferase activity of a cider yeast strain
biotechnology
food industry
-
after 5 days of fermentation, the concentrations of ethyl acetate, isoamyl acetate, and isobutyl acetate in yellow rice wines fermented with yeasts overexpressing isoform ATF2 increase to 137.79 mg/L (an approximate 4.9fold increase relative to the parent cell), 26.68 mg/L, and 7.60 mg/L, respectively
nutrition
-
polishing of rice for use in sake brewing is necessary to remove inositol from rice, thereby increasing AATase activity. A high AATase activity leads to an abundance of acetate esters of higher alcohols in sake, such as isoamyl acetate, one of the most favorable odor-enhancing compounds
synthesis
synthesis
engineering of Escherichia coli to produce biodiesel, which depends on the expression of Saccharomyces cerevisiae alcohol acetyltransferase ATF1, fatty acyl-ACP reductase from Synechococcus elongates, carboxylic acid reductase from Mycobacterium marinum, fatty acyl-CoA reductase from Marinobacter aquaeolei, aldehyde reductase from Escherichia coli, fatty acyl-CoA synthetase from Escherichia coli, and TesA, a truncated fatty acyl-ACP thioesterase from Escherichia coli
synthesis
production of acetate esters by a mutant alpha5 strain overexpressing ATF1 with aminotransferase BAT2 deletion is 1353.4 mg/l, which is 43.16fold higher than that by the original strain. Isoform ATF1 overexpression with BAT2 deletion can further increase the ratio of ester to higher alcohol to a greater extent than isoform ATF2 overexpression with BAT2 deletion
biotechnology
-
a low-cost fermentation process for isoamyl acetate biosynthesis by overexpressing the yeast alcohol acetyl-transferase AFT1 in Escherichia coli is developed
biotechnology
-
a low-cost fermentation process for isoamyl acetate biosynthesis by overexpressing the yeast alcohol acetyl-transferase AFT2 in Escherichia coli is developed
synthesis
-
overexpression of ATF1 in Chinese liquor yeast through precise and seamless insertion of PGK1 promoter. In the liquid fermentation of corn hydrolysate, both mRNA level and alcohol acetyltransferase activity of ATF1 in mutant are pronounced higher than the parental strain. Productivity of ethyl acetate increases from 25.04 to 78.76 mg/l
synthesis
production of acetate esters by a mutant alpha5 strain overexpressing ATF1 with aminotransferase BAT2 deletion is 73.4 mg/l, which is 2.34fold higher than that by the original strain. Isoform ATF1 overexpression with BAT2 deletion can further increase the ratio of ester to higher alcohol to a greater extent than isoform ATF2 overexpression with BAT2 deletion
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Akita, O.; Suzuki, S.; Obata, T.
Purification and some properties of alcohol acetyltransferase from sake yeast
Agric. Biol. Chem.
54
1485-1490
1990
Saccharomyces cerevisiae
-
Minetoki, T.; Bogaki, T.; Iwamatsu, A.; Fujii, T.; Hamachi, M.
The purification, properties and internal peptide sequences of alcohol acetyltransferase isolated from Saccharomyces cerevisiae Kyokai No. 7
Biosci. Biotechnol. Biochem.
57
2094-2098
1993
Cladosporium cladosporioides, Saccharomyces cerevisiae
Fujii, T.; Nagasawa, N.; Iwamatsu, A.; Bogaki, T.; Tamai, Y.; Hamachi, M.
Molecular cloning, sequence analysis, and expression of the yeast alcohol acetyltransferase gene
Appl. Environ. Microbiol.
60
2786-2792
1994
Saccharomyces cerevisiae, Saccharomyces uvarum
Del Carmen Plata, M.; Mauricio, J.C.; Millan, C.; Ortega, J.M.
In vitro specific activity of alcohol acetyltransferase and esterase in two flor yeast strains during biological aging of sherry wines
J. Ferment. Bioeng.
85
369-374
1998
Saccharomyces cerevisiae
-
Fukuda, K.; Yamamoto, N.; Kiyokawa, Y.; Yanagiuchi, T.; Wakai, Y.; Kitamoto, K.; Inoue, Y.; Kimura, A.
Balance of activities of alcohol acetyltransferase and esterase in Saccharomyces cerevisiae is important for production of isoamyl acetate
Appl. Environ. Microbiol.
64
4076-4078
1998
Cyberlindnera mrakii, Saccharomyces cerevisiae
Mason, A.B.; Dufour, J.P.
Alcohol acetyltransferases and the significance of ester synthesis in yeast
Yeast
16
1287-1298
2000
Saccharomyces cerevisiae, Saccharomyces pastorianus
Lilly, M.; Lambrechts, M.G.; Pretorius, I.S.
Effect of increased yeast alcohol acetyltransferase activity on flavor profiles of wine and distillates
Appl. Environ. Microbiol.
66
744-753
2000
Saccharomyces cerevisiae
Verstrepen, K.J.; Van Laere, S.D.; Vanderhaegen, B.M.; Derdelinckx, G.; Dufour, J.P.; Pretorius, I.S.; Winderickx, J.; Thevelein, J.M.; Delvaux, F.R.
Expression levels of the yeast alcohol acetyltransferase genes ATF1, Lg-ATF1, and ATF2 control the formation of a broad range of volatile esters
Appl. Environ. Microbiol.
69
5228-5237
2003
Saccharomyces cerevisiae (Q6XBT0), Saccharomyces cerevisiae
Verstrepen, K.J.; Derdelinckx, G.; Dufour, J.P.; Winderickx, J.; Pretorius, I.S.; Thevelein, J.M.; Delvaux, F.R.
The Saccharomyces cerevisiae alcohol acetyl transferase gene ATF1 is a target of the cAMP/PKA and FGM nutrient-signalling pathways
FEMS Yeast Res.
4
285-296
2003
Saccharomyces cerevisiae
Furukawa, K.; Yamada, T.; Mizoguchi, H.; Hara, S.
Increased alcohol acetyltransferase activity by inositol limitation in Saccharomyces cerevisiae in sake mash
J. Biosci. Bioeng.
96
380-386
2003
Saccharomyces cerevisiae
Horton, C.E.; Huang, K.X.; Bennett, G.N.; Rudolph, F.B.
Heterologous expression of the Saccharomyces cerevisiae alcohol acetyltransferase genes in Clostridium acetobutylicum and Escherichia coli for the production of isoamyl acetate
J. Ind. Microbiol. Biotechnol.
30
427-432
2003
Saccharomyces cerevisiae
Plata, C.; Mauricio, J.C.; Millan, C.; Ortega, J.M.
Influence of glucose and oxygen on the production of ethyl acetate and isoamyl acetate by a Saccharomyces cerevisiae strain during alcoholic fermentation
World J. Microbiol. Biotechnol.
21
115-121
2005
Saccharomyces cerevisiae
-
Verstrepen, K.J.; Van Laere, S.D.; Vercammen, J.; Derdelinckx, G.; Dufour, J.P.; Pretorius, I.S.; Winderickx, J.; Thevelein, J.M.; Delvaux, F.R.
The Saccharomyces cerevisiae alcohol acetyl transferase Atf1p is localized in lipid particles
Yeast
21
367-377
2004
Saccharomyces cerevisiae
Hirooka, K.; Yamamoto, Y.; Tsutsui, N.; Tanaka, T.
Improved production of isoamyl acetate by a sake yeast mutant resistant to an isoprenoid analog and its dependence on alcohol acetyltransferase activity, but not on isoamyl alcohol production
J. Biosci. Bioeng.
99
125-129
2005
Saccharomyces cerevisiae
Lilly, M.; Bauer, F.F.; Lambrechts, M.G.; Swiegers, J.H.; Cozzolino, D.; Pretorius, I.S.
The effect of increased yeast alcohol acetyltransferase and esterase activity on the flavour profiles of wine and distillates
Yeast
23
641-659
2006
Saccharomyces cerevisiae
Singh, R.; Vadlani, P.; Harrison, M.; Bennett, G.; San, K.
Aerobic production of isoamyl acetate by overexpression of the yeast alcohol acetyl-transferases AFT1 and AFT2 in Escherichia coli and using low-cost fermentation ingredients
Bioprocess Biosyst. Eng.
31
299-306
2008
Saccharomyces cerevisiae
Guo, D.; Pan, H.; Li, X.
Metabolic engineering of Escherichia coli for production of biodiesel from fatty alcohols and acetyl-CoA
Appl. Microbiol. Biotechnol.
99
7805-7812
2015
Saccharomyces cerevisiae (P40353), Saccharomyces cerevisiae
Zhang, J.; Zhang, C.; Qi, Y.; Dai, L.; Ma, H.; Guo, X.; Xiao, D.
Acetate ester production by Chinese yellow rice wine yeast overexpressing the alcohol acetyltransferase-encoding gene ATF2
Genet. Mol. Res.
13
9735-9746
2014
Saccharomyces cerevisiae
Dong, J.; Xu, H.; Zhao, L.; Chen, Y.; Zhang, C.; Guo, X.; Hou, X.; Chen, D.; Zhang, C.; Xiao, D.
Enhanced acetate ester production of Chinese liquor yeast by overexpressing ATF1 through precise and seamless insertion of PGK1 promoter
J. Ind. Microbiol. Biotechnol.
41
1823-1828
2014
Saccharomyces cerevisiae
Ding, B.J.; Lager, I.; Bansal, S.; Durrett, T.P.; Stymne, S.; Loefstedt, C.
The yeast ATF1 acetyltransferase efficiently acetylates insect pheromone alcohols: implications for the biological production of moth pheromones
Lipids
51
469-475
2016
Saccharomyces cerevisiae (P40353), Saccharomyces cerevisiae
Lin, J.L.; Wheeldon, I.
Dual N- and C-terminal helices are required for endoplasmic reticulum and lipid droplet association of alcohol acetyltransferases in Saccharomyces cerevisiae
PLoS ONE
9
e104141
2014
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4742
Kong, S.; Zhang, J.; Li, X.; Pan, H.; Guo, D.
De novo biosynthesis of indole-3-ethanol and indole-3-ethanol acetate in engineered Escherichia coli
Biochem. Eng. J.
154
107432
2020
Saccharomyces cerevisiae, Saccharomyces cerevisiae YPH499
-
Li, W.; Cui, D.; Wang, J.; Liu, X.; Xu, J.; Zhou, Z.; Zhang, C.; Chen, Y.; Xiao, D.
Overexpression of different alcohol acetyltransferase genes with BAT2 deletion in Saccharomyces cerevisiae affects acetate esters and higher alcohols
Eur. Food Res. Technol.
244
555-564
2018
Saccharomyces cerevisiae (P40353), Saccharomyces cerevisiae (P53296), Saccharomyces cerevisiae ATCC 204508 (P40353), Saccharomyces cerevisiae ATCC 204508 (P53296)
-
Hu, Z.; Li, X.; Wang, H.; Niu, C.; Yuan, Y.; Yue, T.
A novel method to quantify the activity of alcohol acetyltransferase using a SnO2-based sensor of electronic nose
Food Chem.
203
498-504
2016
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P40353), Saccharomyces cerevisiae 38 (P40353), Saccharomyces cerevisiae ATCC 204508 (P40353)
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