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Novel Catechol O-methyltransferases from Lentinula edodes Catalyze the Generation of Taste-Active Flavonoids

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Novel Catechol O-methyltransferases from Lentinula edodes Catalyze the Generation of Taste-Active Flavonoids. / Kanter, Jean-Philippe; Milke, Lars; Metz, Judith K; Biabani, Ali; Schlüter, Hartmut; Gand, Martin; Ley, Jakob P; Zorn, Holger.

in: J AGR FOOD CHEM, Jahrgang 72, Nr. 19, 15.05.2024, S. 11002-11012.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Kanter, J-P, Milke, L, Metz, JK, Biabani, A, Schlüter, H, Gand, M, Ley, JP & Zorn, H 2024, 'Novel Catechol O-methyltransferases from Lentinula edodes Catalyze the Generation of Taste-Active Flavonoids', J AGR FOOD CHEM, Jg. 72, Nr. 19, S. 11002-11012. https://doi.org/10.1021/acs.jafc.4c01514

APA

Kanter, J-P., Milke, L., Metz, J. K., Biabani, A., Schlüter, H., Gand, M., Ley, J. P., & Zorn, H. (2024). Novel Catechol O-methyltransferases from Lentinula edodes Catalyze the Generation of Taste-Active Flavonoids. J AGR FOOD CHEM, 72(19), 11002-11012. https://doi.org/10.1021/acs.jafc.4c01514

Vancouver

Kanter J-P, Milke L, Metz JK, Biabani A, Schlüter H, Gand M et al. Novel Catechol O-methyltransferases from Lentinula edodes Catalyze the Generation of Taste-Active Flavonoids. J AGR FOOD CHEM. 2024 Mai 15;72(19):11002-11012. https://doi.org/10.1021/acs.jafc.4c01514

Bibtex

@article{33340610671f4de7bd85afa7146e5733,
title = "Novel Catechol O-methyltransferases from Lentinula edodes Catalyze the Generation of Taste-Active Flavonoids",
abstract = "Due to the increasing demand for natural food ingredients, including taste-active compounds, enzyme-catalyzed conversions of natural substrates, such as flavonoids, are promising tools to align with the principles of Green Chemistry. In this study, a novel O-methyltransferase activity was identified in the mycelium of Lentinula edodes, which was successfully applied to generate the taste-active flavonoids hesperetin, hesperetin dihydrochalcone, homoeriodictyol, and homoeriodictyol dihydrochalcone. Furthermore, the mycelium-mediated OMT activity allowed for the conversion of various catecholic substrates, yielding their respective (iso-)vanilloids, while monohydroxylated compounds were not converted. By means of a bottom-up proteomics approach, three putative O-methyltransferases were identified, and subsequently, synthetic, codon-optimized genes were heterologously expressed in Escherichia coli. The purified enzymes confirmed the biocatalytic O-methylation activity against targeted flavonoids containing catechol motifs.",
keywords = "Shiitake Mushrooms/enzymology, Catechol O-Methyltransferase/genetics, Fungal Proteins/genetics, Flavonoids/chemistry, Biocatalysis, Flavoring Agents/metabolism, Mycelium/enzymology, Substrate Specificity",
author = "Jean-Philippe Kanter and Lars Milke and Metz, {Judith K} and Ali Biabani and Hartmut Schl{\"u}ter and Martin Gand and Ley, {Jakob P} and Holger Zorn",
year = "2024",
month = may,
day = "15",
doi = "10.1021/acs.jafc.4c01514",
language = "English",
volume = "72",
pages = "11002--11012",
journal = "J AGR FOOD CHEM",
issn = "0021-8561",
publisher = "American Chemical Society",
number = "19",

}

RIS

TY - JOUR

T1 - Novel Catechol O-methyltransferases from Lentinula edodes Catalyze the Generation of Taste-Active Flavonoids

AU - Kanter, Jean-Philippe

AU - Milke, Lars

AU - Metz, Judith K

AU - Biabani, Ali

AU - Schlüter, Hartmut

AU - Gand, Martin

AU - Ley, Jakob P

AU - Zorn, Holger

PY - 2024/5/15

Y1 - 2024/5/15

N2 - Due to the increasing demand for natural food ingredients, including taste-active compounds, enzyme-catalyzed conversions of natural substrates, such as flavonoids, are promising tools to align with the principles of Green Chemistry. In this study, a novel O-methyltransferase activity was identified in the mycelium of Lentinula edodes, which was successfully applied to generate the taste-active flavonoids hesperetin, hesperetin dihydrochalcone, homoeriodictyol, and homoeriodictyol dihydrochalcone. Furthermore, the mycelium-mediated OMT activity allowed for the conversion of various catecholic substrates, yielding their respective (iso-)vanilloids, while monohydroxylated compounds were not converted. By means of a bottom-up proteomics approach, three putative O-methyltransferases were identified, and subsequently, synthetic, codon-optimized genes were heterologously expressed in Escherichia coli. The purified enzymes confirmed the biocatalytic O-methylation activity against targeted flavonoids containing catechol motifs.

AB - Due to the increasing demand for natural food ingredients, including taste-active compounds, enzyme-catalyzed conversions of natural substrates, such as flavonoids, are promising tools to align with the principles of Green Chemistry. In this study, a novel O-methyltransferase activity was identified in the mycelium of Lentinula edodes, which was successfully applied to generate the taste-active flavonoids hesperetin, hesperetin dihydrochalcone, homoeriodictyol, and homoeriodictyol dihydrochalcone. Furthermore, the mycelium-mediated OMT activity allowed for the conversion of various catecholic substrates, yielding their respective (iso-)vanilloids, while monohydroxylated compounds were not converted. By means of a bottom-up proteomics approach, three putative O-methyltransferases were identified, and subsequently, synthetic, codon-optimized genes were heterologously expressed in Escherichia coli. The purified enzymes confirmed the biocatalytic O-methylation activity against targeted flavonoids containing catechol motifs.

KW - Shiitake Mushrooms/enzymology

KW - Catechol O-Methyltransferase/genetics

KW - Fungal Proteins/genetics

KW - Flavonoids/chemistry

KW - Biocatalysis

KW - Flavoring Agents/metabolism

KW - Mycelium/enzymology

KW - Substrate Specificity

U2 - 10.1021/acs.jafc.4c01514

DO - 10.1021/acs.jafc.4c01514

M3 - SCORING: Journal article

C2 - 38700031

VL - 72

SP - 11002

EP - 11012

JO - J AGR FOOD CHEM

JF - J AGR FOOD CHEM

SN - 0021-8561

IS - 19

ER -