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, Vol. 72, No. 19, 15.05.2024, p. 11002-11012.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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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 -