Details
| Original language | English |
|---|---|
| Pages (from-to) | 763-774 |
| Number of pages | 12 |
| Journal | Fungal biology |
| Volume | 121 |
| Issue number | 9 |
| Publication status | Published - 3 Jun 2017 |
Abstract
A decarboxylase (IfPAD) from the ascomycete Isaria farinosa converted ferulic acid to 4-vinylguaiacol (4-VG), a volatile which imparts the distinct “smoke flavor” of pyrolized wood. The activity was enhanced by adding (E)-ferulic acid to the culture medium and peaked with 3.6 U g−1 mycelium (1 μmol 4-VG min−1). The coding sequence of 543 bp was translated into a 25 kDa protein with a homology of 91 % to putative phenolic acid decarboxylases of its teleomorph, Cordyceps militaris, and Beauveria bassiana, the anamorph of Cordyceps bassiana. Cold shock expression in Escherichia coli yielded 411 U g−1 wet mass. Substrate conversion required a hydroxyl substituent para to a trans-unsaturated C3-side chain of the aromatic ring. Km and kcat/Km values were determined to 0.3 mM and 78.4 mM−1s−1 for p-coumaric acid and 1.9 mM and 45.1 mM−1s−1 for (E)-ferulic acid, respectively. The native enzyme and its recombinant counterpart showed pH-optima at pH 6.0 and pH 5.5, and low temperature optima of 19 °C and 14 °C, respectively. IfPAD produced 4-VG from destarched wheat bran and sugar beet fiber, confirming activity on complex plant biomass. This is the first report on the biochemical characterization of a phenolic acid decarboxylase from a filamentous ascomycete.
Keywords
- (E)-ferulic acid, 4-Vinylguaiacol, Biotransformation, Complex plant biomass, Filamentous fungus, PAD family
ASJC Scopus subject areas
- Agricultural and Biological Sciences(all)
- Ecology, Evolution, Behavior and Systematics
- Biochemistry, Genetics and Molecular Biology(all)
- Genetics
- Medicine(all)
- Infectious Diseases
Sustainable Development Goals
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In: Fungal biology, Vol. 121, No. 9, 03.06.2017, p. 763-774.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Cold generation of smoke flavour by the first phenolic acid decarboxylase from a filamentous ascomycete
T2 - Isaria farinosa
AU - Linke, Diana
AU - Riemer, Stephanie
AU - Schimanski, Silke
AU - Nieter, Annabel
AU - Krings, Ulrich
AU - Berger, Ralf G.
PY - 2017/6/3
Y1 - 2017/6/3
N2 - A decarboxylase (IfPAD) from the ascomycete Isaria farinosa converted ferulic acid to 4-vinylguaiacol (4-VG), a volatile which imparts the distinct “smoke flavor” of pyrolized wood. The activity was enhanced by adding (E)-ferulic acid to the culture medium and peaked with 3.6 U g−1 mycelium (1 μmol 4-VG min−1). The coding sequence of 543 bp was translated into a 25 kDa protein with a homology of 91 % to putative phenolic acid decarboxylases of its teleomorph, Cordyceps militaris, and Beauveria bassiana, the anamorph of Cordyceps bassiana. Cold shock expression in Escherichia coli yielded 411 U g−1 wet mass. Substrate conversion required a hydroxyl substituent para to a trans-unsaturated C3-side chain of the aromatic ring. Km and kcat/Km values were determined to 0.3 mM and 78.4 mM−1s−1 for p-coumaric acid and 1.9 mM and 45.1 mM−1s−1 for (E)-ferulic acid, respectively. The native enzyme and its recombinant counterpart showed pH-optima at pH 6.0 and pH 5.5, and low temperature optima of 19 °C and 14 °C, respectively. IfPAD produced 4-VG from destarched wheat bran and sugar beet fiber, confirming activity on complex plant biomass. This is the first report on the biochemical characterization of a phenolic acid decarboxylase from a filamentous ascomycete.
AB - A decarboxylase (IfPAD) from the ascomycete Isaria farinosa converted ferulic acid to 4-vinylguaiacol (4-VG), a volatile which imparts the distinct “smoke flavor” of pyrolized wood. The activity was enhanced by adding (E)-ferulic acid to the culture medium and peaked with 3.6 U g−1 mycelium (1 μmol 4-VG min−1). The coding sequence of 543 bp was translated into a 25 kDa protein with a homology of 91 % to putative phenolic acid decarboxylases of its teleomorph, Cordyceps militaris, and Beauveria bassiana, the anamorph of Cordyceps bassiana. Cold shock expression in Escherichia coli yielded 411 U g−1 wet mass. Substrate conversion required a hydroxyl substituent para to a trans-unsaturated C3-side chain of the aromatic ring. Km and kcat/Km values were determined to 0.3 mM and 78.4 mM−1s−1 for p-coumaric acid and 1.9 mM and 45.1 mM−1s−1 for (E)-ferulic acid, respectively. The native enzyme and its recombinant counterpart showed pH-optima at pH 6.0 and pH 5.5, and low temperature optima of 19 °C and 14 °C, respectively. IfPAD produced 4-VG from destarched wheat bran and sugar beet fiber, confirming activity on complex plant biomass. This is the first report on the biochemical characterization of a phenolic acid decarboxylase from a filamentous ascomycete.
KW - (E)-ferulic acid
KW - 4-Vinylguaiacol
KW - Biotransformation
KW - Complex plant biomass
KW - Filamentous fungus
KW - PAD family
UR - http://www.scopus.com/inward/record.url?scp=85021246015&partnerID=8YFLogxK
U2 - 10.1016/j.funbio.2017.05.006
DO - 10.1016/j.funbio.2017.05.006
M3 - Article
C2 - 28800848
AN - SCOPUS:85021246015
VL - 121
SP - 763
EP - 774
JO - Fungal biology
JF - Fungal biology
SN - 1878-6146
IS - 9
ER -