Details
| Original language | English |
|---|---|
| Pages (from-to) | 9944-9950 |
| Number of pages | 7 |
| Journal | Journal of Agricultural and Food Chemistry |
| Volume | 57 |
| Issue number | 21 |
| Publication status | Published - 9 Oct 2009 |
Abstract
The enzymatic conversion of a-pinene to verbenols, verbenone, and minor volatile flavors was studied using submerged cultured cells, lyophilisate, and microsomal fractions of the edible basidiomycete Pleurotos sapidus. The similarity of the product range obtained by the bioconversions with the range of products found after autoxidatlon of α-pinene at 100 °C suggested similar initial pinene radicals. Extracts of the bioconversions were analyzed using thin layer chromatography with hydroperoxide staining and cool on-column capillary gas chromatography-mass spectrometry. Two isomer a-pinene hydroperoxides were identified as the key intermediates and their structures confirmed by comparison with synthesized reference samples and by microchemical reduction to (Z)- and (E)-verbenol. When the biocatalysts were supplemented with one of the verbenols, only the (ZHsomer was oxidized, indicating the activity of a highly stereospecific monoterpenol dehydrogenase. The structural comparison of subunits shows that fungal oxifunctionalization reactions of some common terpene substrates, such as (+)-Hmonene or (+)-valencene, might likewise be catalyzed by dloxygenases rather than by CYP450 enzymes, as previously assumed.
Keywords
- α-plnene dioxygenase, Autoxldatlon, Hydroperoxides, Pleurotos sapidus, Stereoselective verbenol dehydrogenase
ASJC Scopus subject areas
- Chemistry(all)
- General Chemistry
- Agricultural and Biological Sciences(all)
- General Agricultural and Biological Sciences
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In: Journal of Agricultural and Food Chemistry, Vol. 57, No. 21, 09.10.2009, p. 9944-9950.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Autoxidation versus biotransformation of a-pinene to flavors with pleurotus sapidus
T2 - regioselective hydroperoxidation of a-pinene and stereoselective dehydrogenation of verbenol
AU - Krings, Ulrich
AU - Lehnert, Nicole
AU - Fraatz, Marco A.
AU - Hardebusch, Björn
AU - Zorn, Holger
AU - Berger, Ralf G.
PY - 2009/10/9
Y1 - 2009/10/9
N2 - The enzymatic conversion of a-pinene to verbenols, verbenone, and minor volatile flavors was studied using submerged cultured cells, lyophilisate, and microsomal fractions of the edible basidiomycete Pleurotos sapidus. The similarity of the product range obtained by the bioconversions with the range of products found after autoxidatlon of α-pinene at 100 °C suggested similar initial pinene radicals. Extracts of the bioconversions were analyzed using thin layer chromatography with hydroperoxide staining and cool on-column capillary gas chromatography-mass spectrometry. Two isomer a-pinene hydroperoxides were identified as the key intermediates and their structures confirmed by comparison with synthesized reference samples and by microchemical reduction to (Z)- and (E)-verbenol. When the biocatalysts were supplemented with one of the verbenols, only the (ZHsomer was oxidized, indicating the activity of a highly stereospecific monoterpenol dehydrogenase. The structural comparison of subunits shows that fungal oxifunctionalization reactions of some common terpene substrates, such as (+)-Hmonene or (+)-valencene, might likewise be catalyzed by dloxygenases rather than by CYP450 enzymes, as previously assumed.
AB - The enzymatic conversion of a-pinene to verbenols, verbenone, and minor volatile flavors was studied using submerged cultured cells, lyophilisate, and microsomal fractions of the edible basidiomycete Pleurotos sapidus. The similarity of the product range obtained by the bioconversions with the range of products found after autoxidatlon of α-pinene at 100 °C suggested similar initial pinene radicals. Extracts of the bioconversions were analyzed using thin layer chromatography with hydroperoxide staining and cool on-column capillary gas chromatography-mass spectrometry. Two isomer a-pinene hydroperoxides were identified as the key intermediates and their structures confirmed by comparison with synthesized reference samples and by microchemical reduction to (Z)- and (E)-verbenol. When the biocatalysts were supplemented with one of the verbenols, only the (ZHsomer was oxidized, indicating the activity of a highly stereospecific monoterpenol dehydrogenase. The structural comparison of subunits shows that fungal oxifunctionalization reactions of some common terpene substrates, such as (+)-Hmonene or (+)-valencene, might likewise be catalyzed by dloxygenases rather than by CYP450 enzymes, as previously assumed.
KW - α-plnene dioxygenase
KW - Autoxldatlon
KW - Hydroperoxides
KW - Pleurotos sapidus
KW - Stereoselective verbenol dehydrogenase
UR - http://www.scopus.com/inward/record.url?scp=70449103488&partnerID=8YFLogxK
U2 - 10.1021/jf901442q
DO - 10.1021/jf901442q
M3 - Article
C2 - 19817425
AN - SCOPUS:70449103488
VL - 57
SP - 9944
EP - 9950
JO - Journal of Agricultural and Food Chemistry
JF - Journal of Agricultural and Food Chemistry
SN - 0021-8561
IS - 21
ER -