Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 99-104 |
| Seitenumfang | 6 |
| Fachzeitschrift | Journal of Molecular Catalysis B: Enzymatic |
| Jahrgang | 87 |
| Publikationsstatus | Veröffentlicht - 16 Nov. 2012 |
Abstract
A dioxygenase from the edible basidiomycete Pleurotus sapidus, originally researched because of its distinct ability to convert the sequiterpene (+)-valencene to the valuable grapefruit aroma (+)-nootkatone, was identified as a potent lipoxygenase (LOXPsa1). Kinetic parameters, pH and temperature optima of the pure recombinant enzyme were determined using linoleic acid as the substrate. Km, vmax, and kcat were 40.3 μM, 130.3 U mg-1, and 157 s-1, respectively. The maximal enzymatic activity was found at pH 7.0 and 35°C. Showing high specificity toward free linoleic acid, the enzyme was classified as lipoxygenase type 1. Conversion of linoleic acid yielded mainly (S)-13-hydroperoxy-9Z,11E- octadecadienoic acid (94% ee), as was confirmed by chiral HPLC analysis of the hydroperoxides. The amino acid sequence showed homology to lipoxygenases catalyzing S stereospecific oxygenation, and thus the enzyme was characterized as a 13S-lipoxygenase. This is the first lipoxygenase described to accept terpene hydrocarbons as substrates.
ASJC Scopus Sachgebiete
- Chemische Verfahrenstechnik (insg.)
- Katalyse
- Chemische Verfahrenstechnik (insg.)
- Bioengineering
- Biochemie, Genetik und Molekularbiologie (insg.)
- Biochemie
- Chemische Verfahrenstechnik (insg.)
- Prozesschemie und -technologie
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in: Journal of Molecular Catalysis B: Enzymatic, Jahrgang 87, 16.11.2012, S. 99-104.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - LOXPsa1, the first recombinant lipoxygenase from a basidiomycete fungus
AU - Plagemann, Ina
AU - Zelena, Katerina
AU - Arendt, Philipp
AU - Ringel, Peter D.
AU - Krings, Ulrich
AU - Berger, Ralf G.
PY - 2012/11/16
Y1 - 2012/11/16
N2 - A dioxygenase from the edible basidiomycete Pleurotus sapidus, originally researched because of its distinct ability to convert the sequiterpene (+)-valencene to the valuable grapefruit aroma (+)-nootkatone, was identified as a potent lipoxygenase (LOXPsa1). Kinetic parameters, pH and temperature optima of the pure recombinant enzyme were determined using linoleic acid as the substrate. Km, vmax, and kcat were 40.3 μM, 130.3 U mg-1, and 157 s-1, respectively. The maximal enzymatic activity was found at pH 7.0 and 35°C. Showing high specificity toward free linoleic acid, the enzyme was classified as lipoxygenase type 1. Conversion of linoleic acid yielded mainly (S)-13-hydroperoxy-9Z,11E- octadecadienoic acid (94% ee), as was confirmed by chiral HPLC analysis of the hydroperoxides. The amino acid sequence showed homology to lipoxygenases catalyzing S stereospecific oxygenation, and thus the enzyme was characterized as a 13S-lipoxygenase. This is the first lipoxygenase described to accept terpene hydrocarbons as substrates.
AB - A dioxygenase from the edible basidiomycete Pleurotus sapidus, originally researched because of its distinct ability to convert the sequiterpene (+)-valencene to the valuable grapefruit aroma (+)-nootkatone, was identified as a potent lipoxygenase (LOXPsa1). Kinetic parameters, pH and temperature optima of the pure recombinant enzyme were determined using linoleic acid as the substrate. Km, vmax, and kcat were 40.3 μM, 130.3 U mg-1, and 157 s-1, respectively. The maximal enzymatic activity was found at pH 7.0 and 35°C. Showing high specificity toward free linoleic acid, the enzyme was classified as lipoxygenase type 1. Conversion of linoleic acid yielded mainly (S)-13-hydroperoxy-9Z,11E- octadecadienoic acid (94% ee), as was confirmed by chiral HPLC analysis of the hydroperoxides. The amino acid sequence showed homology to lipoxygenases catalyzing S stereospecific oxygenation, and thus the enzyme was characterized as a 13S-lipoxygenase. This is the first lipoxygenase described to accept terpene hydrocarbons as substrates.
KW - Basidiomycete
KW - Lipoxygenase
KW - Promiscuity
KW - Recombinant
KW - Terpene
UR - http://www.scopus.com/inward/record.url?scp=84871805286&partnerID=8YFLogxK
U2 - 10.1016/j.molcatb.2012.11.004
DO - 10.1016/j.molcatb.2012.11.004
M3 - Article
AN - SCOPUS:84871805286
VL - 87
SP - 99
EP - 104
JO - Journal of Molecular Catalysis B: Enzymatic
JF - Journal of Molecular Catalysis B: Enzymatic
SN - 1381-1177
ER -