Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 149-154 |
| Seitenumfang | 6 |
| Fachzeitschrift | Zeitschrift fur Naturforschung - Section C Journal of Biosciences |
| Jahrgang | 69 C |
| Ausgabenummer | 3-4 |
| Publikationsstatus | Veröffentlicht - 2 Juni 2014 |
Abstract
The lipoxygenase LOXPsa1 of Pleurotus sapidus, originally investigated because of its ability to oxidize (+)-valencene to the valuable grapefruit aroma (+)-nootkatone, was isolated from the peptidase-rich lyophilisate using a three-step purification scheme including preparative isoelectric focusing and chromatographic techniques. Nano-liquid chromatography electrospray ionization tandem mass spectrometry (nLC-ESI-MS/MS) of the purified enzyme and peptide mass fingerprint analysis gave 38 peptides of the lipoxygenase from P. sapidus. Nearly 50% of the 643 amino acids long sequence encoded by the cDNA was covered. Both terminal peptides of the native LOXPsa1 were identified by de novo sequencing, and the postulated molecular mass of 72:5 kDa was confirmed. With linoleic acid as the substrate, the LOXPsa1 showed a specific activity of 113 U mg-1 and maximal activity at pH 7.0 and 30 °C, respectively.
ASJC Scopus Sachgebiete
- Biochemie, Genetik und Molekularbiologie (insg.)
- Allgemeine Biochemie, Genetik und Molekularbiologie
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in: Zeitschrift fur Naturforschung - Section C Journal of Biosciences, Jahrgang 69 C, Nr. 3-4, 02.06.2014, S. 149-154.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Isolation and characterization of wild-type lipoxygenase LOXPsa1 from Pleurotus sapidus
AU - Plagemann, Ina
AU - Krings, Ulrich
AU - Berger, Ralf G.
PY - 2014/6/2
Y1 - 2014/6/2
N2 - The lipoxygenase LOXPsa1 of Pleurotus sapidus, originally investigated because of its ability to oxidize (+)-valencene to the valuable grapefruit aroma (+)-nootkatone, was isolated from the peptidase-rich lyophilisate using a three-step purification scheme including preparative isoelectric focusing and chromatographic techniques. Nano-liquid chromatography electrospray ionization tandem mass spectrometry (nLC-ESI-MS/MS) of the purified enzyme and peptide mass fingerprint analysis gave 38 peptides of the lipoxygenase from P. sapidus. Nearly 50% of the 643 amino acids long sequence encoded by the cDNA was covered. Both terminal peptides of the native LOXPsa1 were identified by de novo sequencing, and the postulated molecular mass of 72:5 kDa was confirmed. With linoleic acid as the substrate, the LOXPsa1 showed a specific activity of 113 U mg-1 and maximal activity at pH 7.0 and 30 °C, respectively.
AB - The lipoxygenase LOXPsa1 of Pleurotus sapidus, originally investigated because of its ability to oxidize (+)-valencene to the valuable grapefruit aroma (+)-nootkatone, was isolated from the peptidase-rich lyophilisate using a three-step purification scheme including preparative isoelectric focusing and chromatographic techniques. Nano-liquid chromatography electrospray ionization tandem mass spectrometry (nLC-ESI-MS/MS) of the purified enzyme and peptide mass fingerprint analysis gave 38 peptides of the lipoxygenase from P. sapidus. Nearly 50% of the 643 amino acids long sequence encoded by the cDNA was covered. Both terminal peptides of the native LOXPsa1 were identified by de novo sequencing, and the postulated molecular mass of 72:5 kDa was confirmed. With linoleic acid as the substrate, the LOXPsa1 showed a specific activity of 113 U mg-1 and maximal activity at pH 7.0 and 30 °C, respectively.
KW - Basidiomycete
KW - Lipoxygenase
KW - Pleurotus sapidus
UR - http://www.scopus.com/inward/record.url?scp=84901396348&partnerID=8YFLogxK
U2 - 10.5560/znc.2013-0133
DO - 10.5560/znc.2013-0133
M3 - Article
C2 - 24873036
AN - SCOPUS:84901396348
VL - 69 C
SP - 149
EP - 154
JO - Zeitschrift fur Naturforschung - Section C Journal of Biosciences
JF - Zeitschrift fur Naturforschung - Section C Journal of Biosciences
SN - 0939-5075
IS - 3-4
ER -