LOXPsa1, the first recombinant lipoxygenase from a basidiomycete fungus

Research output: Contribution to journal › Article › Research › peer review

Authors

  • Ina Plagemann
  • Katerina Zelena
  • Philipp Arendt
  • Peter D. Ringel
  • Ulrich Krings
  • Ralf G. Berger

Research Organisations

View graph of relations

Details

Original languageEnglish
Pages (from-to)99-104
Number of pages6
JournalJournal of Molecular Catalysis B: Enzymatic
Volume87
Publication statusPublished - 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.

Keywords

    Basidiomycete, Lipoxygenase, Promiscuity, Recombinant, Terpene

ASJC Scopus subject areas

Cite this

LOXPsa1, the first recombinant lipoxygenase from a basidiomycete fungus. / Plagemann, Ina; Zelena, Katerina; Arendt, Philipp et al.
In: Journal of Molecular Catalysis B: Enzymatic, Vol. 87, 16.11.2012, p. 99-104.

Research output: Contribution to journal › Article › Research › peer review

Plagemann, I, Zelena, K, Arendt, P, Ringel, PD, Krings, U & Berger, RG 2012, 'LOXPsa1, the first recombinant lipoxygenase from a basidiomycete fungus', Journal of Molecular Catalysis B: Enzymatic, vol. 87, pp. 99-104. https://doi.org/10.1016/j.molcatb.2012.11.004
Plagemann, I., Zelena, K., Arendt, P., Ringel, P. D., Krings, U., & Berger, R. G. (2012). LOXPsa1, the first recombinant lipoxygenase from a basidiomycete fungus. Journal of Molecular Catalysis B: Enzymatic, 87, 99-104. https://doi.org/10.1016/j.molcatb.2012.11.004
Plagemann I, Zelena K, Arendt P, Ringel PD, Krings U, Berger RG. LOXPsa1, the first recombinant lipoxygenase from a basidiomycete fungus. Journal of Molecular Catalysis B: Enzymatic. 2012 Nov 16;87:99-104. doi: 10.1016/j.molcatb.2012.11.004
Plagemann, Ina ; Zelena, Katerina ; Arendt, Philipp et al. / LOXPsa1, the first recombinant lipoxygenase from a basidiomycete fungus. In: Journal of Molecular Catalysis B: Enzymatic. 2012 ; Vol. 87. pp. 99-104.
Download
@article{53b10fafa17a4001919b23bf136a6def,
title = "LOXPsa1, the first recombinant lipoxygenase from a basidiomycete fungus",
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.",
keywords = "Basidiomycete, Lipoxygenase, Promiscuity, Recombinant, Terpene",
author = "Ina Plagemann and Katerina Zelena and Philipp Arendt and Ringel, {Peter D.} and Ulrich Krings and Berger, {Ralf G.}",
year = "2012",
month = nov,
day = "16",
doi = "10.1016/j.molcatb.2012.11.004",
language = "English",
volume = "87",
pages = "99--104",
journal = "Journal of Molecular Catalysis B: Enzymatic",
issn = "1381-1177",
publisher = "Elsevier",

}

Download

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 -