Characterization of the monolignol oxidoreductase AtBBE-like protein 15 L182V for biocatalytic applications

Sabine Pils, Kordula Schnabl, Silvia Wallner, Marko Kljajic, Nina Kupresanin, Rolf Breinbauer, Jörg Schrittwieser, Michael Fuchs, Wolfgang Kroutil, Bastian Daniel, Peter Macheroux

Research output: Contribution to journalArticleResearchpeer-review

Abstract

Monolignol oxidoreductases from the berberine bridge enzyme-like (BBE-like) protein family (pfam 08031) catalyze the oxidation of monolignols to the corresponding aldehydes. In this report, we explore the potential of a monolignol oxidoreductase from Arabidopsis thaliana (AtBBE-like protein 15) as biocatalyst for oxidative reactions. For this study we employed a variant with enhanced reactivity towards oxygen, which was obtained by a single amino acid exchange (L182V). The pH and temperature optima of the purified AtBBE-like protein 15 L182V were determined as well as the tolerance toward organic co-solvents; furthermore the substrate scope was characterized. The enzyme has a temperature optimum of 50 °C and retains more than 50% activity between pH 5 and pH 10 within 5 minutes. The enzyme shows increased activity in the presence of various co-solvents (10-50% v/v), including acetonitrile, 2-propanol, 1,4-dioxane, and dimethyl sulfoxide. Primary benzylic and primary or secondary allylic alcohols were accepted as substrates. The enantioselectivity E in the oxidation of secondary alcohols was good to excellent (E >34 to >200).
Original languageEnglish
Pages (from-to)S6-S14
JournalJournal of molecular catalysis / B
Volume133
Issue numberSuppl.1
DOIs
Publication statusPublished - 2016

Cite this

Characterization of the monolignol oxidoreductase AtBBE-like protein 15 L182V for biocatalytic applications. / Pils, Sabine; Schnabl, Kordula; Wallner, Silvia; Kljajic, Marko; Kupresanin, Nina; Breinbauer, Rolf; Schrittwieser, Jörg; Fuchs, Michael; Kroutil, Wolfgang; Daniel, Bastian; Macheroux, Peter.

In: Journal of molecular catalysis / B, Vol. 133, No. Suppl.1, 2016, p. S6-S14.

Research output: Contribution to journalArticleResearchpeer-review

Pils, Sabine ; Schnabl, Kordula ; Wallner, Silvia ; Kljajic, Marko ; Kupresanin, Nina ; Breinbauer, Rolf ; Schrittwieser, Jörg ; Fuchs, Michael ; Kroutil, Wolfgang ; Daniel, Bastian ; Macheroux, Peter. / Characterization of the monolignol oxidoreductase AtBBE-like protein 15 L182V for biocatalytic applications. In: Journal of molecular catalysis / B. 2016 ; Vol. 133, No. Suppl.1. pp. S6-S14.
@article{bf049d850a674a2681e3eede04180e25,
title = "Characterization of the monolignol oxidoreductase AtBBE-like protein 15 L182V for biocatalytic applications",
abstract = "Monolignol oxidoreductases from the berberine bridge enzyme-like (BBE-like) protein family (pfam 08031) catalyze the oxidation of monolignols to the corresponding aldehydes. In this report, we explore the potential of a monolignol oxidoreductase from Arabidopsis thaliana (AtBBE-like protein 15) as biocatalyst for oxidative reactions. For this study we employed a variant with enhanced reactivity towards oxygen, which was obtained by a single amino acid exchange (L182V). The pH and temperature optima of the purified AtBBE-like protein 15 L182V were determined as well as the tolerance toward organic co-solvents; furthermore the substrate scope was characterized. The enzyme has a temperature optimum of 50 °C and retains more than 50{\%} activity between pH 5 and pH 10 within 5 minutes. The enzyme shows increased activity in the presence of various co-solvents (10-50{\%} v/v), including acetonitrile, 2-propanol, 1,4-dioxane, and dimethyl sulfoxide. Primary benzylic and primary or secondary allylic alcohols were accepted as substrates. The enantioselectivity E in the oxidation of secondary alcohols was good to excellent (E >34 to >200).",
author = "Sabine Pils and Kordula Schnabl and Silvia Wallner and Marko Kljajic and Nina Kupresanin and Rolf Breinbauer and J{\"o}rg Schrittwieser and Michael Fuchs and Wolfgang Kroutil and Bastian Daniel and Peter Macheroux",
year = "2016",
doi = "10.1016/j.molcatb.2016.10.018",
language = "English",
volume = "133",
pages = "S6--S14",
journal = "Journal of molecular catalysis / B",
issn = "1381-1177",
publisher = "Elsevier B.V.",
number = "Suppl.1",

}

TY - JOUR

T1 - Characterization of the monolignol oxidoreductase AtBBE-like protein 15 L182V for biocatalytic applications

AU - Pils, Sabine

AU - Schnabl, Kordula

AU - Wallner, Silvia

AU - Kljajic, Marko

AU - Kupresanin, Nina

AU - Breinbauer, Rolf

AU - Schrittwieser, Jörg

AU - Fuchs, Michael

AU - Kroutil, Wolfgang

AU - Daniel, Bastian

AU - Macheroux, Peter

PY - 2016

Y1 - 2016

N2 - Monolignol oxidoreductases from the berberine bridge enzyme-like (BBE-like) protein family (pfam 08031) catalyze the oxidation of monolignols to the corresponding aldehydes. In this report, we explore the potential of a monolignol oxidoreductase from Arabidopsis thaliana (AtBBE-like protein 15) as biocatalyst for oxidative reactions. For this study we employed a variant with enhanced reactivity towards oxygen, which was obtained by a single amino acid exchange (L182V). The pH and temperature optima of the purified AtBBE-like protein 15 L182V were determined as well as the tolerance toward organic co-solvents; furthermore the substrate scope was characterized. The enzyme has a temperature optimum of 50 °C and retains more than 50% activity between pH 5 and pH 10 within 5 minutes. The enzyme shows increased activity in the presence of various co-solvents (10-50% v/v), including acetonitrile, 2-propanol, 1,4-dioxane, and dimethyl sulfoxide. Primary benzylic and primary or secondary allylic alcohols were accepted as substrates. The enantioselectivity E in the oxidation of secondary alcohols was good to excellent (E >34 to >200).

AB - Monolignol oxidoreductases from the berberine bridge enzyme-like (BBE-like) protein family (pfam 08031) catalyze the oxidation of monolignols to the corresponding aldehydes. In this report, we explore the potential of a monolignol oxidoreductase from Arabidopsis thaliana (AtBBE-like protein 15) as biocatalyst for oxidative reactions. For this study we employed a variant with enhanced reactivity towards oxygen, which was obtained by a single amino acid exchange (L182V). The pH and temperature optima of the purified AtBBE-like protein 15 L182V were determined as well as the tolerance toward organic co-solvents; furthermore the substrate scope was characterized. The enzyme has a temperature optimum of 50 °C and retains more than 50% activity between pH 5 and pH 10 within 5 minutes. The enzyme shows increased activity in the presence of various co-solvents (10-50% v/v), including acetonitrile, 2-propanol, 1,4-dioxane, and dimethyl sulfoxide. Primary benzylic and primary or secondary allylic alcohols were accepted as substrates. The enantioselectivity E in the oxidation of secondary alcohols was good to excellent (E >34 to >200).

U2 - 10.1016/j.molcatb.2016.10.018

DO - 10.1016/j.molcatb.2016.10.018

M3 - Article

VL - 133

SP - S6-S14

JO - Journal of molecular catalysis / B

JF - Journal of molecular catalysis / B

SN - 1381-1177

IS - Suppl.1

ER -