Cargando…

Successful Production and Ligninolytic Activity of a Bacterial Laccase, Lac51, Made in Nicotiana benthamiana via Transient Expression

Giant panda could have bamboo as their exclusive diet for about 2 million years because of the contribution of numerous enzymes produced by their gut bacteria, for instance laccases. Laccases are blue multi-copper oxidases that catalyze the oxidation of a broad spectrum of phenolic and aromatic comp...

Descripción completa

Detalles Bibliográficos
Autores principales: van Eerde, André, Várnai, Anikó, Wang, Yanliang, Paruch, Lisa, Jameson, John-Kristian, Qiao, Fen, Eiken, Hans Geir, Su, Hang, Eijsink, Vincent G. H., Clarke, Jihong Liu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9141054/
https://www.ncbi.nlm.nih.gov/pubmed/35646038
http://dx.doi.org/10.3389/fpls.2022.912293
_version_ 1784715251300696064
author van Eerde, André
Várnai, Anikó
Wang, Yanliang
Paruch, Lisa
Jameson, John-Kristian
Qiao, Fen
Eiken, Hans Geir
Su, Hang
Eijsink, Vincent G. H.
Clarke, Jihong Liu
author_facet van Eerde, André
Várnai, Anikó
Wang, Yanliang
Paruch, Lisa
Jameson, John-Kristian
Qiao, Fen
Eiken, Hans Geir
Su, Hang
Eijsink, Vincent G. H.
Clarke, Jihong Liu
author_sort van Eerde, André
collection PubMed
description Giant panda could have bamboo as their exclusive diet for about 2 million years because of the contribution of numerous enzymes produced by their gut bacteria, for instance laccases. Laccases are blue multi-copper oxidases that catalyze the oxidation of a broad spectrum of phenolic and aromatic compounds with water as the only byproduct. As a “green enzyme,” laccases have potential in industrial applications, for example, when dealing with degradation of recalcitrant biopolymers, such as lignin. In the current study, a bacterial laccase, Lac51, originating from Pseudomonas putida and identified in the gut microbiome of the giant panda’s gut was transiently expressed in the non-food plant Nicotiana benthamiana and characterized. Our results show that recombinant Lac51 exhibits bacterial laccase properties, with optimal pH and temperature at 7–8 and 40°C, respectively, when using syringaldazine as substrate. Moreover, we demonstrate the functional capability of the plant expressed Lac51 to oxidize lignin using selected lignin monomers that serve as substrates of Lac51. In summary, our study demonstrates the potential of green and non-food plants as a viable enzyme production platform for bacterial laccases. This result enriches our understanding of plant-made enzymes, as, to our knowledge, Lac51 is the first functional recombinant laccase produced in plants.
format Online
Article
Text
id pubmed-9141054
institution National Center for Biotechnology Information
language English
publishDate 2022
publisher Frontiers Media S.A.
record_format MEDLINE/PubMed
spelling pubmed-91410542022-05-28 Successful Production and Ligninolytic Activity of a Bacterial Laccase, Lac51, Made in Nicotiana benthamiana via Transient Expression van Eerde, André Várnai, Anikó Wang, Yanliang Paruch, Lisa Jameson, John-Kristian Qiao, Fen Eiken, Hans Geir Su, Hang Eijsink, Vincent G. H. Clarke, Jihong Liu Front Plant Sci Plant Science Giant panda could have bamboo as their exclusive diet for about 2 million years because of the contribution of numerous enzymes produced by their gut bacteria, for instance laccases. Laccases are blue multi-copper oxidases that catalyze the oxidation of a broad spectrum of phenolic and aromatic compounds with water as the only byproduct. As a “green enzyme,” laccases have potential in industrial applications, for example, when dealing with degradation of recalcitrant biopolymers, such as lignin. In the current study, a bacterial laccase, Lac51, originating from Pseudomonas putida and identified in the gut microbiome of the giant panda’s gut was transiently expressed in the non-food plant Nicotiana benthamiana and characterized. Our results show that recombinant Lac51 exhibits bacterial laccase properties, with optimal pH and temperature at 7–8 and 40°C, respectively, when using syringaldazine as substrate. Moreover, we demonstrate the functional capability of the plant expressed Lac51 to oxidize lignin using selected lignin monomers that serve as substrates of Lac51. In summary, our study demonstrates the potential of green and non-food plants as a viable enzyme production platform for bacterial laccases. This result enriches our understanding of plant-made enzymes, as, to our knowledge, Lac51 is the first functional recombinant laccase produced in plants. Frontiers Media S.A. 2022-05-13 /pmc/articles/PMC9141054/ /pubmed/35646038 http://dx.doi.org/10.3389/fpls.2022.912293 Text en Copyright © 2022 van Eerde, Várnai, Wang, Paruch, Jameson, Qiao, Eiken, Su, Eijsink and Clarke. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
van Eerde, André
Várnai, Anikó
Wang, Yanliang
Paruch, Lisa
Jameson, John-Kristian
Qiao, Fen
Eiken, Hans Geir
Su, Hang
Eijsink, Vincent G. H.
Clarke, Jihong Liu
Successful Production and Ligninolytic Activity of a Bacterial Laccase, Lac51, Made in Nicotiana benthamiana via Transient Expression
title Successful Production and Ligninolytic Activity of a Bacterial Laccase, Lac51, Made in Nicotiana benthamiana via Transient Expression
title_full Successful Production and Ligninolytic Activity of a Bacterial Laccase, Lac51, Made in Nicotiana benthamiana via Transient Expression
title_fullStr Successful Production and Ligninolytic Activity of a Bacterial Laccase, Lac51, Made in Nicotiana benthamiana via Transient Expression
title_full_unstemmed Successful Production and Ligninolytic Activity of a Bacterial Laccase, Lac51, Made in Nicotiana benthamiana via Transient Expression
title_short Successful Production and Ligninolytic Activity of a Bacterial Laccase, Lac51, Made in Nicotiana benthamiana via Transient Expression
title_sort successful production and ligninolytic activity of a bacterial laccase, lac51, made in nicotiana benthamiana via transient expression
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9141054/
https://www.ncbi.nlm.nih.gov/pubmed/35646038
http://dx.doi.org/10.3389/fpls.2022.912293
work_keys_str_mv AT vaneerdeandre successfulproductionandligninolyticactivityofabacteriallaccaselac51madeinnicotianabenthamianaviatransientexpression
AT varnaianiko successfulproductionandligninolyticactivityofabacteriallaccaselac51madeinnicotianabenthamianaviatransientexpression
AT wangyanliang successfulproductionandligninolyticactivityofabacteriallaccaselac51madeinnicotianabenthamianaviatransientexpression
AT paruchlisa successfulproductionandligninolyticactivityofabacteriallaccaselac51madeinnicotianabenthamianaviatransientexpression
AT jamesonjohnkristian successfulproductionandligninolyticactivityofabacteriallaccaselac51madeinnicotianabenthamianaviatransientexpression
AT qiaofen successfulproductionandligninolyticactivityofabacteriallaccaselac51madeinnicotianabenthamianaviatransientexpression
AT eikenhansgeir successfulproductionandligninolyticactivityofabacteriallaccaselac51madeinnicotianabenthamianaviatransientexpression
AT suhang successfulproductionandligninolyticactivityofabacteriallaccaselac51madeinnicotianabenthamianaviatransientexpression
AT eijsinkvincentgh successfulproductionandligninolyticactivityofabacteriallaccaselac51madeinnicotianabenthamianaviatransientexpression
AT clarkejihongliu successfulproductionandligninolyticactivityofabacteriallaccaselac51madeinnicotianabenthamianaviatransientexpression