Cargando…

Laccase-derived lignin compounds boost cellulose oxidative enzymes AA9

BACKGROUND: The discovery of lignin as activator for the redox enzyme lytic polysaccharide monooxygenases (LPMOs) for the oxidation of cell-wall polysaccharides opens a new scenario for investigation of the interplay between different lignocellulose-degrading enzymes. The lignin-active enzymes in on...

Descripción completa

Detalles Bibliográficos
Autores principales: Brenelli, Lívia, Squina, Fabio M., Felby, Claus, Cannella, David
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5771016/
https://www.ncbi.nlm.nih.gov/pubmed/29371886
http://dx.doi.org/10.1186/s13068-017-0985-8
_version_ 1783293180156837888
author Brenelli, Lívia
Squina, Fabio M.
Felby, Claus
Cannella, David
author_facet Brenelli, Lívia
Squina, Fabio M.
Felby, Claus
Cannella, David
author_sort Brenelli, Lívia
collection PubMed
description BACKGROUND: The discovery of lignin as activator for the redox enzyme lytic polysaccharide monooxygenases (LPMOs) for the oxidation of cell-wall polysaccharides opens a new scenario for investigation of the interplay between different lignocellulose-degrading enzymes. The lignin-active enzymes in one hand, and the carbohydrate active in the other, are linked through a variety of electrons carrier molecules either derived from lignin or enzymatically transferred. Likewise, in nature, many lignocellulose-degrading organisms are expressing those enzymes simultaneously, and we wanted to test if a major commercial available lignin oxidase enzyme, i.e., laccase could benefit and synergize the activity of the LPMOs by depolymerizing the insoluble lignin. RESULTS: In this work, two fungal laccases together with a mediator (ABTS) were used to isolate low-molecular-weight lignin from lignocellulosic biomass. The isolated lignins were used as electron donors for activation of LPMOs. A direct correlation between the low-molecular-weight lignin isolated with laccases and an increased activity of a cellulolytic cocktail containing LPMO was found when pure cellulose was hydrolyzed. We then tried to implement existing commercial cellulases cocktail with laccase enzymes, but under the conditions tested, the co-incubation of laccases with LPMOs showed a substrate competition towards oxygen inhibiting the LPMO. In addition, we found that laccase treatment may cause other modifications to pure cellulose, rendering the material more recalcitrant for enzymatic saccharification. CONCLUSIONS: Laccase-mediated system was able to depolymerize lignin from pre-treated and native sugarcane bagasse and wheat straw, and the released phenolic molecules were able to donate electrons to LPMO enzymes boosting the overall enzymatic hydrolysis of cellulose. Likewise, other poly-phenol oxidase, we might have just started showing possible pros or cons in applying several oxidase enzymes for a simultaneous degradation of cellulose and lignin, and we found that the competition towards oxygen and their different consumption rates must be taken into account for any possible co-application. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s13068-017-0985-8) contains supplementary material, which is available to authorized users.
format Online
Article
Text
id pubmed-5771016
institution National Center for Biotechnology Information
language English
publishDate 2018
publisher BioMed Central
record_format MEDLINE/PubMed
spelling pubmed-57710162018-01-25 Laccase-derived lignin compounds boost cellulose oxidative enzymes AA9 Brenelli, Lívia Squina, Fabio M. Felby, Claus Cannella, David Biotechnol Biofuels Research BACKGROUND: The discovery of lignin as activator for the redox enzyme lytic polysaccharide monooxygenases (LPMOs) for the oxidation of cell-wall polysaccharides opens a new scenario for investigation of the interplay between different lignocellulose-degrading enzymes. The lignin-active enzymes in one hand, and the carbohydrate active in the other, are linked through a variety of electrons carrier molecules either derived from lignin or enzymatically transferred. Likewise, in nature, many lignocellulose-degrading organisms are expressing those enzymes simultaneously, and we wanted to test if a major commercial available lignin oxidase enzyme, i.e., laccase could benefit and synergize the activity of the LPMOs by depolymerizing the insoluble lignin. RESULTS: In this work, two fungal laccases together with a mediator (ABTS) were used to isolate low-molecular-weight lignin from lignocellulosic biomass. The isolated lignins were used as electron donors for activation of LPMOs. A direct correlation between the low-molecular-weight lignin isolated with laccases and an increased activity of a cellulolytic cocktail containing LPMO was found when pure cellulose was hydrolyzed. We then tried to implement existing commercial cellulases cocktail with laccase enzymes, but under the conditions tested, the co-incubation of laccases with LPMOs showed a substrate competition towards oxygen inhibiting the LPMO. In addition, we found that laccase treatment may cause other modifications to pure cellulose, rendering the material more recalcitrant for enzymatic saccharification. CONCLUSIONS: Laccase-mediated system was able to depolymerize lignin from pre-treated and native sugarcane bagasse and wheat straw, and the released phenolic molecules were able to donate electrons to LPMO enzymes boosting the overall enzymatic hydrolysis of cellulose. Likewise, other poly-phenol oxidase, we might have just started showing possible pros or cons in applying several oxidase enzymes for a simultaneous degradation of cellulose and lignin, and we found that the competition towards oxygen and their different consumption rates must be taken into account for any possible co-application. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s13068-017-0985-8) contains supplementary material, which is available to authorized users. BioMed Central 2018-01-17 /pmc/articles/PMC5771016/ /pubmed/29371886 http://dx.doi.org/10.1186/s13068-017-0985-8 Text en © The Author(s) 2018 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research
Brenelli, Lívia
Squina, Fabio M.
Felby, Claus
Cannella, David
Laccase-derived lignin compounds boost cellulose oxidative enzymes AA9
title Laccase-derived lignin compounds boost cellulose oxidative enzymes AA9
title_full Laccase-derived lignin compounds boost cellulose oxidative enzymes AA9
title_fullStr Laccase-derived lignin compounds boost cellulose oxidative enzymes AA9
title_full_unstemmed Laccase-derived lignin compounds boost cellulose oxidative enzymes AA9
title_short Laccase-derived lignin compounds boost cellulose oxidative enzymes AA9
title_sort laccase-derived lignin compounds boost cellulose oxidative enzymes aa9
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5771016/
https://www.ncbi.nlm.nih.gov/pubmed/29371886
http://dx.doi.org/10.1186/s13068-017-0985-8
work_keys_str_mv AT brenellilivia laccasederivedlignincompoundsboostcelluloseoxidativeenzymesaa9
AT squinafabiom laccasederivedlignincompoundsboostcelluloseoxidativeenzymesaa9
AT felbyclaus laccasederivedlignincompoundsboostcelluloseoxidativeenzymesaa9
AT cannelladavid laccasederivedlignincompoundsboostcelluloseoxidativeenzymesaa9