A secretomic view of woody and nonwoody lignocellulose degradation by Pleurotus ostreatus
Fecha
2016Autor
Versión
Acceso abierto / Sarbide irekia
Tipo
Artículo / Artikulua
Versión
Versión publicada / Argitaratu den bertsioa
Identificador del proyecto
Impacto
|
10.1186/s13068-016-0462-9
Resumen
Background: Pleurotus ostreatus is the second edible mushroom worldwide, and a model fungus for delignification
applications, with the advantage of growing on woody and nonwoody feedstocks. Its sequenced genome is available,
and this gave us the opportunity to perform proteomic studies to identify the enzymes overproduced in lignocellulose
cultures.
Results: Monokaryotic P. ostreatus (PC9) wa ...
[++]
Background: Pleurotus ostreatus is the second edible mushroom worldwide, and a model fungus for delignification
applications, with the advantage of growing on woody and nonwoody feedstocks. Its sequenced genome is available,
and this gave us the opportunity to perform proteomic studies to identify the enzymes overproduced in lignocellulose
cultures.
Results: Monokaryotic P. ostreatus (PC9) was grown with poplar wood or wheat straw as the sole C/N source and the
extracellular proteins were analyzed, together with those from glucose medium. Using nano-liquid chromatography
coupled to tandem mass spectrometry of whole-protein hydrolyzate, over five-hundred proteins were identified.
Thirty-four percent were unique of the straw cultures, while only 15 and 6 % were unique of the glucose and poplar
cultures, respectively (20 % were produced under the three conditions, and additional 19 % were shared by the two
lignocellulose cultures). Semi-quantitative analysis showed oxidoreductases as the main protein type both in the
poplar (39 % total abundance) and straw (31 %) secretomes, while carbohydrate-active enzymes (CAZys) were only
slightly overproduced (14–16 %). Laccase 10 (LACC10) was the main protein in the two lignocellulose secretomes
(10–14 %) and, together with LACC2, LACC9, LACC6, versatile peroxidase 1 (VP1), and manganese peroxidase 3
(MnP3), were strongly overproduced in the lignocellulose cultures. Seven CAZys were also among the top-50 proteins,
but only CE16 acetylesterase was overproduced on lignocellulose. When the woody and nonwoody secretomes
were compared, GH1 and GH3 β-glycosidases were more abundant on poplar and straw, respectively and, among less
abundant proteins, VP2 was overproduced on straw, while VP3 was only found on poplar. The treated lignocellulosic
substrates were analyzed by two-dimensional nuclear magnetic resonance (2D NMR), and a decrease of lignin relative
to carbohydrate signals was observed, together with the disappearance of some minor lignin substructures, and an
increase of sugar reducing ends.
Conclusions: Oxidoreductases are strongly induced when P. ostreatus grows on woody and nonwoody lignocellulosic
substrates. One laccase occupied the first position in both secretomes, and three more were overproduced
together with one VP and one MnP, suggesting an important role in lignocellulose degradation. Preferential removal
of lignin vs carbohydrates was shown by 2D NMR, in agreement with the above secretomic results. [--]
Materias
Pleurotus ostreatus,
Secreted proteins,
Poplar wood,
Wheat straw,
LC–MS/MS,
Lignin-modifying enzymes,
Laccases,
Carbohydrate-active enzymes,
2D NMR
Editor
BioMed Central
Publicado en
Biotechnology for Biofuels, (2016) 9:49
Departamento
Universidad Pública de Navarra. Departamento de Producción Agraria /
Nafarroako Unibertsitate Publikoa. Nekazaritza Ekoizpena Saila
Versión del editor
Entidades Financiadoras
This work was supported by the INDOX (KBBE-2013-613549) EU project, the BIO2014-56388-R, AGL2014-53730-R, and AGL2011-30495 projects of the Spanish Ministry of Economy and Competitiveness (MINECO) co-financed by FEDER funds, and the ProteoRed platform of the Spanish Institute of Health Carlos III (ISCIII). The work conducted by the US DOE JGI is supported by the Office of Science of the US DOE under contract number DE-AC02-05CH11231. FJR-D thanks a Ramón y Cajal contract of the Spanish MINECO, and JR thanks a contract of the CSIC project 201440E097.
Aparece en las colecciones
Los documentos de Academica-e están protegidos por derechos de autor con todos los derechos reservados, a no ser que se indique lo contrario.
La licencia del ítem se describe como © 2016 Fernández-Fueyo et al. This article is distributed under the terms of the Creative Commons Attribution 4.0 International
License, 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.