AA16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes

Background Lignocellulosic biomass is considered as a promising alternative to fossil resources for the production of fuels, materials and chemicals. Efficient enzymatic systems are needed to degrade the plant cell wall and overcome its recalcitrance. A widely used producer of cellulolytic cocktails is the ascomycete Trichoderma reesei, but this organism secretes a limited set of enzymes. To improve the saccharification yields, one strategy is to upgrade the T. reesei enzyme cocktail with enzymes produced by other biomass-degrading filamentous fungi isolated from biodiversity. Results In this study, the enzymatic cocktails secreted by five strains from the genus Aspergillus (Aspergillus japonicus strains BRFM 405, 1487, 1489, 1490 and Aspergillus niger strain BRFM 430) were tested for their ability to boost a T. reesei reference cocktail for the saccharification of pretreated biomass. Proteomic analysis of fungal secretomes that significantly improved biomass degradation showed that the presence of proteins belonging to a putative LPMO family previously identified by genome analysis and awaiting experimental demonstration of activity. Members of this novel LPMO family, named AA16, are encountered in fungi and oomycetes with life styles oriented toward interactions with plant biomass. One AA16 protein from Aspergillus aculeatus (AaAA16) was produced to high level in Pichia pastoris. LPMO-type enzyme activity was demonstrated on cellulose with oxidative cleavage at the C1 position of the glucose unit. AaAA16 LPMO was found to significantly improve the activity of T. reesei CBHI on cellulosic substrates. Conclusions Although Aspergillus spp. has been investigated for decades for their CAZymes diversity, we identified members of a new fungal LPMO family using secretomics and functional assays. Properties of the founding member of the AA16 family characterized herein could be of interest for use in biorefineries. Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Filiatrault-Chastel, Camille [verfasserIn] Navarro, David Haon, Mireille Grisel, Sacha Herpoël-Gimbert, Isabelle Chevret, Didier Fanuel, Mathieu Henrissat, Bernard Heiss-Blanquet, Senta Margeot, Antoine Berrin, Jean-Guy

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2019

Schlagwörter:	Filamentous fungi Plant biomass Cellulolytic enzymes production LPMO Biofuels

Anmerkung:	© The Author(s) 2019

Übergeordnetes Werk:	Enthalten in: Biotechnology for biofuels - London : BioMed Central, 2008, 12(2019), 1 vom: 16. März
Übergeordnetes Werk:	volume:12 ; year:2019 ; number:1 ; day:16 ; month:03

Links:	Volltext

DOI / URN:	10.1186/s13068-019-1394-y

Katalog-ID:	SPR030159326

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allfields	10.1186/s13068-019-1394-y doi (DE-627)SPR030159326 (SPR)s13068-019-1394-y-e DE-627 ger DE-627 rakwb eng Filiatrault-Chastel, Camille verfasserin aut AA16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2019 Background Lignocellulosic biomass is considered as a promising alternative to fossil resources for the production of fuels, materials and chemicals. Efficient enzymatic systems are needed to degrade the plant cell wall and overcome its recalcitrance. A widely used producer of cellulolytic cocktails is the ascomycete Trichoderma reesei, but this organism secretes a limited set of enzymes. To improve the saccharification yields, one strategy is to upgrade the T. reesei enzyme cocktail with enzymes produced by other biomass-degrading filamentous fungi isolated from biodiversity. Results In this study, the enzymatic cocktails secreted by five strains from the genus Aspergillus (Aspergillus japonicus strains BRFM 405, 1487, 1489, 1490 and Aspergillus niger strain BRFM 430) were tested for their ability to boost a T. reesei reference cocktail for the saccharification of pretreated biomass. Proteomic analysis of fungal secretomes that significantly improved biomass degradation showed that the presence of proteins belonging to a putative LPMO family previously identified by genome analysis and awaiting experimental demonstration of activity. Members of this novel LPMO family, named AA16, are encountered in fungi and oomycetes with life styles oriented toward interactions with plant biomass. One AA16 protein from Aspergillus aculeatus (AaAA16) was produced to high level in Pichia pastoris. LPMO-type enzyme activity was demonstrated on cellulose with oxidative cleavage at the C1 position of the glucose unit. AaAA16 LPMO was found to significantly improve the activity of T. reesei CBHI on cellulosic substrates. Conclusions Although Aspergillus spp. has been investigated for decades for their CAZymes diversity, we identified members of a new fungal LPMO family using secretomics and functional assays. Properties of the founding member of the AA16 family characterized herein could be of interest for use in biorefineries. Filamentous fungi (dpeaa)DE-He213 Plant biomass (dpeaa)DE-He213 Cellulolytic enzymes production (dpeaa)DE-He213 LPMO (dpeaa)DE-He213 Biofuels (dpeaa)DE-He213 Navarro, David aut Haon, Mireille aut Grisel, Sacha aut Herpoël-Gimbert, Isabelle aut Chevret, Didier aut Fanuel, Mathieu aut Henrissat, Bernard aut Heiss-Blanquet, Senta aut Margeot, Antoine aut Berrin, Jean-Guy (orcid)0000-0001-7570-3745 aut Enthalten in Biotechnology for biofuels London : BioMed Central, 2008 12(2019), 1 vom: 16. März (DE-627)563167882 (DE-600)2421351-2 1754-6834 nnns volume:12 year:2019 number:1 day:16 month:03 https://dx.doi.org/10.1186/s13068-019-1394-y kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_2055 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2119 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2019 1 16 03
spelling	10.1186/s13068-019-1394-y doi (DE-627)SPR030159326 (SPR)s13068-019-1394-y-e DE-627 ger DE-627 rakwb eng Filiatrault-Chastel, Camille verfasserin aut AA16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2019 Background Lignocellulosic biomass is considered as a promising alternative to fossil resources for the production of fuels, materials and chemicals. Efficient enzymatic systems are needed to degrade the plant cell wall and overcome its recalcitrance. A widely used producer of cellulolytic cocktails is the ascomycete Trichoderma reesei, but this organism secretes a limited set of enzymes. To improve the saccharification yields, one strategy is to upgrade the T. reesei enzyme cocktail with enzymes produced by other biomass-degrading filamentous fungi isolated from biodiversity. Results In this study, the enzymatic cocktails secreted by five strains from the genus Aspergillus (Aspergillus japonicus strains BRFM 405, 1487, 1489, 1490 and Aspergillus niger strain BRFM 430) were tested for their ability to boost a T. reesei reference cocktail for the saccharification of pretreated biomass. Proteomic analysis of fungal secretomes that significantly improved biomass degradation showed that the presence of proteins belonging to a putative LPMO family previously identified by genome analysis and awaiting experimental demonstration of activity. Members of this novel LPMO family, named AA16, are encountered in fungi and oomycetes with life styles oriented toward interactions with plant biomass. One AA16 protein from Aspergillus aculeatus (AaAA16) was produced to high level in Pichia pastoris. LPMO-type enzyme activity was demonstrated on cellulose with oxidative cleavage at the C1 position of the glucose unit. AaAA16 LPMO was found to significantly improve the activity of T. reesei CBHI on cellulosic substrates. Conclusions Although Aspergillus spp. has been investigated for decades for their CAZymes diversity, we identified members of a new fungal LPMO family using secretomics and functional assays. Properties of the founding member of the AA16 family characterized herein could be of interest for use in biorefineries. Filamentous fungi (dpeaa)DE-He213 Plant biomass (dpeaa)DE-He213 Cellulolytic enzymes production (dpeaa)DE-He213 LPMO (dpeaa)DE-He213 Biofuels (dpeaa)DE-He213 Navarro, David aut Haon, Mireille aut Grisel, Sacha aut Herpoël-Gimbert, Isabelle aut Chevret, Didier aut Fanuel, Mathieu aut Henrissat, Bernard aut Heiss-Blanquet, Senta aut Margeot, Antoine aut Berrin, Jean-Guy (orcid)0000-0001-7570-3745 aut Enthalten in Biotechnology for biofuels London : BioMed Central, 2008 12(2019), 1 vom: 16. März (DE-627)563167882 (DE-600)2421351-2 1754-6834 nnns volume:12 year:2019 number:1 day:16 month:03 https://dx.doi.org/10.1186/s13068-019-1394-y kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_2055 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2119 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2019 1 16 03
allfields_unstemmed	10.1186/s13068-019-1394-y doi (DE-627)SPR030159326 (SPR)s13068-019-1394-y-e DE-627 ger DE-627 rakwb eng Filiatrault-Chastel, Camille verfasserin aut AA16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2019 Background Lignocellulosic biomass is considered as a promising alternative to fossil resources for the production of fuels, materials and chemicals. Efficient enzymatic systems are needed to degrade the plant cell wall and overcome its recalcitrance. A widely used producer of cellulolytic cocktails is the ascomycete Trichoderma reesei, but this organism secretes a limited set of enzymes. To improve the saccharification yields, one strategy is to upgrade the T. reesei enzyme cocktail with enzymes produced by other biomass-degrading filamentous fungi isolated from biodiversity. Results In this study, the enzymatic cocktails secreted by five strains from the genus Aspergillus (Aspergillus japonicus strains BRFM 405, 1487, 1489, 1490 and Aspergillus niger strain BRFM 430) were tested for their ability to boost a T. reesei reference cocktail for the saccharification of pretreated biomass. Proteomic analysis of fungal secretomes that significantly improved biomass degradation showed that the presence of proteins belonging to a putative LPMO family previously identified by genome analysis and awaiting experimental demonstration of activity. Members of this novel LPMO family, named AA16, are encountered in fungi and oomycetes with life styles oriented toward interactions with plant biomass. One AA16 protein from Aspergillus aculeatus (AaAA16) was produced to high level in Pichia pastoris. LPMO-type enzyme activity was demonstrated on cellulose with oxidative cleavage at the C1 position of the glucose unit. AaAA16 LPMO was found to significantly improve the activity of T. reesei CBHI on cellulosic substrates. Conclusions Although Aspergillus spp. has been investigated for decades for their CAZymes diversity, we identified members of a new fungal LPMO family using secretomics and functional assays. Properties of the founding member of the AA16 family characterized herein could be of interest for use in biorefineries. Filamentous fungi (dpeaa)DE-He213 Plant biomass (dpeaa)DE-He213 Cellulolytic enzymes production (dpeaa)DE-He213 LPMO (dpeaa)DE-He213 Biofuels (dpeaa)DE-He213 Navarro, David aut Haon, Mireille aut Grisel, Sacha aut Herpoël-Gimbert, Isabelle aut Chevret, Didier aut Fanuel, Mathieu aut Henrissat, Bernard aut Heiss-Blanquet, Senta aut Margeot, Antoine aut Berrin, Jean-Guy (orcid)0000-0001-7570-3745 aut Enthalten in Biotechnology for biofuels London : BioMed Central, 2008 12(2019), 1 vom: 16. März (DE-627)563167882 (DE-600)2421351-2 1754-6834 nnns volume:12 year:2019 number:1 day:16 month:03 https://dx.doi.org/10.1186/s13068-019-1394-y kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_2055 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2119 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2019 1 16 03
allfieldsGer	10.1186/s13068-019-1394-y doi (DE-627)SPR030159326 (SPR)s13068-019-1394-y-e DE-627 ger DE-627 rakwb eng Filiatrault-Chastel, Camille verfasserin aut AA16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2019 Background Lignocellulosic biomass is considered as a promising alternative to fossil resources for the production of fuels, materials and chemicals. Efficient enzymatic systems are needed to degrade the plant cell wall and overcome its recalcitrance. A widely used producer of cellulolytic cocktails is the ascomycete Trichoderma reesei, but this organism secretes a limited set of enzymes. To improve the saccharification yields, one strategy is to upgrade the T. reesei enzyme cocktail with enzymes produced by other biomass-degrading filamentous fungi isolated from biodiversity. Results In this study, the enzymatic cocktails secreted by five strains from the genus Aspergillus (Aspergillus japonicus strains BRFM 405, 1487, 1489, 1490 and Aspergillus niger strain BRFM 430) were tested for their ability to boost a T. reesei reference cocktail for the saccharification of pretreated biomass. Proteomic analysis of fungal secretomes that significantly improved biomass degradation showed that the presence of proteins belonging to a putative LPMO family previously identified by genome analysis and awaiting experimental demonstration of activity. Members of this novel LPMO family, named AA16, are encountered in fungi and oomycetes with life styles oriented toward interactions with plant biomass. One AA16 protein from Aspergillus aculeatus (AaAA16) was produced to high level in Pichia pastoris. LPMO-type enzyme activity was demonstrated on cellulose with oxidative cleavage at the C1 position of the glucose unit. AaAA16 LPMO was found to significantly improve the activity of T. reesei CBHI on cellulosic substrates. Conclusions Although Aspergillus spp. has been investigated for decades for their CAZymes diversity, we identified members of a new fungal LPMO family using secretomics and functional assays. Properties of the founding member of the AA16 family characterized herein could be of interest for use in biorefineries. Filamentous fungi (dpeaa)DE-He213 Plant biomass (dpeaa)DE-He213 Cellulolytic enzymes production (dpeaa)DE-He213 LPMO (dpeaa)DE-He213 Biofuels (dpeaa)DE-He213 Navarro, David aut Haon, Mireille aut Grisel, Sacha aut Herpoël-Gimbert, Isabelle aut Chevret, Didier aut Fanuel, Mathieu aut Henrissat, Bernard aut Heiss-Blanquet, Senta aut Margeot, Antoine aut Berrin, Jean-Guy (orcid)0000-0001-7570-3745 aut Enthalten in Biotechnology for biofuels London : BioMed Central, 2008 12(2019), 1 vom: 16. März (DE-627)563167882 (DE-600)2421351-2 1754-6834 nnns volume:12 year:2019 number:1 day:16 month:03 https://dx.doi.org/10.1186/s13068-019-1394-y kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_2055 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2119 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2019 1 16 03
allfieldsSound	10.1186/s13068-019-1394-y doi (DE-627)SPR030159326 (SPR)s13068-019-1394-y-e DE-627 ger DE-627 rakwb eng Filiatrault-Chastel, Camille verfasserin aut AA16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2019 Background Lignocellulosic biomass is considered as a promising alternative to fossil resources for the production of fuels, materials and chemicals. Efficient enzymatic systems are needed to degrade the plant cell wall and overcome its recalcitrance. A widely used producer of cellulolytic cocktails is the ascomycete Trichoderma reesei, but this organism secretes a limited set of enzymes. To improve the saccharification yields, one strategy is to upgrade the T. reesei enzyme cocktail with enzymes produced by other biomass-degrading filamentous fungi isolated from biodiversity. Results In this study, the enzymatic cocktails secreted by five strains from the genus Aspergillus (Aspergillus japonicus strains BRFM 405, 1487, 1489, 1490 and Aspergillus niger strain BRFM 430) were tested for their ability to boost a T. reesei reference cocktail for the saccharification of pretreated biomass. Proteomic analysis of fungal secretomes that significantly improved biomass degradation showed that the presence of proteins belonging to a putative LPMO family previously identified by genome analysis and awaiting experimental demonstration of activity. Members of this novel LPMO family, named AA16, are encountered in fungi and oomycetes with life styles oriented toward interactions with plant biomass. One AA16 protein from Aspergillus aculeatus (AaAA16) was produced to high level in Pichia pastoris. LPMO-type enzyme activity was demonstrated on cellulose with oxidative cleavage at the C1 position of the glucose unit. AaAA16 LPMO was found to significantly improve the activity of T. reesei CBHI on cellulosic substrates. Conclusions Although Aspergillus spp. has been investigated for decades for their CAZymes diversity, we identified members of a new fungal LPMO family using secretomics and functional assays. Properties of the founding member of the AA16 family characterized herein could be of interest for use in biorefineries. Filamentous fungi (dpeaa)DE-He213 Plant biomass (dpeaa)DE-He213 Cellulolytic enzymes production (dpeaa)DE-He213 LPMO (dpeaa)DE-He213 Biofuels (dpeaa)DE-He213 Navarro, David aut Haon, Mireille aut Grisel, Sacha aut Herpoël-Gimbert, Isabelle aut Chevret, Didier aut Fanuel, Mathieu aut Henrissat, Bernard aut Heiss-Blanquet, Senta aut Margeot, Antoine aut Berrin, Jean-Guy (orcid)0000-0001-7570-3745 aut Enthalten in Biotechnology for biofuels London : BioMed Central, 2008 12(2019), 1 vom: 16. März (DE-627)563167882 (DE-600)2421351-2 1754-6834 nnns volume:12 year:2019 number:1 day:16 month:03 https://dx.doi.org/10.1186/s13068-019-1394-y kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_2055 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2119 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2019 1 16 03
language	English
source	Enthalten in Biotechnology for biofuels 12(2019), 1 vom: 16. März volume:12 year:2019 number:1 day:16 month:03
sourceStr	Enthalten in Biotechnology for biofuels 12(2019), 1 vom: 16. März volume:12 year:2019 number:1 day:16 month:03
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Filamentous fungi Plant biomass Cellulolytic enzymes production LPMO Biofuels
isfreeaccess_bool	true
container_title	Biotechnology for biofuels
authorswithroles_txt_mv	Filiatrault-Chastel, Camille @@aut@@ Navarro, David @@aut@@ Haon, Mireille @@aut@@ Grisel, Sacha @@aut@@ Herpoël-Gimbert, Isabelle @@aut@@ Chevret, Didier @@aut@@ Fanuel, Mathieu @@aut@@ Henrissat, Bernard @@aut@@ Heiss-Blanquet, Senta @@aut@@ Margeot, Antoine @@aut@@ Berrin, Jean-Guy @@aut@@
publishDateDaySort_date	2019-03-16T00:00:00Z
hierarchy_top_id	563167882
id	SPR030159326
language_de	englisch
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Proteomic analysis of fungal secretomes that significantly improved biomass degradation showed that the presence of proteins belonging to a putative LPMO family previously identified by genome analysis and awaiting experimental demonstration of activity. Members of this novel LPMO family, named AA16, are encountered in fungi and oomycetes with life styles oriented toward interactions with plant biomass. One AA16 protein from Aspergillus aculeatus (AaAA16) was produced to high level in Pichia pastoris. LPMO-type enzyme activity was demonstrated on cellulose with oxidative cleavage at the C1 position of the glucose unit. AaAA16 LPMO was found to significantly improve the activity of T. reesei CBHI on cellulosic substrates. Conclusions Although Aspergillus spp. has been investigated for decades for their CAZymes diversity, we identified members of a new fungal LPMO family using secretomics and functional assays. 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author	Filiatrault-Chastel, Camille
spellingShingle	Filiatrault-Chastel, Camille misc Filamentous fungi misc Plant biomass misc Cellulolytic enzymes production misc LPMO misc Biofuels AA16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes
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topic_title	AA16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes Filamentous fungi (dpeaa)DE-He213 Plant biomass (dpeaa)DE-He213 Cellulolytic enzymes production (dpeaa)DE-He213 LPMO (dpeaa)DE-He213 Biofuels (dpeaa)DE-He213
topic	misc Filamentous fungi misc Plant biomass misc Cellulolytic enzymes production misc LPMO misc Biofuels
topic_unstemmed	misc Filamentous fungi misc Plant biomass misc Cellulolytic enzymes production misc LPMO misc Biofuels
topic_browse	misc Filamentous fungi misc Plant biomass misc Cellulolytic enzymes production misc LPMO misc Biofuels
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title	AA16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes
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title_full	AA16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes
author_sort	Filiatrault-Chastel, Camille
journal	Biotechnology for biofuels
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author_browse	Filiatrault-Chastel, Camille Navarro, David Haon, Mireille Grisel, Sacha Herpoël-Gimbert, Isabelle Chevret, Didier Fanuel, Mathieu Henrissat, Bernard Heiss-Blanquet, Senta Margeot, Antoine Berrin, Jean-Guy
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title_sort	aa16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes
title_auth	AA16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes
abstract	Background Lignocellulosic biomass is considered as a promising alternative to fossil resources for the production of fuels, materials and chemicals. Efficient enzymatic systems are needed to degrade the plant cell wall and overcome its recalcitrance. A widely used producer of cellulolytic cocktails is the ascomycete Trichoderma reesei, but this organism secretes a limited set of enzymes. To improve the saccharification yields, one strategy is to upgrade the T. reesei enzyme cocktail with enzymes produced by other biomass-degrading filamentous fungi isolated from biodiversity. Results In this study, the enzymatic cocktails secreted by five strains from the genus Aspergillus (Aspergillus japonicus strains BRFM 405, 1487, 1489, 1490 and Aspergillus niger strain BRFM 430) were tested for their ability to boost a T. reesei reference cocktail for the saccharification of pretreated biomass. Proteomic analysis of fungal secretomes that significantly improved biomass degradation showed that the presence of proteins belonging to a putative LPMO family previously identified by genome analysis and awaiting experimental demonstration of activity. Members of this novel LPMO family, named AA16, are encountered in fungi and oomycetes with life styles oriented toward interactions with plant biomass. One AA16 protein from Aspergillus aculeatus (AaAA16) was produced to high level in Pichia pastoris. LPMO-type enzyme activity was demonstrated on cellulose with oxidative cleavage at the C1 position of the glucose unit. AaAA16 LPMO was found to significantly improve the activity of T. reesei CBHI on cellulosic substrates. Conclusions Although Aspergillus spp. has been investigated for decades for their CAZymes diversity, we identified members of a new fungal LPMO family using secretomics and functional assays. Properties of the founding member of the AA16 family characterized herein could be of interest for use in biorefineries. © The Author(s) 2019
abstractGer	Background Lignocellulosic biomass is considered as a promising alternative to fossil resources for the production of fuels, materials and chemicals. Efficient enzymatic systems are needed to degrade the plant cell wall and overcome its recalcitrance. A widely used producer of cellulolytic cocktails is the ascomycete Trichoderma reesei, but this organism secretes a limited set of enzymes. To improve the saccharification yields, one strategy is to upgrade the T. reesei enzyme cocktail with enzymes produced by other biomass-degrading filamentous fungi isolated from biodiversity. Results In this study, the enzymatic cocktails secreted by five strains from the genus Aspergillus (Aspergillus japonicus strains BRFM 405, 1487, 1489, 1490 and Aspergillus niger strain BRFM 430) were tested for their ability to boost a T. reesei reference cocktail for the saccharification of pretreated biomass. Proteomic analysis of fungal secretomes that significantly improved biomass degradation showed that the presence of proteins belonging to a putative LPMO family previously identified by genome analysis and awaiting experimental demonstration of activity. Members of this novel LPMO family, named AA16, are encountered in fungi and oomycetes with life styles oriented toward interactions with plant biomass. One AA16 protein from Aspergillus aculeatus (AaAA16) was produced to high level in Pichia pastoris. LPMO-type enzyme activity was demonstrated on cellulose with oxidative cleavage at the C1 position of the glucose unit. AaAA16 LPMO was found to significantly improve the activity of T. reesei CBHI on cellulosic substrates. Conclusions Although Aspergillus spp. has been investigated for decades for their CAZymes diversity, we identified members of a new fungal LPMO family using secretomics and functional assays. Properties of the founding member of the AA16 family characterized herein could be of interest for use in biorefineries. © The Author(s) 2019
abstract_unstemmed	Background Lignocellulosic biomass is considered as a promising alternative to fossil resources for the production of fuels, materials and chemicals. Efficient enzymatic systems are needed to degrade the plant cell wall and overcome its recalcitrance. A widely used producer of cellulolytic cocktails is the ascomycete Trichoderma reesei, but this organism secretes a limited set of enzymes. To improve the saccharification yields, one strategy is to upgrade the T. reesei enzyme cocktail with enzymes produced by other biomass-degrading filamentous fungi isolated from biodiversity. Results In this study, the enzymatic cocktails secreted by five strains from the genus Aspergillus (Aspergillus japonicus strains BRFM 405, 1487, 1489, 1490 and Aspergillus niger strain BRFM 430) were tested for their ability to boost a T. reesei reference cocktail for the saccharification of pretreated biomass. Proteomic analysis of fungal secretomes that significantly improved biomass degradation showed that the presence of proteins belonging to a putative LPMO family previously identified by genome analysis and awaiting experimental demonstration of activity. Members of this novel LPMO family, named AA16, are encountered in fungi and oomycetes with life styles oriented toward interactions with plant biomass. One AA16 protein from Aspergillus aculeatus (AaAA16) was produced to high level in Pichia pastoris. LPMO-type enzyme activity was demonstrated on cellulose with oxidative cleavage at the C1 position of the glucose unit. AaAA16 LPMO was found to significantly improve the activity of T. reesei CBHI on cellulosic substrates. Conclusions Although Aspergillus spp. has been investigated for decades for their CAZymes diversity, we identified members of a new fungal LPMO family using secretomics and functional assays. Properties of the founding member of the AA16 family characterized herein could be of interest for use in biorefineries. © The Author(s) 2019
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title_short	AA16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes
url	https://dx.doi.org/10.1186/s13068-019-1394-y
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author2	Navarro, David Haon, Mireille Grisel, Sacha Herpoël-Gimbert, Isabelle Chevret, Didier Fanuel, Mathieu Henrissat, Bernard Heiss-Blanquet, Senta Margeot, Antoine Berrin, Jean-Guy
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AA16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes

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Vorhandene Bände

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