Secretome profile of Cellulomonas sp. B6 growing on lignocellulosic substrates

Aims: Lignocellulosic biomass deconstruction is a bottleneck for obtaining biofuels and value-added products. Our main goal was to characterize the secretome of a novel isolate, Cellulomonas sp. B6, when grown on residual biomass for the formulation of cost-efficient enzymatic cocktails. Methods and...

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Autores principales: Piccinni, F.E., Ontañon, O.M., Ghio, S., Sauka, D.H., Talia, P.M., Rivarola, M.L., Valacco, M.P., Campos, E.
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_13645072_v126_n3_p811_Piccinni
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spelling todo:paper_13645072_v126_n3_p811_Piccinni2023-10-03T16:11:04Z Secretome profile of Cellulomonas sp. B6 growing on lignocellulosic substrates Piccinni, F.E. Ontañon, O.M. Ghio, S. Sauka, D.H. Talia, P.M. Rivarola, M.L. Valacco, M.P. Campos, E. cazymes cellulomonas gh10 glucanases glycosyl hydrolases lignocellulose secretome xylanases arabinofuranosidase bacterial DNA bacterial enzyme bacterial RNA carboxymethylcellulose exoglucanase glucan synthase glycosidase lignocellulose RNA 16S unclassified drug xylan 1,4 beta xylosidase xylan endo 1,3 beta xylosidase xyloglucanase bacterium biofuel biotechnology biotransformation cellulose crop residue enzyme activity genome lignin secretion straw Article bacterial genome bacterial growth bacterium culture biomass Cellulomonas Cellulomonas aerilata Cellulomonas biazotea Cellulomonas bogoriensis Cellulomonas carbonis Cellulomonas cellasea Cellulomonas chitinilytica Cellulomonas composti Cellulomonas denverensis Cellulomonas fimi Cellulomonas flavigena Cellulomonas gelida Cellulomonas hominis Cellulomonas humilata Cellulomonas iranensis Cellulomonas marina Cellulomonas massiliensis Cellulomonas oligotrophica Cellulomonas pakistanensis Cellulomonas phragmiteti Cellulomonas soli Cellulomonas terrae Cellulomonas uda Cellulomonas xylanilytica controlled study DNA DNA hybridization enzyme activity enzyme substrate Micrococcus luteus nonhuman phylogeny protein secretion RNA sequence sugarcane Cellulomonas Cellulomonas sp. Saccharum Triticum aestivum Aims: Lignocellulosic biomass deconstruction is a bottleneck for obtaining biofuels and value-added products. Our main goal was to characterize the secretome of a novel isolate, Cellulomonas sp. B6, when grown on residual biomass for the formulation of cost-efficient enzymatic cocktails. Methods and Results: We identified 205 potential CAZymes in the genome of Cellulomonas sp. B6, 91 of which were glycoside hydrolases (GH). By secretome analysis of supernatants from cultures in either extruded wheat straw (EWS), grinded sugar cane straw (SCR) or carboxymethylcellulose (CMC), we identified which proteins played a role in lignocellulose deconstruction. Growth on CMC resulted in the secretion of two exoglucanases (GH6 and GH48) and two GH10 xylanases, while growth on SCR or EWS resulted in the identification of a diversity of CAZymes. From the 32 GHs predicted to be secreted, 22 were identified in supernatants from EWS and/or SCR cultures, including endo- and exoglucanases, xylanases, a xyloglucanase, an arabinofuranosidase/β-xylosidase, a β-glucosidase and an AA10. Surprisingly, among the xylanases, seven were GH10. Conclusions: Growth of Cellulomonas sp. B6 on lignocellulosic biomass induced the secretion of a diverse repertoire of CAZymes. Significance and Impact of the Study: Cellulomonas sp. B6 could serve as a source of lignocellulose-degrading enzymes applicable to bioprocessing and biotechnological industries. © 2018 The Society for Applied Microbiology JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_13645072_v126_n3_p811_Piccinni
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic cazymes
cellulomonas
gh10
glucanases
glycosyl hydrolases
lignocellulose
secretome
xylanases
arabinofuranosidase
bacterial DNA
bacterial enzyme
bacterial RNA
carboxymethylcellulose
exoglucanase
glucan synthase
glycosidase
lignocellulose
RNA 16S
unclassified drug
xylan 1,4 beta xylosidase
xylan endo 1,3 beta xylosidase
xyloglucanase
bacterium
biofuel
biotechnology
biotransformation
cellulose
crop residue
enzyme activity
genome
lignin
secretion
straw
Article
bacterial genome
bacterial growth
bacterium culture
biomass
Cellulomonas
Cellulomonas aerilata
Cellulomonas biazotea
Cellulomonas bogoriensis
Cellulomonas carbonis
Cellulomonas cellasea
Cellulomonas chitinilytica
Cellulomonas composti
Cellulomonas denverensis
Cellulomonas fimi
Cellulomonas flavigena
Cellulomonas gelida
Cellulomonas hominis
Cellulomonas humilata
Cellulomonas iranensis
Cellulomonas marina
Cellulomonas massiliensis
Cellulomonas oligotrophica
Cellulomonas pakistanensis
Cellulomonas phragmiteti
Cellulomonas soli
Cellulomonas terrae
Cellulomonas uda
Cellulomonas xylanilytica
controlled study
DNA DNA hybridization
enzyme activity
enzyme substrate
Micrococcus luteus
nonhuman
phylogeny
protein secretion
RNA sequence
sugarcane
Cellulomonas
Cellulomonas sp.
Saccharum
Triticum aestivum
spellingShingle cazymes
cellulomonas
gh10
glucanases
glycosyl hydrolases
lignocellulose
secretome
xylanases
arabinofuranosidase
bacterial DNA
bacterial enzyme
bacterial RNA
carboxymethylcellulose
exoglucanase
glucan synthase
glycosidase
lignocellulose
RNA 16S
unclassified drug
xylan 1,4 beta xylosidase
xylan endo 1,3 beta xylosidase
xyloglucanase
bacterium
biofuel
biotechnology
biotransformation
cellulose
crop residue
enzyme activity
genome
lignin
secretion
straw
Article
bacterial genome
bacterial growth
bacterium culture
biomass
Cellulomonas
Cellulomonas aerilata
Cellulomonas biazotea
Cellulomonas bogoriensis
Cellulomonas carbonis
Cellulomonas cellasea
Cellulomonas chitinilytica
Cellulomonas composti
Cellulomonas denverensis
Cellulomonas fimi
Cellulomonas flavigena
Cellulomonas gelida
Cellulomonas hominis
Cellulomonas humilata
Cellulomonas iranensis
Cellulomonas marina
Cellulomonas massiliensis
Cellulomonas oligotrophica
Cellulomonas pakistanensis
Cellulomonas phragmiteti
Cellulomonas soli
Cellulomonas terrae
Cellulomonas uda
Cellulomonas xylanilytica
controlled study
DNA DNA hybridization
enzyme activity
enzyme substrate
Micrococcus luteus
nonhuman
phylogeny
protein secretion
RNA sequence
sugarcane
Cellulomonas
Cellulomonas sp.
Saccharum
Triticum aestivum
Piccinni, F.E.
Ontañon, O.M.
Ghio, S.
Sauka, D.H.
Talia, P.M.
Rivarola, M.L.
Valacco, M.P.
Campos, E.
Secretome profile of Cellulomonas sp. B6 growing on lignocellulosic substrates
topic_facet cazymes
cellulomonas
gh10
glucanases
glycosyl hydrolases
lignocellulose
secretome
xylanases
arabinofuranosidase
bacterial DNA
bacterial enzyme
bacterial RNA
carboxymethylcellulose
exoglucanase
glucan synthase
glycosidase
lignocellulose
RNA 16S
unclassified drug
xylan 1,4 beta xylosidase
xylan endo 1,3 beta xylosidase
xyloglucanase
bacterium
biofuel
biotechnology
biotransformation
cellulose
crop residue
enzyme activity
genome
lignin
secretion
straw
Article
bacterial genome
bacterial growth
bacterium culture
biomass
Cellulomonas
Cellulomonas aerilata
Cellulomonas biazotea
Cellulomonas bogoriensis
Cellulomonas carbonis
Cellulomonas cellasea
Cellulomonas chitinilytica
Cellulomonas composti
Cellulomonas denverensis
Cellulomonas fimi
Cellulomonas flavigena
Cellulomonas gelida
Cellulomonas hominis
Cellulomonas humilata
Cellulomonas iranensis
Cellulomonas marina
Cellulomonas massiliensis
Cellulomonas oligotrophica
Cellulomonas pakistanensis
Cellulomonas phragmiteti
Cellulomonas soli
Cellulomonas terrae
Cellulomonas uda
Cellulomonas xylanilytica
controlled study
DNA DNA hybridization
enzyme activity
enzyme substrate
Micrococcus luteus
nonhuman
phylogeny
protein secretion
RNA sequence
sugarcane
Cellulomonas
Cellulomonas sp.
Saccharum
Triticum aestivum
description Aims: Lignocellulosic biomass deconstruction is a bottleneck for obtaining biofuels and value-added products. Our main goal was to characterize the secretome of a novel isolate, Cellulomonas sp. B6, when grown on residual biomass for the formulation of cost-efficient enzymatic cocktails. Methods and Results: We identified 205 potential CAZymes in the genome of Cellulomonas sp. B6, 91 of which were glycoside hydrolases (GH). By secretome analysis of supernatants from cultures in either extruded wheat straw (EWS), grinded sugar cane straw (SCR) or carboxymethylcellulose (CMC), we identified which proteins played a role in lignocellulose deconstruction. Growth on CMC resulted in the secretion of two exoglucanases (GH6 and GH48) and two GH10 xylanases, while growth on SCR or EWS resulted in the identification of a diversity of CAZymes. From the 32 GHs predicted to be secreted, 22 were identified in supernatants from EWS and/or SCR cultures, including endo- and exoglucanases, xylanases, a xyloglucanase, an arabinofuranosidase/β-xylosidase, a β-glucosidase and an AA10. Surprisingly, among the xylanases, seven were GH10. Conclusions: Growth of Cellulomonas sp. B6 on lignocellulosic biomass induced the secretion of a diverse repertoire of CAZymes. Significance and Impact of the Study: Cellulomonas sp. B6 could serve as a source of lignocellulose-degrading enzymes applicable to bioprocessing and biotechnological industries. © 2018 The Society for Applied Microbiology
format JOUR
author Piccinni, F.E.
Ontañon, O.M.
Ghio, S.
Sauka, D.H.
Talia, P.M.
Rivarola, M.L.
Valacco, M.P.
Campos, E.
author_facet Piccinni, F.E.
Ontañon, O.M.
Ghio, S.
Sauka, D.H.
Talia, P.M.
Rivarola, M.L.
Valacco, M.P.
Campos, E.
author_sort Piccinni, F.E.
title Secretome profile of Cellulomonas sp. B6 growing on lignocellulosic substrates
title_short Secretome profile of Cellulomonas sp. B6 growing on lignocellulosic substrates
title_full Secretome profile of Cellulomonas sp. B6 growing on lignocellulosic substrates
title_fullStr Secretome profile of Cellulomonas sp. B6 growing on lignocellulosic substrates
title_full_unstemmed Secretome profile of Cellulomonas sp. B6 growing on lignocellulosic substrates
title_sort secretome profile of cellulomonas sp. b6 growing on lignocellulosic substrates
url http://hdl.handle.net/20.500.12110/paper_13645072_v126_n3_p811_Piccinni
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