Diversity of GH51 α-L-arabinofuranosidase homolog sequences from subantarctic intertidal sediments

Autores
Dionisi, Hebe Monica; Lozada, Mariana; Campos, Eleonora
Año de publicación
2023
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Bacteria from coastal habitats exposed to challenging environmental conditions constitute a promising source of enzymes with novel catalytic properties for the depolymerization of complex carbohydrates of terrestrial and marine origins. In this work, we investigated the sequence and structural diversity of putative enzymes related to the glycoside hydrolase family 51 (GH51) identified in a metagenomic dataset of intertidal sediments from a subantarctic environment. The majority of the characterized members of the GH51 family are α-L-arabinofuranosidases (EC 3.2.1.55), enzymes with important industrial applications that catalyze the hydrolysis of side chains from arabinose-substituted polysaccharides. The 28 sequences identified in the metagenome were highly diverse and were assigned to the Bacteroidota, Planctomycetota, Chloroflexota, Pseudomonadota, and Kiritimatiellaeota phyla, with four sequences remaining unassigned. In a sequence similarity network, most GH51 homolog sequences clustered with uncharacterized members of the GH51 family or were highly divergent. Three-dimensional models of the putative enzymes showed distinctive structural characteristics, including a highly variable length of the loop located between β-strand 2 and α-helix 2 and the absence in some of the sequences of a highly conserved Trp residue in this loop. Important differences in the predicted surface electrostatic potential in models of closely related GH51 homologs suggest various levels of adaptation to the prevailing environmental conditions. This work provides an insight into the characteristics of putative enzymes related to the GH51 family from intertidal sediment bacteria, from taxa that are relevant in the marine environment but remain poorly characterized due to the difficulties in their cultivation.
Fil: Dionisi, Hebe Monica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Centro para el Estudio de Sistemas Marinos; Argentina
Fil: Lozada, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Centro para el Estudio de Sistemas Marinos; Argentina
Fil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Agrobiotecnología y Biología Molecular. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Agrobiotecnología y Biología Molecular; Argentina
Materia
GH51
GLYCOSIDE HYDROLASES
INTERTIDAL SEDIMENTS
METAGENOME
Α-L-ARABINOFURANOSIDASES
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/228706
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/228706
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Diversity of GH51 α-L-arabinofuranosidase homolog sequences from subantarctic intertidal sedimentsDionisi, Hebe MonicaLozada, MarianaCampos, EleonoraGH51GLYCOSIDE HYDROLASESINTERTIDAL SEDIMENTSMETAGENOMEΑ-L-ARABINOFURANOSIDASEShttps://purl.org/becyt/ford/2.8https://purl.org/becyt/ford/2Bacteria from coastal habitats exposed to challenging environmental conditions constitute a promising source of enzymes with novel catalytic properties for the depolymerization of complex carbohydrates of terrestrial and marine origins. In this work, we investigated the sequence and structural diversity of putative enzymes related to the glycoside hydrolase family 51 (GH51) identified in a metagenomic dataset of intertidal sediments from a subantarctic environment. The majority of the characterized members of the GH51 family are α-L-arabinofuranosidases (EC 3.2.1.55), enzymes with important industrial applications that catalyze the hydrolysis of side chains from arabinose-substituted polysaccharides. The 28 sequences identified in the metagenome were highly diverse and were assigned to the Bacteroidota, Planctomycetota, Chloroflexota, Pseudomonadota, and Kiritimatiellaeota phyla, with four sequences remaining unassigned. In a sequence similarity network, most GH51 homolog sequences clustered with uncharacterized members of the GH51 family or were highly divergent. Three-dimensional models of the putative enzymes showed distinctive structural characteristics, including a highly variable length of the loop located between β-strand 2 and α-helix 2 and the absence in some of the sequences of a highly conserved Trp residue in this loop. Important differences in the predicted surface electrostatic potential in models of closely related GH51 homologs suggest various levels of adaptation to the prevailing environmental conditions. This work provides an insight into the characteristics of putative enzymes related to the GH51 family from intertidal sediment bacteria, from taxa that are relevant in the marine environment but remain poorly characterized due to the difficulties in their cultivation.Fil: Dionisi, Hebe Monica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Centro para el Estudio de Sistemas Marinos; ArgentinaFil: Lozada, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Centro para el Estudio de Sistemas Marinos; ArgentinaFil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Agrobiotecnología y Biología Molecular. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Agrobiotecnología y Biología Molecular; ArgentinaVersita2023-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/228706Dionisi, Hebe Monica; Lozada, Mariana; Campos, Eleonora; Diversity of GH51 α-L-arabinofuranosidase homolog sequences from subantarctic intertidal sediments; Versita; Biologia; 78; 7; 3-2023; 1899-19180006-3088CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://link.springer.com/collections/aeiicidbafinfo:eu-repo/semantics/altIdentifier/doi/10.1007/s11756-023-01382-xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:12:46Zoai:ri.conicet.gov.ar:11336/228706instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:12:47.181CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Diversity of GH51 α-L-arabinofuranosidase homolog sequences from subantarctic intertidal sediments
title Diversity of GH51 α-L-arabinofuranosidase homolog sequences from subantarctic intertidal sediments
spellingShingle Diversity of GH51 α-L-arabinofuranosidase homolog sequences from subantarctic intertidal sediments
Dionisi, Hebe Monica
GH51
GLYCOSIDE HYDROLASES
INTERTIDAL SEDIMENTS
METAGENOME
Α-L-ARABINOFURANOSIDASES
title_short Diversity of GH51 α-L-arabinofuranosidase homolog sequences from subantarctic intertidal sediments
title_full Diversity of GH51 α-L-arabinofuranosidase homolog sequences from subantarctic intertidal sediments
title_fullStr Diversity of GH51 α-L-arabinofuranosidase homolog sequences from subantarctic intertidal sediments
title_full_unstemmed Diversity of GH51 α-L-arabinofuranosidase homolog sequences from subantarctic intertidal sediments
title_sort Diversity of GH51 α-L-arabinofuranosidase homolog sequences from subantarctic intertidal sediments
dc.creator.none.fl_str_mv Dionisi, Hebe Monica
Lozada, Mariana
Campos, Eleonora
author Dionisi, Hebe Monica
author_facet Dionisi, Hebe Monica
Lozada, Mariana
Campos, Eleonora
author_role author
author2 Lozada, Mariana
Campos, Eleonora
author2_role author
author
dc.subject.none.fl_str_mv GH51
GLYCOSIDE HYDROLASES
INTERTIDAL SEDIMENTS
METAGENOME
Α-L-ARABINOFURANOSIDASES
topic GH51
GLYCOSIDE HYDROLASES
INTERTIDAL SEDIMENTS
METAGENOME
Α-L-ARABINOFURANOSIDASES
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.8
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Bacteria from coastal habitats exposed to challenging environmental conditions constitute a promising source of enzymes with novel catalytic properties for the depolymerization of complex carbohydrates of terrestrial and marine origins. In this work, we investigated the sequence and structural diversity of putative enzymes related to the glycoside hydrolase family 51 (GH51) identified in a metagenomic dataset of intertidal sediments from a subantarctic environment. The majority of the characterized members of the GH51 family are α-L-arabinofuranosidases (EC 3.2.1.55), enzymes with important industrial applications that catalyze the hydrolysis of side chains from arabinose-substituted polysaccharides. The 28 sequences identified in the metagenome were highly diverse and were assigned to the Bacteroidota, Planctomycetota, Chloroflexota, Pseudomonadota, and Kiritimatiellaeota phyla, with four sequences remaining unassigned. In a sequence similarity network, most GH51 homolog sequences clustered with uncharacterized members of the GH51 family or were highly divergent. Three-dimensional models of the putative enzymes showed distinctive structural characteristics, including a highly variable length of the loop located between β-strand 2 and α-helix 2 and the absence in some of the sequences of a highly conserved Trp residue in this loop. Important differences in the predicted surface electrostatic potential in models of closely related GH51 homologs suggest various levels of adaptation to the prevailing environmental conditions. This work provides an insight into the characteristics of putative enzymes related to the GH51 family from intertidal sediment bacteria, from taxa that are relevant in the marine environment but remain poorly characterized due to the difficulties in their cultivation.
Fil: Dionisi, Hebe Monica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Centro para el Estudio de Sistemas Marinos; Argentina
Fil: Lozada, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Centro para el Estudio de Sistemas Marinos; Argentina
Fil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Agrobiotecnología y Biología Molecular. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Agrobiotecnología y Biología Molecular; Argentina
description Bacteria from coastal habitats exposed to challenging environmental conditions constitute a promising source of enzymes with novel catalytic properties for the depolymerization of complex carbohydrates of terrestrial and marine origins. In this work, we investigated the sequence and structural diversity of putative enzymes related to the glycoside hydrolase family 51 (GH51) identified in a metagenomic dataset of intertidal sediments from a subantarctic environment. The majority of the characterized members of the GH51 family are α-L-arabinofuranosidases (EC 3.2.1.55), enzymes with important industrial applications that catalyze the hydrolysis of side chains from arabinose-substituted polysaccharides. The 28 sequences identified in the metagenome were highly diverse and were assigned to the Bacteroidota, Planctomycetota, Chloroflexota, Pseudomonadota, and Kiritimatiellaeota phyla, with four sequences remaining unassigned. In a sequence similarity network, most GH51 homolog sequences clustered with uncharacterized members of the GH51 family or were highly divergent. Three-dimensional models of the putative enzymes showed distinctive structural characteristics, including a highly variable length of the loop located between β-strand 2 and α-helix 2 and the absence in some of the sequences of a highly conserved Trp residue in this loop. Important differences in the predicted surface electrostatic potential in models of closely related GH51 homologs suggest various levels of adaptation to the prevailing environmental conditions. This work provides an insight into the characteristics of putative enzymes related to the GH51 family from intertidal sediment bacteria, from taxa that are relevant in the marine environment but remain poorly characterized due to the difficulties in their cultivation.
publishDate 2023
dc.date.none.fl_str_mv 2023-03
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/228706
Dionisi, Hebe Monica; Lozada, Mariana; Campos, Eleonora; Diversity of GH51 α-L-arabinofuranosidase homolog sequences from subantarctic intertidal sediments; Versita; Biologia; 78; 7; 3-2023; 1899-1918
0006-3088
CONICET Digital
CONICET
url http://hdl.handle.net/11336/228706
identifier_str_mv Dionisi, Hebe Monica; Lozada, Mariana; Campos, Eleonora; Diversity of GH51 α-L-arabinofuranosidase homolog sequences from subantarctic intertidal sediments; Versita; Biologia; 78; 7; 3-2023; 1899-1918
0006-3088
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/collections/aeiicidbaf
info:eu-repo/semantics/altIdentifier/doi/10.1007/s11756-023-01382-x
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Versita
publisher.none.fl_str_mv Versita
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.070432

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