Biosynthesis and degradation of glycerides in external mycelium of <i>Glomus mosseae</i>

Autores
Gaspar, María Laura; Pollero, Ricardo José; Cabello, Marta Noemí
Año de publicación
2001
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The activities of enzymes involved in the glyceride metabolism of Glomus mosseae external mycelium are reported. Total mycelial homogenates were incubated with radiolabeled triolein and palmitic acid for various times under different conditions. The results obtained demonstrate the capacity of G. mosseae external mycelium to synthesize and hydrolyze its own acylglycerides. Neutral lipid biosynthesis progressively increased along with root colonization. Incorporation of [¹⁴C]-palmitate was mainly into triacylglycerols and as a minor fraction into diacylglycerols. The activity of palmitoyl-CoA ligase in external mycelium also increased in parallel with mycorrhiza development. The hydrolysis of triacylglycerols was very low at the beginning of colonization and then increased. However, lipase activity was lower than that of acyl-CoA ligase even at late stages of colonization. Thus, triacylglycerol biosynthesis apparently prevails over degradation during G. mosseae mycelium development in the period examined.
Instituto de Investigaciones Bioquímicas de La Plata
Instituto de Botánica "Dr. Carlos Spegazzini"
Materia
Bioquímica
Ciencias Naturales
Acyl-CoA ligase
Acylglycerol synthetase
External mycelium
Lipase activity
Triacylglycerols
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/141441
Acceder
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oai_identifier_str oai:sedici.unlp.edu.ar:10915/141441
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Biosynthesis and degradation of glycerides in external mycelium of <i>Glomus mosseae</i>Gaspar, María LauraPollero, Ricardo JoséCabello, Marta NoemíBioquímicaCiencias NaturalesAcyl-CoA ligaseAcylglycerol synthetaseExternal myceliumLipase activityTriacylglycerolsThe activities of enzymes involved in the glyceride metabolism of <i>Glomus mosseae</i> external mycelium are reported. Total mycelial homogenates were incubated with radiolabeled triolein and palmitic acid for various times under different conditions. The results obtained demonstrate the capacity of <i>G. mosseae</i> external mycelium to synthesize and hydrolyze its own acylglycerides. Neutral lipid biosynthesis progressively increased along with root colonization. Incorporation of [¹⁴C]-palmitate was mainly into triacylglycerols and as a minor fraction into diacylglycerols. The activity of palmitoyl-CoA ligase in external mycelium also increased in parallel with mycorrhiza development. The hydrolysis of triacylglycerols was very low at the beginning of colonization and then increased. However, lipase activity was lower than that of acyl-CoA ligase even at late stages of colonization. Thus, triacylglycerol biosynthesis apparently prevails over degradation during <i>G. mosseae</i> mycelium development in the period examined.Instituto de Investigaciones Bioquímicas de La PlataInstituto de Botánica "Dr. Carlos Spegazzini"2001-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf257-261http://sedici.unlp.edu.ar/handle/10915/141441enginfo:eu-repo/semantics/altIdentifier/issn/0940-6360info:eu-repo/semantics/altIdentifier/issn/1432-1890info:eu-repo/semantics/altIdentifier/doi/10.1007/s005720100130info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:32:26Zoai:sedici.unlp.edu.ar:10915/141441Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:32:27.148SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Biosynthesis and degradation of glycerides in external mycelium of <i>Glomus mosseae</i>
title Biosynthesis and degradation of glycerides in external mycelium of <i>Glomus mosseae</i>
spellingShingle Biosynthesis and degradation of glycerides in external mycelium of <i>Glomus mosseae</i>
Gaspar, María Laura
Bioquímica
Ciencias Naturales
Acyl-CoA ligase
Acylglycerol synthetase
External mycelium
Lipase activity
Triacylglycerols
title_short Biosynthesis and degradation of glycerides in external mycelium of <i>Glomus mosseae</i>
title_full Biosynthesis and degradation of glycerides in external mycelium of <i>Glomus mosseae</i>
title_fullStr Biosynthesis and degradation of glycerides in external mycelium of <i>Glomus mosseae</i>
title_full_unstemmed Biosynthesis and degradation of glycerides in external mycelium of <i>Glomus mosseae</i>
title_sort Biosynthesis and degradation of glycerides in external mycelium of <i>Glomus mosseae</i>
dc.creator.none.fl_str_mv Gaspar, María Laura
Pollero, Ricardo José
Cabello, Marta Noemí
author Gaspar, María Laura
author_facet Gaspar, María Laura
Pollero, Ricardo José
Cabello, Marta Noemí
author_role author
author2 Pollero, Ricardo José
Cabello, Marta Noemí
author2_role author
author
dc.subject.none.fl_str_mv Bioquímica
Ciencias Naturales
Acyl-CoA ligase
Acylglycerol synthetase
External mycelium
Lipase activity
Triacylglycerols
topic Bioquímica
Ciencias Naturales
Acyl-CoA ligase
Acylglycerol synthetase
External mycelium
Lipase activity
Triacylglycerols
dc.description.none.fl_txt_mv The activities of enzymes involved in the glyceride metabolism of <i>Glomus mosseae</i> external mycelium are reported. Total mycelial homogenates were incubated with radiolabeled triolein and palmitic acid for various times under different conditions. The results obtained demonstrate the capacity of <i>G. mosseae</i> external mycelium to synthesize and hydrolyze its own acylglycerides. Neutral lipid biosynthesis progressively increased along with root colonization. Incorporation of [¹⁴C]-palmitate was mainly into triacylglycerols and as a minor fraction into diacylglycerols. The activity of palmitoyl-CoA ligase in external mycelium also increased in parallel with mycorrhiza development. The hydrolysis of triacylglycerols was very low at the beginning of colonization and then increased. However, lipase activity was lower than that of acyl-CoA ligase even at late stages of colonization. Thus, triacylglycerol biosynthesis apparently prevails over degradation during <i>G. mosseae</i> mycelium development in the period examined.
Instituto de Investigaciones Bioquímicas de La Plata
Instituto de Botánica "Dr. Carlos Spegazzini"
description The activities of enzymes involved in the glyceride metabolism of <i>Glomus mosseae</i> external mycelium are reported. Total mycelial homogenates were incubated with radiolabeled triolein and palmitic acid for various times under different conditions. The results obtained demonstrate the capacity of <i>G. mosseae</i> external mycelium to synthesize and hydrolyze its own acylglycerides. Neutral lipid biosynthesis progressively increased along with root colonization. Incorporation of [¹⁴C]-palmitate was mainly into triacylglycerols and as a minor fraction into diacylglycerols. The activity of palmitoyl-CoA ligase in external mycelium also increased in parallel with mycorrhiza development. The hydrolysis of triacylglycerols was very low at the beginning of colonization and then increased. However, lipase activity was lower than that of acyl-CoA ligase even at late stages of colonization. Thus, triacylglycerol biosynthesis apparently prevails over degradation during <i>G. mosseae</i> mycelium development in the period examined.
publishDate 2001
dc.date.none.fl_str_mv 2001-10
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/141441
url http://sedici.unlp.edu.ar/handle/10915/141441
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/0940-6360
info:eu-repo/semantics/altIdentifier/issn/1432-1890
info:eu-repo/semantics/altIdentifier/doi/10.1007/s005720100130
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.format.none.fl_str_mv application/pdf
257-261
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 13.070432

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