Lipolytic activity in free and immobilized cells of Phoma glomerata

Autores
Pollero, Ricardo José; Gaspar, María Laura; Cabello, Marta Noemí
Año de publicación
1997
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The lipolytic activity of free and immobilized whole cells of the pathogenic fungus Phoma glomerata was demonstrated, and several properties of the lipase involved were determined. Free fungal cells and small pieces of immobilized cells, prepared by spontaneous colonization on a solid surface or entrapped in calcium alginate, were incubated with triolein in buffered medium. Different incubation conditions were assayed to optimize the reaction, to determine the effects of heating and time on stability of the immobilized preparations and the time course of the reactions. Although the enzyme cleaves all ester bonds of triolein, it shows some preference for the outer bonds. An optimal pH of 7.5–8.0, optimal temperature of 45°C for free and 50°C for immobilized cell preparations, the necessity for substrate emulsifiers, and reaction independence from calcium and magnesium were demonstrated. Results suggest that immobilized whole cells of P. glomerata would be a suitable tool to study its lipid physiology and to explore further the possible biotechnological use of its lipase activity.
Instituto de Investigaciones Bioquímicas de La Plata
Materia
Ciencias Médicas
Química
Fungal lipase
immobilized cells
lipase
lipids
lipolytic activity
microbial enzyme
Phoma
triacylglycerol hydrolysis
triolein degradation
whole cells
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:10915/140856
Acceder
id SEDICI_70bea57deae1d09139c5afdfb9f2b3ef
oai_identifier_str oai:sedici.unlp.edu.ar:10915/140856
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Lipolytic activity in free and immobilized cells of Phoma glomerataPollero, Ricardo JoséGaspar, María LauraCabello, Marta NoemíCiencias MédicasQuímicaFungal lipaseimmobilized cellslipaselipidslipolytic activitymicrobial enzymePhomatriacylglycerol hydrolysistriolein degradationwhole cellsThe lipolytic activity of free and immobilized whole cells of the pathogenic fungus Phoma glomerata was demonstrated, and several properties of the lipase involved were determined. Free fungal cells and small pieces of immobilized cells, prepared by spontaneous colonization on a solid surface or entrapped in calcium alginate, were incubated with triolein in buffered medium. Different incubation conditions were assayed to optimize the reaction, to determine the effects of heating and time on stability of the immobilized preparations and the time course of the reactions. Although the enzyme cleaves all ester bonds of triolein, it shows some preference for the outer bonds. An optimal pH of 7.5–8.0, optimal temperature of 45°C for free and 50°C for immobilized cell preparations, the necessity for substrate emulsifiers, and reaction independence from calcium and magnesium were demonstrated. Results suggest that immobilized whole cells of P. glomerata would be a suitable tool to study its lipid physiology and to explore further the possible biotechnological use of its lipase activity.Instituto de Investigaciones Bioquímicas de La Plata1997-04-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf451-454http://sedici.unlp.edu.ar/handle/10915/140856enginfo:eu-repo/semantics/altIdentifier/issn/0003-021xinfo:eu-repo/semantics/altIdentifier/issn/1558-9331info:eu-repo/semantics/altIdentifier/doi/10.1007/s11746-997-0105-1info: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:UNLP2025-09-29T11:32:07Zoai:sedici.unlp.edu.ar:10915/140856Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:32:08.282SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Lipolytic activity in free and immobilized cells of Phoma glomerata
title Lipolytic activity in free and immobilized cells of Phoma glomerata
spellingShingle Lipolytic activity in free and immobilized cells of Phoma glomerata
Pollero, Ricardo José
Ciencias Médicas
Química
Fungal lipase
immobilized cells
lipase
lipids
lipolytic activity
microbial enzyme
Phoma
triacylglycerol hydrolysis
triolein degradation
whole cells
title_short Lipolytic activity in free and immobilized cells of Phoma glomerata
title_full Lipolytic activity in free and immobilized cells of Phoma glomerata
title_fullStr Lipolytic activity in free and immobilized cells of Phoma glomerata
title_full_unstemmed Lipolytic activity in free and immobilized cells of Phoma glomerata
title_sort Lipolytic activity in free and immobilized cells of Phoma glomerata
dc.creator.none.fl_str_mv Pollero, Ricardo José
Gaspar, María Laura
Cabello, Marta Noemí
author Pollero, Ricardo José
author_facet Pollero, Ricardo José
Gaspar, María Laura
Cabello, Marta Noemí
author_role author
author2 Gaspar, María Laura
Cabello, Marta Noemí
author2_role author
author
dc.subject.none.fl_str_mv Ciencias Médicas
Química
Fungal lipase
immobilized cells
lipase
lipids
lipolytic activity
microbial enzyme
Phoma
triacylglycerol hydrolysis
triolein degradation
whole cells
topic Ciencias Médicas
Química
Fungal lipase
immobilized cells
lipase
lipids
lipolytic activity
microbial enzyme
Phoma
triacylglycerol hydrolysis
triolein degradation
whole cells
dc.description.none.fl_txt_mv The lipolytic activity of free and immobilized whole cells of the pathogenic fungus Phoma glomerata was demonstrated, and several properties of the lipase involved were determined. Free fungal cells and small pieces of immobilized cells, prepared by spontaneous colonization on a solid surface or entrapped in calcium alginate, were incubated with triolein in buffered medium. Different incubation conditions were assayed to optimize the reaction, to determine the effects of heating and time on stability of the immobilized preparations and the time course of the reactions. Although the enzyme cleaves all ester bonds of triolein, it shows some preference for the outer bonds. An optimal pH of 7.5–8.0, optimal temperature of 45°C for free and 50°C for immobilized cell preparations, the necessity for substrate emulsifiers, and reaction independence from calcium and magnesium were demonstrated. Results suggest that immobilized whole cells of P. glomerata would be a suitable tool to study its lipid physiology and to explore further the possible biotechnological use of its lipase activity.
Instituto de Investigaciones Bioquímicas de La Plata
description The lipolytic activity of free and immobilized whole cells of the pathogenic fungus Phoma glomerata was demonstrated, and several properties of the lipase involved were determined. Free fungal cells and small pieces of immobilized cells, prepared by spontaneous colonization on a solid surface or entrapped in calcium alginate, were incubated with triolein in buffered medium. Different incubation conditions were assayed to optimize the reaction, to determine the effects of heating and time on stability of the immobilized preparations and the time course of the reactions. Although the enzyme cleaves all ester bonds of triolein, it shows some preference for the outer bonds. An optimal pH of 7.5–8.0, optimal temperature of 45°C for free and 50°C for immobilized cell preparations, the necessity for substrate emulsifiers, and reaction independence from calcium and magnesium were demonstrated. Results suggest that immobilized whole cells of P. glomerata would be a suitable tool to study its lipid physiology and to explore further the possible biotechnological use of its lipase activity.
publishDate 1997
dc.date.none.fl_str_mv 1997-04-01
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/10915/140856
url http://sedici.unlp.edu.ar/handle/10915/140856
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/0003-021x
info:eu-repo/semantics/altIdentifier/issn/1558-9331
info:eu-repo/semantics/altIdentifier/doi/10.1007/s11746-997-0105-1
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
451-454
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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