Esterolytic and lipolytic activities of lactic acid bacteria isolated from ewe's milk and cheese
- Autores
- Katz, Marta; Medina, Roxana Beatriz; Gonzalez, Silvia Nelina; Oliver, Guillermo
- Año de publicación
- 2002
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- In the present work, we report on the esterase and lipase activities of lactic acid bacteria representing the genera Lactococcus, Leuconostoc, Lactobacillus, and Enterococcus isolated from ewe’s milk and cheeses. Esterase activity was studied using a- and b-naphthyl derivatives of 2 to 12 carbon atoms and postelectrophoretic detection. The lactic acid bacteria evaluated had intracellular esterase activities, which preferentially degraded the a- and b-naphthyl derivatives of 2 to 6 carbon atoms. By studying postelectrophoretic patterns, it was found that some strains presented more than one esterase. Lactobacillus plantarum O236 showed four enzymes that hydrolyze carboxyl ester linkages with different speci city. Lipase activity was studied in intracellular and extracellular fractions using tributyrin, tricaprylin, triolein, and milk fat as substrates. The intracellular and extracellular fractions of Leuconostoc mesenteroides O257, Lactobacillus plantarum O236, and Lactobacillus acidophilus O177 were able to hydrolyze tributyrin. L. plantarum O186, L. acidophilus O252, Enterococcus faecium O174 and O426, and Enterococcus faecalis Ov409 showed lipase activity associated with the intracellular fraction on tributyrin. Lactococcus lactis O233, L. plantarum O155, and Lactobacillus casei O190 did not hydrolyze triglycerides. Not all strains that showed esterase activity exhibited high activity on triglycerides. Esterase and lipase activities were species- and strainspeci c. Wide variations in activity between strains highlight the need for selecting appropriate starters to produce enzyme-modified cheese as well as accelerated ripened cheese.
Fil: Katz, Marta. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina. Universidad Nacional de Salta; Argentina
Fil: Medina, Roxana Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina
Fil: Gonzalez, Silvia Nelina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina
Fil: Oliver, Guillermo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina - Materia
-
ESTERASES
LIPASES
LACTIC ACID BACTERIA
EWE'S MILK CHEESE - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/112374
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Esterolytic and lipolytic activities of lactic acid bacteria isolated from ewe's milk and cheeseKatz, MartaMedina, Roxana BeatrizGonzalez, Silvia NelinaOliver, GuillermoESTERASESLIPASESLACTIC ACID BACTERIAEWE'S MILK CHEESEhttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2In the present work, we report on the esterase and lipase activities of lactic acid bacteria representing the genera Lactococcus, Leuconostoc, Lactobacillus, and Enterococcus isolated from ewe’s milk and cheeses. Esterase activity was studied using a- and b-naphthyl derivatives of 2 to 12 carbon atoms and postelectrophoretic detection. The lactic acid bacteria evaluated had intracellular esterase activities, which preferentially degraded the a- and b-naphthyl derivatives of 2 to 6 carbon atoms. By studying postelectrophoretic patterns, it was found that some strains presented more than one esterase. Lactobacillus plantarum O236 showed four enzymes that hydrolyze carboxyl ester linkages with different speci city. Lipase activity was studied in intracellular and extracellular fractions using tributyrin, tricaprylin, triolein, and milk fat as substrates. The intracellular and extracellular fractions of Leuconostoc mesenteroides O257, Lactobacillus plantarum O236, and Lactobacillus acidophilus O177 were able to hydrolyze tributyrin. L. plantarum O186, L. acidophilus O252, Enterococcus faecium O174 and O426, and Enterococcus faecalis Ov409 showed lipase activity associated with the intracellular fraction on tributyrin. Lactococcus lactis O233, L. plantarum O155, and Lactobacillus casei O190 did not hydrolyze triglycerides. Not all strains that showed esterase activity exhibited high activity on triglycerides. Esterase and lipase activities were species- and strainspeci c. Wide variations in activity between strains highlight the need for selecting appropriate starters to produce enzyme-modified cheese as well as accelerated ripened cheese.Fil: Katz, Marta. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina. Universidad Nacional de Salta; ArgentinaFil: Medina, Roxana Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; ArgentinaFil: Gonzalez, Silvia Nelina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; ArgentinaFil: Oliver, Guillermo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; ArgentinaInternational Association for Food Protection2002-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/112374Katz, Marta; Medina, Roxana Beatriz; Gonzalez, Silvia Nelina; Oliver, Guillermo; Esterolytic and lipolytic activities of lactic acid bacteria isolated from ewe's milk and cheese; International Association for Food Protection; Journal of Food Protection; 65; 12; 12-2002; 1997-20010362-028X1944-9097CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.4315/0362-028x-65.12.1997info:eu-repo/semantics/altIdentifier/url/https://meridian.allenpress.com/jfp/article/65/12/1997/169707/Esterolytic-and-Lipolytic-Activities-of-Lacticinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:52:37Zoai:ri.conicet.gov.ar:11336/112374instacron: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:34982025-09-03 09:52:37.501CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Esterolytic and lipolytic activities of lactic acid bacteria isolated from ewe's milk and cheese |
title |
Esterolytic and lipolytic activities of lactic acid bacteria isolated from ewe's milk and cheese |
spellingShingle |
Esterolytic and lipolytic activities of lactic acid bacteria isolated from ewe's milk and cheese Katz, Marta ESTERASES LIPASES LACTIC ACID BACTERIA EWE'S MILK CHEESE |
title_short |
Esterolytic and lipolytic activities of lactic acid bacteria isolated from ewe's milk and cheese |
title_full |
Esterolytic and lipolytic activities of lactic acid bacteria isolated from ewe's milk and cheese |
title_fullStr |
Esterolytic and lipolytic activities of lactic acid bacteria isolated from ewe's milk and cheese |
title_full_unstemmed |
Esterolytic and lipolytic activities of lactic acid bacteria isolated from ewe's milk and cheese |
title_sort |
Esterolytic and lipolytic activities of lactic acid bacteria isolated from ewe's milk and cheese |
dc.creator.none.fl_str_mv |
Katz, Marta Medina, Roxana Beatriz Gonzalez, Silvia Nelina Oliver, Guillermo |
author |
Katz, Marta |
author_facet |
Katz, Marta Medina, Roxana Beatriz Gonzalez, Silvia Nelina Oliver, Guillermo |
author_role |
author |
author2 |
Medina, Roxana Beatriz Gonzalez, Silvia Nelina Oliver, Guillermo |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
ESTERASES LIPASES LACTIC ACID BACTERIA EWE'S MILK CHEESE |
topic |
ESTERASES LIPASES LACTIC ACID BACTERIA EWE'S MILK CHEESE |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/2.11 https://purl.org/becyt/ford/2 |
dc.description.none.fl_txt_mv |
In the present work, we report on the esterase and lipase activities of lactic acid bacteria representing the genera Lactococcus, Leuconostoc, Lactobacillus, and Enterococcus isolated from ewe’s milk and cheeses. Esterase activity was studied using a- and b-naphthyl derivatives of 2 to 12 carbon atoms and postelectrophoretic detection. The lactic acid bacteria evaluated had intracellular esterase activities, which preferentially degraded the a- and b-naphthyl derivatives of 2 to 6 carbon atoms. By studying postelectrophoretic patterns, it was found that some strains presented more than one esterase. Lactobacillus plantarum O236 showed four enzymes that hydrolyze carboxyl ester linkages with different speci city. Lipase activity was studied in intracellular and extracellular fractions using tributyrin, tricaprylin, triolein, and milk fat as substrates. The intracellular and extracellular fractions of Leuconostoc mesenteroides O257, Lactobacillus plantarum O236, and Lactobacillus acidophilus O177 were able to hydrolyze tributyrin. L. plantarum O186, L. acidophilus O252, Enterococcus faecium O174 and O426, and Enterococcus faecalis Ov409 showed lipase activity associated with the intracellular fraction on tributyrin. Lactococcus lactis O233, L. plantarum O155, and Lactobacillus casei O190 did not hydrolyze triglycerides. Not all strains that showed esterase activity exhibited high activity on triglycerides. Esterase and lipase activities were species- and strainspeci c. Wide variations in activity between strains highlight the need for selecting appropriate starters to produce enzyme-modified cheese as well as accelerated ripened cheese. Fil: Katz, Marta. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina. Universidad Nacional de Salta; Argentina Fil: Medina, Roxana Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina Fil: Gonzalez, Silvia Nelina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina Fil: Oliver, Guillermo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina |
description |
In the present work, we report on the esterase and lipase activities of lactic acid bacteria representing the genera Lactococcus, Leuconostoc, Lactobacillus, and Enterococcus isolated from ewe’s milk and cheeses. Esterase activity was studied using a- and b-naphthyl derivatives of 2 to 12 carbon atoms and postelectrophoretic detection. The lactic acid bacteria evaluated had intracellular esterase activities, which preferentially degraded the a- and b-naphthyl derivatives of 2 to 6 carbon atoms. By studying postelectrophoretic patterns, it was found that some strains presented more than one esterase. Lactobacillus plantarum O236 showed four enzymes that hydrolyze carboxyl ester linkages with different speci city. Lipase activity was studied in intracellular and extracellular fractions using tributyrin, tricaprylin, triolein, and milk fat as substrates. The intracellular and extracellular fractions of Leuconostoc mesenteroides O257, Lactobacillus plantarum O236, and Lactobacillus acidophilus O177 were able to hydrolyze tributyrin. L. plantarum O186, L. acidophilus O252, Enterococcus faecium O174 and O426, and Enterococcus faecalis Ov409 showed lipase activity associated with the intracellular fraction on tributyrin. Lactococcus lactis O233, L. plantarum O155, and Lactobacillus casei O190 did not hydrolyze triglycerides. Not all strains that showed esterase activity exhibited high activity on triglycerides. Esterase and lipase activities were species- and strainspeci c. Wide variations in activity between strains highlight the need for selecting appropriate starters to produce enzyme-modified cheese as well as accelerated ripened cheese. |
publishDate |
2002 |
dc.date.none.fl_str_mv |
2002-12 |
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/11336/112374 Katz, Marta; Medina, Roxana Beatriz; Gonzalez, Silvia Nelina; Oliver, Guillermo; Esterolytic and lipolytic activities of lactic acid bacteria isolated from ewe's milk and cheese; International Association for Food Protection; Journal of Food Protection; 65; 12; 12-2002; 1997-2001 0362-028X 1944-9097 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/112374 |
identifier_str_mv |
Katz, Marta; Medina, Roxana Beatriz; Gonzalez, Silvia Nelina; Oliver, Guillermo; Esterolytic and lipolytic activities of lactic acid bacteria isolated from ewe's milk and cheese; International Association for Food Protection; Journal of Food Protection; 65; 12; 12-2002; 1997-2001 0362-028X 1944-9097 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.4315/0362-028x-65.12.1997 info:eu-repo/semantics/altIdentifier/url/https://meridian.allenpress.com/jfp/article/65/12/1997/169707/Esterolytic-and-Lipolytic-Activities-of-Lactic |
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 |
International Association for Food Protection |
publisher.none.fl_str_mv |
International Association for Food Protection |
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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1842269171310657536 |
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13.13397 |