Alkaline and thermostable polygalacturonase from Streptomyces halstedii ATCC 10897 with applications in waste waters

Autores
Ramírez Tapias, Yuly Andrea; Rivero, Cintia Wanda; Britos, Claudia Noelia; Trelles, Jorge Abel
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Pectin degrading enzymes with polygalacturonase (PG) activity hydrolyze α-(1,4) glycosidic bonds of polysaccharides present in higher plants. In the current study one hundred bacterial strains were screened for extracellular PG activity using an inductive culture medium. Optimization of fermentation conditions for Streptomyces halstedii ATCC 10897 was conducted using experimental designs. The maximum enzymatic activity obtained was 3.489. U/mL and 98.0% of viscosity reduction after 12. h of fermentation using soy peptone as unique source of carbon and nitrogen. PG from S. halstedii ATCC 10897 showed high thermal stability, an approximate molecular weight of 48. kDa and its optimum conditions for catalytic reaction were 50. °C and pH 12.0. This study reveals that alkaline PG is a useful enzyme for depectinization in alkaline pulping mill and papermaking waste waters. halstedii produces extremely alkalophilic polygalacturonase (48kDa) at 12h.
Fil: Ramírez Tapias, Yuly Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; Argentina
Fil: Rivero, Cintia Wanda. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; Argentina
Fil: Britos, Claudia Noelia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; Argentina
Fil: Trelles, Jorge Abel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; Argentina
Materia
Culture Medium Design
Fermentation Optimization
Screening
Waste Waters
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:11336/51013
Acceder
id CONICETDig_c8fd6cecb4d96f8fea2f4f234164a9fa
oai_identifier_str oai:ri.conicet.gov.ar:11336/51013
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Alkaline and thermostable polygalacturonase from Streptomyces halstedii ATCC 10897 with applications in waste watersRamírez Tapias, Yuly AndreaRivero, Cintia WandaBritos, Claudia NoeliaTrelles, Jorge AbelCulture Medium DesignFermentation OptimizationScreeningWaste Watershttps://purl.org/becyt/ford/2.4https://purl.org/becyt/ford/2Pectin degrading enzymes with polygalacturonase (PG) activity hydrolyze α-(1,4) glycosidic bonds of polysaccharides present in higher plants. In the current study one hundred bacterial strains were screened for extracellular PG activity using an inductive culture medium. Optimization of fermentation conditions for Streptomyces halstedii ATCC 10897 was conducted using experimental designs. The maximum enzymatic activity obtained was 3.489. U/mL and 98.0% of viscosity reduction after 12. h of fermentation using soy peptone as unique source of carbon and nitrogen. PG from S. halstedii ATCC 10897 showed high thermal stability, an approximate molecular weight of 48. kDa and its optimum conditions for catalytic reaction were 50. °C and pH 12.0. This study reveals that alkaline PG is a useful enzyme for depectinization in alkaline pulping mill and papermaking waste waters. halstedii produces extremely alkalophilic polygalacturonase (48kDa) at 12h.Fil: Ramírez Tapias, Yuly Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; ArgentinaFil: Rivero, Cintia Wanda. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; ArgentinaFil: Britos, Claudia Noelia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; ArgentinaFil: Trelles, Jorge Abel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; ArgentinaElsevier2015-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/51013Ramírez Tapias, Yuly Andrea; Rivero, Cintia Wanda; Britos, Claudia Noelia; Trelles, Jorge Abel; Alkaline and thermostable polygalacturonase from Streptomyces halstedii ATCC 10897 with applications in waste waters; Elsevier; Biocatalysis and Agricultural Biotechnology; 4; 2; 4-2015; 221-2281878-8181CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bcab.2014.12.004info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1878818114001546info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:34:35Zoai:ri.conicet.gov.ar:11336/51013instacron: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 09:34:36.208CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Alkaline and thermostable polygalacturonase from Streptomyces halstedii ATCC 10897 with applications in waste waters
title Alkaline and thermostable polygalacturonase from Streptomyces halstedii ATCC 10897 with applications in waste waters
spellingShingle Alkaline and thermostable polygalacturonase from Streptomyces halstedii ATCC 10897 with applications in waste waters
Ramírez Tapias, Yuly Andrea
Culture Medium Design
Fermentation Optimization
Screening
Waste Waters
title_short Alkaline and thermostable polygalacturonase from Streptomyces halstedii ATCC 10897 with applications in waste waters
title_full Alkaline and thermostable polygalacturonase from Streptomyces halstedii ATCC 10897 with applications in waste waters
title_fullStr Alkaline and thermostable polygalacturonase from Streptomyces halstedii ATCC 10897 with applications in waste waters
title_full_unstemmed Alkaline and thermostable polygalacturonase from Streptomyces halstedii ATCC 10897 with applications in waste waters
title_sort Alkaline and thermostable polygalacturonase from Streptomyces halstedii ATCC 10897 with applications in waste waters
dc.creator.none.fl_str_mv Ramírez Tapias, Yuly Andrea
Rivero, Cintia Wanda
Britos, Claudia Noelia
Trelles, Jorge Abel
author Ramírez Tapias, Yuly Andrea
author_facet Ramírez Tapias, Yuly Andrea
Rivero, Cintia Wanda
Britos, Claudia Noelia
Trelles, Jorge Abel
author_role author
author2 Rivero, Cintia Wanda
Britos, Claudia Noelia
Trelles, Jorge Abel
author2_role author
author
author
dc.subject.none.fl_str_mv Culture Medium Design
Fermentation Optimization
Screening
Waste Waters
topic Culture Medium Design
Fermentation Optimization
Screening
Waste Waters
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.4
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Pectin degrading enzymes with polygalacturonase (PG) activity hydrolyze α-(1,4) glycosidic bonds of polysaccharides present in higher plants. In the current study one hundred bacterial strains were screened for extracellular PG activity using an inductive culture medium. Optimization of fermentation conditions for Streptomyces halstedii ATCC 10897 was conducted using experimental designs. The maximum enzymatic activity obtained was 3.489. U/mL and 98.0% of viscosity reduction after 12. h of fermentation using soy peptone as unique source of carbon and nitrogen. PG from S. halstedii ATCC 10897 showed high thermal stability, an approximate molecular weight of 48. kDa and its optimum conditions for catalytic reaction were 50. °C and pH 12.0. This study reveals that alkaline PG is a useful enzyme for depectinization in alkaline pulping mill and papermaking waste waters. halstedii produces extremely alkalophilic polygalacturonase (48kDa) at 12h.
Fil: Ramírez Tapias, Yuly Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; Argentina
Fil: Rivero, Cintia Wanda. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; Argentina
Fil: Britos, Claudia Noelia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; Argentina
Fil: Trelles, Jorge Abel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; Argentina
description Pectin degrading enzymes with polygalacturonase (PG) activity hydrolyze α-(1,4) glycosidic bonds of polysaccharides present in higher plants. In the current study one hundred bacterial strains were screened for extracellular PG activity using an inductive culture medium. Optimization of fermentation conditions for Streptomyces halstedii ATCC 10897 was conducted using experimental designs. The maximum enzymatic activity obtained was 3.489. U/mL and 98.0% of viscosity reduction after 12. h of fermentation using soy peptone as unique source of carbon and nitrogen. PG from S. halstedii ATCC 10897 showed high thermal stability, an approximate molecular weight of 48. kDa and its optimum conditions for catalytic reaction were 50. °C and pH 12.0. This study reveals that alkaline PG is a useful enzyme for depectinization in alkaline pulping mill and papermaking waste waters. halstedii produces extremely alkalophilic polygalacturonase (48kDa) at 12h.
publishDate 2015
dc.date.none.fl_str_mv 2015-04
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/11336/51013
Ramírez Tapias, Yuly Andrea; Rivero, Cintia Wanda; Britos, Claudia Noelia; Trelles, Jorge Abel; Alkaline and thermostable polygalacturonase from Streptomyces halstedii ATCC 10897 with applications in waste waters; Elsevier; Biocatalysis and Agricultural Biotechnology; 4; 2; 4-2015; 221-228
1878-8181
CONICET Digital
CONICET
url http://hdl.handle.net/11336/51013
identifier_str_mv Ramírez Tapias, Yuly Andrea; Rivero, Cintia Wanda; Britos, Claudia Noelia; Trelles, Jorge Abel; Alkaline and thermostable polygalacturonase from Streptomyces halstedii ATCC 10897 with applications in waste waters; Elsevier; Biocatalysis and Agricultural Biotechnology; 4; 2; 4-2015; 221-228
1878-8181
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bcab.2014.12.004
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1878818114001546
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 Elsevier
publisher.none.fl_str_mv Elsevier
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
_version_ 1844613071370190848
score 13.070432

Publicaciones similares