Bacteria producing L-asparaginase isolated from Peruvian saline environments
Descripción del Articulo
L-asparaginase (EC 3.5.1.1) hydrolyzes L-asparagine in L-aspartic acid and ammonia. Its efficiency is subject to its kinetics and specificity on the substrate, characteristics that vary from one source to another. Thus, microorganisms from saline environments constitute a phylogenetic and metabolica...
| Autores: | , , , , , , |
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| Formato: | artículo |
| Fecha de Publicación: | 2021 |
| Institución: | Universidad Nacional de Tumbes |
| Repositorio: | Revistas - Universidad Nacional de Tumbes |
| Lenguaje: | español |
| OAI Identifier: | oai:ojs.www.untumbes.edu.pe:article/243 |
| Enlace del recurso: | https://erp.untumbes.edu.pe/revistas/index.php/manglar/article/view/243 |
| Nivel de acceso: | acceso abierto |
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Bacteria producing L-asparaginase isolated from Peruvian saline environmentsMontes, Jeanett; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima.Canales, Pamela Elizabeth; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima.Flores-Santos, Juan Carlos; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima.Saavedra, Stephy; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima.Hurtado-Gómez, Abad; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima.Esquerre-Huallpa, Cynthia; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima.Iris Zavaleta, Amparo; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima.L-asparaginase (EC 3.5.1.1) hydrolyzes L-asparagine in L-aspartic acid and ammonia. Its efficiency is subject to its kinetics and specificity on the substrate, characteristics that vary from one source to another. Thus, microorganisms from saline environments constitute a phylogenetic and metabolically heterogeneous group for the search of new enzymes. Therefore, the objective of this study was the phenotypic and genotypic characterization of bacteria with L-asparaginase activity isolated from Maras, Pilluana and Chilca salterns. The 24 evaluated bacteria were classified as 38% Gram-negative bacilli and 54% positive; and 8% Gram-positive cocci. The majority grew in 5% salt water, pH 7.0 and 37 °C, all assimilated glucose. Of the 24 bacteria that produced L-asparaginase in solid medium, enzymatic activity was determined in submerged cultures by the Nessler method in 14 of them. The CH11, M62, M64, M68, and P19 strains identified as Bacillus sp., by partial sequencing of the 16S ribosomal gene, presented higher L-asparaginase activity and instability due to the presence of proteases. Saline environments bacteria are potential sources for the prospective production of L-asparaginase to use them as a therapeutic agent and in the food industry.Manglar2021-06-22info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://erp.untumbes.edu.pe/revistas/index.php/manglar/article/view/24310.17268/manglar.2021.026Manglar; Vol. 18, núm. 2 (2021): Abril-Junio; 193-1991816-7667reponame:Revistas - Universidad Nacional de Tumbesinstname:Universidad Nacional de Tumbesinstacron:UNTUMBESspahttps://erp.untumbes.edu.pe/revistas/index.php/manglar/article/view/243/368Copyright (c) 2022 Jeanett Montes, Pamela Elizabeth Canales, Juan Carlos Flores-Santos, Stephy Saavedra, Abad Hurtado-Gómez, Cynthia Esquerre-Huallpa, Amparo Iris Zavaletahttp://creativecommons.org/licenses/by/4.0info:eu-repo/semantics/openAccessoai:ojs.www.untumbes.edu.pe:article/2432021-06-22T05:38:48Z |
| dc.title.none.fl_str_mv |
Bacteria producing L-asparaginase isolated from Peruvian saline environments |
| title |
Bacteria producing L-asparaginase isolated from Peruvian saline environments |
| spellingShingle |
Bacteria producing L-asparaginase isolated from Peruvian saline environments Montes, Jeanett; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima. |
| title_short |
Bacteria producing L-asparaginase isolated from Peruvian saline environments |
| title_full |
Bacteria producing L-asparaginase isolated from Peruvian saline environments |
| title_fullStr |
Bacteria producing L-asparaginase isolated from Peruvian saline environments |
| title_full_unstemmed |
Bacteria producing L-asparaginase isolated from Peruvian saline environments |
| title_sort |
Bacteria producing L-asparaginase isolated from Peruvian saline environments |
| dc.creator.none.fl_str_mv |
Montes, Jeanett; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima. Canales, Pamela Elizabeth; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima. Flores-Santos, Juan Carlos; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima. Saavedra, Stephy; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima. Hurtado-Gómez, Abad; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima. Esquerre-Huallpa, Cynthia; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima. Iris Zavaleta, Amparo; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima. |
| author |
Montes, Jeanett; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima. |
| author_facet |
Montes, Jeanett; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima. Canales, Pamela Elizabeth; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima. Flores-Santos, Juan Carlos; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima. Saavedra, Stephy; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima. Hurtado-Gómez, Abad; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima. Esquerre-Huallpa, Cynthia; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima. Iris Zavaleta, Amparo; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima. |
| author_role |
author |
| author2 |
Canales, Pamela Elizabeth; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima. Flores-Santos, Juan Carlos; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima. Saavedra, Stephy; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima. Hurtado-Gómez, Abad; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima. Esquerre-Huallpa, Cynthia; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima. Iris Zavaleta, Amparo; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima. |
| author2_role |
author author author author author author |
| dc.contributor.none.fl_str_mv |
|
| description |
L-asparaginase (EC 3.5.1.1) hydrolyzes L-asparagine in L-aspartic acid and ammonia. Its efficiency is subject to its kinetics and specificity on the substrate, characteristics that vary from one source to another. Thus, microorganisms from saline environments constitute a phylogenetic and metabolically heterogeneous group for the search of new enzymes. Therefore, the objective of this study was the phenotypic and genotypic characterization of bacteria with L-asparaginase activity isolated from Maras, Pilluana and Chilca salterns. The 24 evaluated bacteria were classified as 38% Gram-negative bacilli and 54% positive; and 8% Gram-positive cocci. The majority grew in 5% salt water, pH 7.0 and 37 °C, all assimilated glucose. Of the 24 bacteria that produced L-asparaginase in solid medium, enzymatic activity was determined in submerged cultures by the Nessler method in 14 of them. The CH11, M62, M64, M68, and P19 strains identified as Bacillus sp., by partial sequencing of the 16S ribosomal gene, presented higher L-asparaginase activity and instability due to the presence of proteases. Saline environments bacteria are potential sources for the prospective production of L-asparaginase to use them as a therapeutic agent and in the food industry. |
| publishDate |
2021 |
| dc.date.none.fl_str_mv |
2021-06-22 |
| dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion |
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article |
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publishedVersion |
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https://erp.untumbes.edu.pe/revistas/index.php/manglar/article/view/243 10.17268/manglar.2021.026 |
| url |
https://erp.untumbes.edu.pe/revistas/index.php/manglar/article/view/243 |
| identifier_str_mv |
10.17268/manglar.2021.026 |
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spa |
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spa |
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https://erp.untumbes.edu.pe/revistas/index.php/manglar/article/view/243/368 |
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http://creativecommons.org/licenses/by/4.0 info:eu-repo/semantics/openAccess |
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http://creativecommons.org/licenses/by/4.0 |
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openAccess |
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application/pdf |
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Manglar |
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Manglar |
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Manglar; Vol. 18, núm. 2 (2021): Abril-Junio; 193-199 1816-7667 reponame:Revistas - Universidad Nacional de Tumbes instname:Universidad Nacional de Tumbes instacron:UNTUMBES |
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La información contenida en este registro es de entera responsabilidad de la institución que gestiona el repositorio institucional donde esta contenido este documento o set de datos. El CONCYTEC no se hace responsable por los contenidos (publicaciones y/o datos) accesibles a través del Repositorio Nacional Digital de Ciencia, Tecnología e Innovación de Acceso Abierto (ALICIA).