Characteristics of a Cold-Adapted L-glutaminase with Potential Applications in the Food Industry

Autores
Ferreira, Flavia Vanina; Herrmann Andrade, Andreina M.; Binolfi, Andrés; Calabrese, Carla D.; Mac Cormack, Walter Patricio; Musumeci, Matias Alejandro
Año de publicación
2021
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
L-glutaminases are enzymes that catalyze the hydrolysis of L-glutamine, producing L-glutamate and ammonium, and they have promising applications in pharmaceutical and food industries. Several investigations have focused on thermo-tolerant L-glutaminases; however, studies on cold-adapted L-glutaminases have not been reported. These enzymes could be useful in the food industry because they display high catalytic activity at low and room temperatures, a valuable feature in processes aimed to save energy. Besides, they can be easily inactivated by warming and are suitable to prevent decomposition of thermo-labile compounds. The objectives of this work were to characterize the L-glutaminase from the Antarctic bacterium Bizionia argentinensis and analyze its capability as flavor enhancer of protein hydrolysates. The enzyme was heterologously expressed and purified from Escherichia coli, obtaining optimum and homogeneous yields. Kinetic parameters Km and Vmax were located at the lower and upper range of values reported for L-glutaminases, suggesting high catalytic efficiency. Optimum temperature was 25 °C, and the enzyme conserved around 90% of maximum activity at 0 °C and in presence of 15% (v/v) ethanol and methanol. In saline conditions, the enzyme conserved around 80% of maximum activity in 3 M NaCl. Analysis of structural model suggested cold-adaptation features such as low Arg/(Arg+Lys) ratio and fewer intramolecular interactions than mesophilic and thermo-tolerant L-glutaminases. This work provides a novel cold-adapted L-glutaminase with promising features in the food industry.
Fil: Ferreira, Flavia Vanina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Entre Ríos. Universidad Nacional de Entre Ríos. Centro de Investigaciones y Transferencia de Entre Ríos; Argentina
Fil: Herrmann Andrade, Andreina M.. Universidad Nacional de Entre Rios. Facultad de Cs. de la Alimentación. Departamento de Cs. de Los Alimentos; Argentina
Fil: Binolfi, Andrés. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Calabrese, Carla D.. Universidad Nacional de Entre Rios. Facultad de Cs. de la Alimentación. Departamento de Cs. de Los Alimentos; Argentina
Fil: Mac Cormack, Walter Patricio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina
Fil: Musumeci, Matias Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Entre Ríos. Universidad Nacional de Entre Ríos. Centro de Investigaciones y Transferencia de Entre Ríos; Argentina
Materia
COLD-ADAPTED ENZYMES
FOOD INDUSTRY
L-GLUTAMINASES
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:11336/184534
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Characteristics of a Cold-Adapted L-glutaminase with Potential Applications in the Food IndustryFerreira, Flavia VaninaHerrmann Andrade, Andreina M.Binolfi, AndrésCalabrese, Carla D.Mac Cormack, Walter PatricioMusumeci, Matias AlejandroCOLD-ADAPTED ENZYMESFOOD INDUSTRYL-GLUTAMINASEShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1https://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2L-glutaminases are enzymes that catalyze the hydrolysis of L-glutamine, producing L-glutamate and ammonium, and they have promising applications in pharmaceutical and food industries. Several investigations have focused on thermo-tolerant L-glutaminases; however, studies on cold-adapted L-glutaminases have not been reported. These enzymes could be useful in the food industry because they display high catalytic activity at low and room temperatures, a valuable feature in processes aimed to save energy. Besides, they can be easily inactivated by warming and are suitable to prevent decomposition of thermo-labile compounds. The objectives of this work were to characterize the L-glutaminase from the Antarctic bacterium Bizionia argentinensis and analyze its capability as flavor enhancer of protein hydrolysates. The enzyme was heterologously expressed and purified from Escherichia coli, obtaining optimum and homogeneous yields. Kinetic parameters Km and Vmax were located at the lower and upper range of values reported for L-glutaminases, suggesting high catalytic efficiency. Optimum temperature was 25 °C, and the enzyme conserved around 90% of maximum activity at 0 °C and in presence of 15% (v/v) ethanol and methanol. In saline conditions, the enzyme conserved around 80% of maximum activity in 3 M NaCl. Analysis of structural model suggested cold-adaptation features such as low Arg/(Arg+Lys) ratio and fewer intramolecular interactions than mesophilic and thermo-tolerant L-glutaminases. This work provides a novel cold-adapted L-glutaminase with promising features in the food industry.Fil: Ferreira, Flavia Vanina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Entre Ríos. Universidad Nacional de Entre Ríos. Centro de Investigaciones y Transferencia de Entre Ríos; ArgentinaFil: Herrmann Andrade, Andreina M.. Universidad Nacional de Entre Rios. Facultad de Cs. de la Alimentación. Departamento de Cs. de Los Alimentos; ArgentinaFil: Binolfi, Andrés. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Calabrese, Carla D.. Universidad Nacional de Entre Rios. Facultad de Cs. de la Alimentación. Departamento de Cs. de Los Alimentos; ArgentinaFil: Mac Cormack, Walter Patricio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; ArgentinaFil: Musumeci, Matias Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Entre Ríos. Universidad Nacional de Entre Ríos. Centro de Investigaciones y Transferencia de Entre Ríos; ArgentinaHumana Press2021-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/184534Ferreira, Flavia Vanina; Herrmann Andrade, Andreina M.; Binolfi, Andrés; Calabrese, Carla D.; Mac Cormack, Walter Patricio; et al.; Characteristics of a Cold-Adapted L-glutaminase with Potential Applications in the Food Industry; Humana Press; Applied Biochemistry And Biotechnology; 193; 10; 10-2021; 3121-31380273-2289CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1007/s12010-021-03596-8info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:41:29Zoai:ri.conicet.gov.ar:11336/184534instacron: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 09:41:29.43CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Characteristics of a Cold-Adapted L-glutaminase with Potential Applications in the Food Industry
title Characteristics of a Cold-Adapted L-glutaminase with Potential Applications in the Food Industry
spellingShingle Characteristics of a Cold-Adapted L-glutaminase with Potential Applications in the Food Industry
Ferreira, Flavia Vanina
COLD-ADAPTED ENZYMES
FOOD INDUSTRY
L-GLUTAMINASES
title_short Characteristics of a Cold-Adapted L-glutaminase with Potential Applications in the Food Industry
title_full Characteristics of a Cold-Adapted L-glutaminase with Potential Applications in the Food Industry
title_fullStr Characteristics of a Cold-Adapted L-glutaminase with Potential Applications in the Food Industry
title_full_unstemmed Characteristics of a Cold-Adapted L-glutaminase with Potential Applications in the Food Industry
title_sort Characteristics of a Cold-Adapted L-glutaminase with Potential Applications in the Food Industry
dc.creator.none.fl_str_mv Ferreira, Flavia Vanina
Herrmann Andrade, Andreina M.
Binolfi, Andrés
Calabrese, Carla D.
Mac Cormack, Walter Patricio
Musumeci, Matias Alejandro
author Ferreira, Flavia Vanina
author_facet Ferreira, Flavia Vanina
Herrmann Andrade, Andreina M.
Binolfi, Andrés
Calabrese, Carla D.
Mac Cormack, Walter Patricio
Musumeci, Matias Alejandro
author_role author
author2 Herrmann Andrade, Andreina M.
Binolfi, Andrés
Calabrese, Carla D.
Mac Cormack, Walter Patricio
Musumeci, Matias Alejandro
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv COLD-ADAPTED ENZYMES
FOOD INDUSTRY
L-GLUTAMINASES
topic COLD-ADAPTED ENZYMES
FOOD INDUSTRY
L-GLUTAMINASES
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv L-glutaminases are enzymes that catalyze the hydrolysis of L-glutamine, producing L-glutamate and ammonium, and they have promising applications in pharmaceutical and food industries. Several investigations have focused on thermo-tolerant L-glutaminases; however, studies on cold-adapted L-glutaminases have not been reported. These enzymes could be useful in the food industry because they display high catalytic activity at low and room temperatures, a valuable feature in processes aimed to save energy. Besides, they can be easily inactivated by warming and are suitable to prevent decomposition of thermo-labile compounds. The objectives of this work were to characterize the L-glutaminase from the Antarctic bacterium Bizionia argentinensis and analyze its capability as flavor enhancer of protein hydrolysates. The enzyme was heterologously expressed and purified from Escherichia coli, obtaining optimum and homogeneous yields. Kinetic parameters Km and Vmax were located at the lower and upper range of values reported for L-glutaminases, suggesting high catalytic efficiency. Optimum temperature was 25 °C, and the enzyme conserved around 90% of maximum activity at 0 °C and in presence of 15% (v/v) ethanol and methanol. In saline conditions, the enzyme conserved around 80% of maximum activity in 3 M NaCl. Analysis of structural model suggested cold-adaptation features such as low Arg/(Arg+Lys) ratio and fewer intramolecular interactions than mesophilic and thermo-tolerant L-glutaminases. This work provides a novel cold-adapted L-glutaminase with promising features in the food industry.
Fil: Ferreira, Flavia Vanina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Entre Ríos. Universidad Nacional de Entre Ríos. Centro de Investigaciones y Transferencia de Entre Ríos; Argentina
Fil: Herrmann Andrade, Andreina M.. Universidad Nacional de Entre Rios. Facultad de Cs. de la Alimentación. Departamento de Cs. de Los Alimentos; Argentina
Fil: Binolfi, Andrés. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Calabrese, Carla D.. Universidad Nacional de Entre Rios. Facultad de Cs. de la Alimentación. Departamento de Cs. de Los Alimentos; Argentina
Fil: Mac Cormack, Walter Patricio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina
Fil: Musumeci, Matias Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Entre Ríos. Universidad Nacional de Entre Ríos. Centro de Investigaciones y Transferencia de Entre Ríos; Argentina
description L-glutaminases are enzymes that catalyze the hydrolysis of L-glutamine, producing L-glutamate and ammonium, and they have promising applications in pharmaceutical and food industries. Several investigations have focused on thermo-tolerant L-glutaminases; however, studies on cold-adapted L-glutaminases have not been reported. These enzymes could be useful in the food industry because they display high catalytic activity at low and room temperatures, a valuable feature in processes aimed to save energy. Besides, they can be easily inactivated by warming and are suitable to prevent decomposition of thermo-labile compounds. The objectives of this work were to characterize the L-glutaminase from the Antarctic bacterium Bizionia argentinensis and analyze its capability as flavor enhancer of protein hydrolysates. The enzyme was heterologously expressed and purified from Escherichia coli, obtaining optimum and homogeneous yields. Kinetic parameters Km and Vmax were located at the lower and upper range of values reported for L-glutaminases, suggesting high catalytic efficiency. Optimum temperature was 25 °C, and the enzyme conserved around 90% of maximum activity at 0 °C and in presence of 15% (v/v) ethanol and methanol. In saline conditions, the enzyme conserved around 80% of maximum activity in 3 M NaCl. Analysis of structural model suggested cold-adaptation features such as low Arg/(Arg+Lys) ratio and fewer intramolecular interactions than mesophilic and thermo-tolerant L-glutaminases. This work provides a novel cold-adapted L-glutaminase with promising features in the food industry.
publishDate 2021
dc.date.none.fl_str_mv 2021-10
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/11336/184534
Ferreira, Flavia Vanina; Herrmann Andrade, Andreina M.; Binolfi, Andrés; Calabrese, Carla D.; Mac Cormack, Walter Patricio; et al.; Characteristics of a Cold-Adapted L-glutaminase with Potential Applications in the Food Industry; Humana Press; Applied Biochemistry And Biotechnology; 193; 10; 10-2021; 3121-3138
0273-2289
CONICET Digital
CONICET
url http://hdl.handle.net/11336/184534
identifier_str_mv Ferreira, Flavia Vanina; Herrmann Andrade, Andreina M.; Binolfi, Andrés; Calabrese, Carla D.; Mac Cormack, Walter Patricio; et al.; Characteristics of a Cold-Adapted L-glutaminase with Potential Applications in the Food Industry; Humana Press; Applied Biochemistry And Biotechnology; 193; 10; 10-2021; 3121-3138
0273-2289
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1007/s12010-021-03596-8
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
application/pdf
dc.publisher.none.fl_str_mv Humana Press
publisher.none.fl_str_mv Humana Press
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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score 13.070432

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