Recombinant lactococcus lactis fails to secrete bovine chymosine
- Autores
- Diniz Luerce, Tessália; Santiago Pacheco Azevedo, Marcela; Leblanc, Jean Guy Joseph; Azevedo, Vasco; Miyoshi, Anderson; Santos Pontes, Daniela
- Año de publicación
- 2014
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Bovine chymosin is an important milk-clotting agent used in the manufacturing of cheeses. Currently, the production of recombinant proteins by genetically modified organisms is widespread, leading to greatly reduced costs. Lactococcus (L.) lactis, the model lactic acid bacterium, was considered a good candidate for heterologous chymosin production for the following reasons: (1) it is considered to be a GRAS (generally regarded as safe) microorganism, (2) only one protease is present on its surface, (3) it can secrete proteins of different sizes, and (4) it allows for the direct production of protein in fermented food products. Thus, three genetically modified L. lactis strains were constructed to produce and target the three different forms of bovine chymosin, prochymosin B, chymosin A and chymosin B to the extracellular medium. Although all three proteins were stably produced in L. lactis, none of the forms were detected in the extracellular medium or showed clotting activity in milk. Our hypothesis is that this secretion deficiency and lack of clotting activity can be explained by the recombinant protein being attached to the cell envelope. Thus, the development of other strategies is necessary to achieve both production and targeting of chymosin in L. lactis, which could facilitate the downstream processing and recovery of this industrially important protein.
Fil: Diniz Luerce, Tessália. Universidade Federal de Minas Gerais; Brasil
Fil: Santiago Pacheco Azevedo, Marcela. Universidade Federal de Minas Gerais; Brasil
Fil: Leblanc, Jean Guy Joseph. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Tucumán. Centro de Referencia para Lactobacilos (i); Argentina
Fil: Azevedo, Vasco. Universidade Federal de Minas Gerais; Brasil
Fil: Miyoshi, Anderson. Universidade Federal de Minas Gerais; Brasil
Fil: Santos Pontes, Daniela. Universidade Estadual da Paraiba; Brasil - Materia
-
BOVINE CHYMOSIN
BOVINE PROCHYMOSIN
HETEROLOGOUS EXPRESSION
LACTOCOCCUS LACTIS - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/2835
Ver los metadatos del registro completo
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Recombinant lactococcus lactis fails to secrete bovine chymosineDiniz Luerce, TessáliaSantiago Pacheco Azevedo, MarcelaLeblanc, Jean Guy JosephAzevedo, VascoMiyoshi, AndersonSantos Pontes, DanielaBOVINE CHYMOSINBOVINE PROCHYMOSINHETEROLOGOUS EXPRESSIONLACTOCOCCUS LACTIShttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2Bovine chymosin is an important milk-clotting agent used in the manufacturing of cheeses. Currently, the production of recombinant proteins by genetically modified organisms is widespread, leading to greatly reduced costs. Lactococcus (L.) lactis, the model lactic acid bacterium, was considered a good candidate for heterologous chymosin production for the following reasons: (1) it is considered to be a GRAS (generally regarded as safe) microorganism, (2) only one protease is present on its surface, (3) it can secrete proteins of different sizes, and (4) it allows for the direct production of protein in fermented food products. Thus, three genetically modified L. lactis strains were constructed to produce and target the three different forms of bovine chymosin, prochymosin B, chymosin A and chymosin B to the extracellular medium. Although all three proteins were stably produced in L. lactis, none of the forms were detected in the extracellular medium or showed clotting activity in milk. Our hypothesis is that this secretion deficiency and lack of clotting activity can be explained by the recombinant protein being attached to the cell envelope. Thus, the development of other strategies is necessary to achieve both production and targeting of chymosin in L. lactis, which could facilitate the downstream processing and recovery of this industrially important protein.Fil: Diniz Luerce, Tessália. Universidade Federal de Minas Gerais; BrasilFil: Santiago Pacheco Azevedo, Marcela. Universidade Federal de Minas Gerais; BrasilFil: Leblanc, Jean Guy Joseph. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Tucumán. Centro de Referencia para Lactobacilos (i); ArgentinaFil: Azevedo, Vasco. Universidade Federal de Minas Gerais; BrasilFil: Miyoshi, Anderson. Universidade Federal de Minas Gerais; BrasilFil: Santos Pontes, Daniela. Universidade Estadual da Paraiba; BrasilTaylor & Francis2014-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/2835Diniz Luerce, Tessália; Santiago Pacheco Azevedo, Marcela; Leblanc, Jean Guy Joseph; Azevedo, Vasco; Miyoshi, Anderson; et al.; Recombinant lactococcus lactis fails to secrete bovine chymosine; Taylor & Francis; Bioengineered; 5; 6; 11-2014; 363-3702165-59792165-5987enginfo:eu-repo/semantics/altIdentifier/doi/10.4161/bioe.36327info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:45:38Zoai:ri.conicet.gov.ar:11336/2835instacron: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 09:45:39.095CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Recombinant lactococcus lactis fails to secrete bovine chymosine |
title |
Recombinant lactococcus lactis fails to secrete bovine chymosine |
spellingShingle |
Recombinant lactococcus lactis fails to secrete bovine chymosine Diniz Luerce, Tessália BOVINE CHYMOSIN BOVINE PROCHYMOSIN HETEROLOGOUS EXPRESSION LACTOCOCCUS LACTIS |
title_short |
Recombinant lactococcus lactis fails to secrete bovine chymosine |
title_full |
Recombinant lactococcus lactis fails to secrete bovine chymosine |
title_fullStr |
Recombinant lactococcus lactis fails to secrete bovine chymosine |
title_full_unstemmed |
Recombinant lactococcus lactis fails to secrete bovine chymosine |
title_sort |
Recombinant lactococcus lactis fails to secrete bovine chymosine |
dc.creator.none.fl_str_mv |
Diniz Luerce, Tessália Santiago Pacheco Azevedo, Marcela Leblanc, Jean Guy Joseph Azevedo, Vasco Miyoshi, Anderson Santos Pontes, Daniela |
author |
Diniz Luerce, Tessália |
author_facet |
Diniz Luerce, Tessália Santiago Pacheco Azevedo, Marcela Leblanc, Jean Guy Joseph Azevedo, Vasco Miyoshi, Anderson Santos Pontes, Daniela |
author_role |
author |
author2 |
Santiago Pacheco Azevedo, Marcela Leblanc, Jean Guy Joseph Azevedo, Vasco Miyoshi, Anderson Santos Pontes, Daniela |
author2_role |
author author author author author |
dc.subject.none.fl_str_mv |
BOVINE CHYMOSIN BOVINE PROCHYMOSIN HETEROLOGOUS EXPRESSION LACTOCOCCUS LACTIS |
topic |
BOVINE CHYMOSIN BOVINE PROCHYMOSIN HETEROLOGOUS EXPRESSION LACTOCOCCUS LACTIS |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/2.11 https://purl.org/becyt/ford/2 |
dc.description.none.fl_txt_mv |
Bovine chymosin is an important milk-clotting agent used in the manufacturing of cheeses. Currently, the production of recombinant proteins by genetically modified organisms is widespread, leading to greatly reduced costs. Lactococcus (L.) lactis, the model lactic acid bacterium, was considered a good candidate for heterologous chymosin production for the following reasons: (1) it is considered to be a GRAS (generally regarded as safe) microorganism, (2) only one protease is present on its surface, (3) it can secrete proteins of different sizes, and (4) it allows for the direct production of protein in fermented food products. Thus, three genetically modified L. lactis strains were constructed to produce and target the three different forms of bovine chymosin, prochymosin B, chymosin A and chymosin B to the extracellular medium. Although all three proteins were stably produced in L. lactis, none of the forms were detected in the extracellular medium or showed clotting activity in milk. Our hypothesis is that this secretion deficiency and lack of clotting activity can be explained by the recombinant protein being attached to the cell envelope. Thus, the development of other strategies is necessary to achieve both production and targeting of chymosin in L. lactis, which could facilitate the downstream processing and recovery of this industrially important protein. Fil: Diniz Luerce, Tessália. Universidade Federal de Minas Gerais; Brasil Fil: Santiago Pacheco Azevedo, Marcela. Universidade Federal de Minas Gerais; Brasil Fil: Leblanc, Jean Guy Joseph. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Tucumán. Centro de Referencia para Lactobacilos (i); Argentina Fil: Azevedo, Vasco. Universidade Federal de Minas Gerais; Brasil Fil: Miyoshi, Anderson. Universidade Federal de Minas Gerais; Brasil Fil: Santos Pontes, Daniela. Universidade Estadual da Paraiba; Brasil |
description |
Bovine chymosin is an important milk-clotting agent used in the manufacturing of cheeses. Currently, the production of recombinant proteins by genetically modified organisms is widespread, leading to greatly reduced costs. Lactococcus (L.) lactis, the model lactic acid bacterium, was considered a good candidate for heterologous chymosin production for the following reasons: (1) it is considered to be a GRAS (generally regarded as safe) microorganism, (2) only one protease is present on its surface, (3) it can secrete proteins of different sizes, and (4) it allows for the direct production of protein in fermented food products. Thus, three genetically modified L. lactis strains were constructed to produce and target the three different forms of bovine chymosin, prochymosin B, chymosin A and chymosin B to the extracellular medium. Although all three proteins were stably produced in L. lactis, none of the forms were detected in the extracellular medium or showed clotting activity in milk. Our hypothesis is that this secretion deficiency and lack of clotting activity can be explained by the recombinant protein being attached to the cell envelope. Thus, the development of other strategies is necessary to achieve both production and targeting of chymosin in L. lactis, which could facilitate the downstream processing and recovery of this industrially important protein. |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014-11 |
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/11336/2835 Diniz Luerce, Tessália; Santiago Pacheco Azevedo, Marcela; Leblanc, Jean Guy Joseph; Azevedo, Vasco; Miyoshi, Anderson; et al.; Recombinant lactococcus lactis fails to secrete bovine chymosine; Taylor & Francis; Bioengineered; 5; 6; 11-2014; 363-370 2165-5979 2165-5987 |
url |
http://hdl.handle.net/11336/2835 |
identifier_str_mv |
Diniz Luerce, Tessália; Santiago Pacheco Azevedo, Marcela; Leblanc, Jean Guy Joseph; Azevedo, Vasco; Miyoshi, Anderson; et al.; Recombinant lactococcus lactis fails to secrete bovine chymosine; Taylor & Francis; Bioengineered; 5; 6; 11-2014; 363-370 2165-5979 2165-5987 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.4161/bioe.36327 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Taylor & Francis |
publisher.none.fl_str_mv |
Taylor & Francis |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
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CONICET Digital (CONICET) |
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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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13.070432 |