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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/2835
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/2835
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling 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 Técnicas2025-10-22T11:14:26Zoai: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:34982025-10-22 11:14:27.061CONICET 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)
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_ 1846781564825894912
score 12.982451

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