Structural aspects of the Mucor bacilliformis proteinase, a new member of the aspartyl-proteinase family

Autores
Machalinski, Claudia; Pirpignani, Maria L.; Marino, Cristina Ester; Mantegazza, Adriana Rita; Biscoglio, Mirtha Josefa
Año de publicación
2006
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Bovine chymosin is considered the best milk-clotting enzyme for cheese manufacture; however, the thermophilic Mucor pusillus proteinase is also used nowadays. We herein report structural aspects of the aspartyl proteinase from the local mesophilic Mucor bacilliformis strain. Sequence data indicate a high similarity degree to those of other family members. The protein is monomeric, not glycosylated, has two disulfide bridges, and mainly includes beta structure. A molecular model was built by using the Rhizopus chinensis proteinase structure as the template. Sequence analysis and comparison of our model with bovine chymosin and M. pusillus proteinase structures, indicate that the M. bacilliformis proteinase is at a similar evolutionary distance on a sequence level; as regards tertiary structure, the M. bacilliformis proteinase superimposes on the bovine chymosin structure in a fashion similar to that of the M. pusillus proteinase. Overall results suggest that this novel proteinase can be utilized as a good milk-clotting enzyme in the dairy industry.
Fil: Machalinski, Claudia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Pirpignani, Maria L.. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Marino, Cristina Ester. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Mantegazza, Adriana Rita. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Biscoglio, Mirtha Josefa. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Materia
Aspartyl-Proteinase Family
Cheese Industry
Mesophilic Proteinases
Milk-Clotting Enzymes
Mucor Bacilliformis Proteinase
Primary Structure
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:11336/39495
Acceder
id CONICETDig_2c4acf24a5fa9962a5b235414d97ef79
oai_identifier_str oai:ri.conicet.gov.ar:11336/39495
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Structural aspects of the Mucor bacilliformis proteinase, a new member of the aspartyl-proteinase familyMachalinski, ClaudiaPirpignani, Maria L.Marino, Cristina EsterMantegazza, Adriana RitaBiscoglio, Mirtha JosefaAspartyl-Proteinase FamilyCheese IndustryMesophilic ProteinasesMilk-Clotting EnzymesMucor Bacilliformis ProteinasePrimary Structurehttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Bovine chymosin is considered the best milk-clotting enzyme for cheese manufacture; however, the thermophilic Mucor pusillus proteinase is also used nowadays. We herein report structural aspects of the aspartyl proteinase from the local mesophilic Mucor bacilliformis strain. Sequence data indicate a high similarity degree to those of other family members. The protein is monomeric, not glycosylated, has two disulfide bridges, and mainly includes beta structure. A molecular model was built by using the Rhizopus chinensis proteinase structure as the template. Sequence analysis and comparison of our model with bovine chymosin and M. pusillus proteinase structures, indicate that the M. bacilliformis proteinase is at a similar evolutionary distance on a sequence level; as regards tertiary structure, the M. bacilliformis proteinase superimposes on the bovine chymosin structure in a fashion similar to that of the M. pusillus proteinase. Overall results suggest that this novel proteinase can be utilized as a good milk-clotting enzyme in the dairy industry.Fil: Machalinski, Claudia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaFil: Pirpignani, Maria L.. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaFil: Marino, Cristina Ester. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Mantegazza, Adriana Rita. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Biscoglio, Mirtha Josefa. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaElsevier Science2006-06info: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/11336/39495Machalinski, Claudia; Pirpignani, Maria L.; Marino, Cristina Ester; Mantegazza, Adriana Rita; Biscoglio, Mirtha Josefa; Structural aspects of the Mucor bacilliformis proteinase, a new member of the aspartyl-proteinase family; Elsevier Science; Journal of Biotechnology; 123; 4; 6-2006; 443-4520168-16561873-4863CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0168-1656(06)00036-8info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jbiotec.2005.12.035info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:05:12Zoai:ri.conicet.gov.ar:11336/39495instacron: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:34982025-09-03 10:05:13.245CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Structural aspects of the Mucor bacilliformis proteinase, a new member of the aspartyl-proteinase family
title Structural aspects of the Mucor bacilliformis proteinase, a new member of the aspartyl-proteinase family
spellingShingle Structural aspects of the Mucor bacilliformis proteinase, a new member of the aspartyl-proteinase family
Machalinski, Claudia
Aspartyl-Proteinase Family
Cheese Industry
Mesophilic Proteinases
Milk-Clotting Enzymes
Mucor Bacilliformis Proteinase
Primary Structure
title_short Structural aspects of the Mucor bacilliformis proteinase, a new member of the aspartyl-proteinase family
title_full Structural aspects of the Mucor bacilliformis proteinase, a new member of the aspartyl-proteinase family
title_fullStr Structural aspects of the Mucor bacilliformis proteinase, a new member of the aspartyl-proteinase family
title_full_unstemmed Structural aspects of the Mucor bacilliformis proteinase, a new member of the aspartyl-proteinase family
title_sort Structural aspects of the Mucor bacilliformis proteinase, a new member of the aspartyl-proteinase family
dc.creator.none.fl_str_mv Machalinski, Claudia
Pirpignani, Maria L.
Marino, Cristina Ester
Mantegazza, Adriana Rita
Biscoglio, Mirtha Josefa
author Machalinski, Claudia
author_facet Machalinski, Claudia
Pirpignani, Maria L.
Marino, Cristina Ester
Mantegazza, Adriana Rita
Biscoglio, Mirtha Josefa
author_role author
author2 Pirpignani, Maria L.
Marino, Cristina Ester
Mantegazza, Adriana Rita
Biscoglio, Mirtha Josefa
author2_role author
author
author
author
dc.subject.none.fl_str_mv Aspartyl-Proteinase Family
Cheese Industry
Mesophilic Proteinases
Milk-Clotting Enzymes
Mucor Bacilliformis Proteinase
Primary Structure
topic Aspartyl-Proteinase Family
Cheese Industry
Mesophilic Proteinases
Milk-Clotting Enzymes
Mucor Bacilliformis Proteinase
Primary Structure
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Bovine chymosin is considered the best milk-clotting enzyme for cheese manufacture; however, the thermophilic Mucor pusillus proteinase is also used nowadays. We herein report structural aspects of the aspartyl proteinase from the local mesophilic Mucor bacilliformis strain. Sequence data indicate a high similarity degree to those of other family members. The protein is monomeric, not glycosylated, has two disulfide bridges, and mainly includes beta structure. A molecular model was built by using the Rhizopus chinensis proteinase structure as the template. Sequence analysis and comparison of our model with bovine chymosin and M. pusillus proteinase structures, indicate that the M. bacilliformis proteinase is at a similar evolutionary distance on a sequence level; as regards tertiary structure, the M. bacilliformis proteinase superimposes on the bovine chymosin structure in a fashion similar to that of the M. pusillus proteinase. Overall results suggest that this novel proteinase can be utilized as a good milk-clotting enzyme in the dairy industry.
Fil: Machalinski, Claudia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Pirpignani, Maria L.. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Marino, Cristina Ester. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Mantegazza, Adriana Rita. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Biscoglio, Mirtha Josefa. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
description Bovine chymosin is considered the best milk-clotting enzyme for cheese manufacture; however, the thermophilic Mucor pusillus proteinase is also used nowadays. We herein report structural aspects of the aspartyl proteinase from the local mesophilic Mucor bacilliformis strain. Sequence data indicate a high similarity degree to those of other family members. The protein is monomeric, not glycosylated, has two disulfide bridges, and mainly includes beta structure. A molecular model was built by using the Rhizopus chinensis proteinase structure as the template. Sequence analysis and comparison of our model with bovine chymosin and M. pusillus proteinase structures, indicate that the M. bacilliformis proteinase is at a similar evolutionary distance on a sequence level; as regards tertiary structure, the M. bacilliformis proteinase superimposes on the bovine chymosin structure in a fashion similar to that of the M. pusillus proteinase. Overall results suggest that this novel proteinase can be utilized as a good milk-clotting enzyme in the dairy industry.
publishDate 2006
dc.date.none.fl_str_mv 2006-06
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/11336/39495
Machalinski, Claudia; Pirpignani, Maria L.; Marino, Cristina Ester; Mantegazza, Adriana Rita; Biscoglio, Mirtha Josefa; Structural aspects of the Mucor bacilliformis proteinase, a new member of the aspartyl-proteinase family; Elsevier Science; Journal of Biotechnology; 123; 4; 6-2006; 443-452
0168-1656
1873-4863
CONICET Digital
CONICET
url http://hdl.handle.net/11336/39495
identifier_str_mv Machalinski, Claudia; Pirpignani, Maria L.; Marino, Cristina Ester; Mantegazza, Adriana Rita; Biscoglio, Mirtha Josefa; Structural aspects of the Mucor bacilliformis proteinase, a new member of the aspartyl-proteinase family; Elsevier Science; Journal of Biotechnology; 123; 4; 6-2006; 443-452
0168-1656
1873-4863
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0168-1656(06)00036-8
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jbiotec.2005.12.035
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 Elsevier Science
publisher.none.fl_str_mv Elsevier Science
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 13.13397

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