Novel Long-Term Phytase from Serratia odorifera: Cloning, Expression, and Characterization.

The appA-So gene, encoding a phytase from Serratia odorifera, was cloned and heterologously expressed in Komagataella phaffii. The open reading frame of appA-So comprised 1281 bp that encoded a 426-amino acid protein, including a 27-amino acid signal peptide. The encoded phytase, AppA-So, showed 52%...

Descripción completa

Detalles Bibliográficos
Autores: Salaet, Ignasi, Marquès, Ramon, Yance Chávez, Tula del Carmen, Macías Vidal, Judit, Giménez Zaragoza, David, Aligué i Alemany, Rosa Maria
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2021
País:España
Institución:Universidad de Barcelona
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/184112
Acceso en línea:https://hdl.handle.net/2445/184112
Access Level:acceso abierto
Palabra clave:Clonatge
Biotecnologia alimentària
Cloning
Food biotechnology
id ES_2d1d01cea29945238d06232de9fa635f
oai_identifier_str oai:diposit.ub.edu:2445/184112
network_acronym_str ES
network_name_str España
repository_id_str
spelling Novel Long-Term Phytase from Serratia odorifera: Cloning, Expression, and Characterization.Salaet, IgnasiMarquès, RamonYance Chávez, Tula del CarmenMacías Vidal, JuditGiménez Zaragoza, DavidAligué i Alemany, Rosa MariaClonatgeBiotecnologia alimentàriaCloningFood biotechnologyThe appA-So gene, encoding a phytase from Serratia odorifera, was cloned and heterologously expressed in Komagataella phaffii. The open reading frame of appA-So comprised 1281 bp that encoded a 426-amino acid protein, including a 27-amino acid signal peptide. The encoded phytase, AppA-So, showed 52% homology with other histidine acid phosphatases. The purified recombinant phytase showed optimal activity at 55 °C and pH 4.5, exhibiting enzymatic activity between pH 3.7 and 5.8, with a specific activity of 1123 U/mg at pH 4.5 and 37 °C. The AppA-So protein retained more than 85% of its initial activity after incubation in different pH conditions (pH 2.5-6.5) at 37 °C for 3 h. AppA-So activity was maintained over time and displayed a low Michaelis-Menten constant (Km) of 0.093 g/L. To the best of our knowledge, this is the first report of the cloning and characterization of the phytase from S. odorifera. Comparison of AppA-So with other well-known phytases suggests that the S. odorifera phytase has the lowest Km and highest stable activity over time, making it very suitable for use in the animal feed industry.Sociedade Brasileira de Ciência e Tecnologia de Alimentos2021info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://hdl.handle.net/2445/184112Articles publicats en revistes (Biomedicina)reponame:Dipòsit Digital de la UBinstname:Universidad de BarcelonaInglésReproducció del document publicat a: https://doi.org/10.1021/acsfoodscitech.0c00074Food Science and Technology, 2021, vol. 1, p. 689-697(c) Salaet, Ignasi et al., 2021info:eu-repo/semantics/openAccessoai:diposit.ub.edu:2445/1841122026-05-27T06:46:51Z
dc.title.none.fl_str_mv Novel Long-Term Phytase from Serratia odorifera: Cloning, Expression, and Characterization.
title Novel Long-Term Phytase from Serratia odorifera: Cloning, Expression, and Characterization.
spellingShingle Novel Long-Term Phytase from Serratia odorifera: Cloning, Expression, and Characterization.
Salaet, Ignasi
Clonatge
Biotecnologia alimentària
Cloning
Food biotechnology
title_short Novel Long-Term Phytase from Serratia odorifera: Cloning, Expression, and Characterization.
title_full Novel Long-Term Phytase from Serratia odorifera: Cloning, Expression, and Characterization.
title_fullStr Novel Long-Term Phytase from Serratia odorifera: Cloning, Expression, and Characterization.
title_full_unstemmed Novel Long-Term Phytase from Serratia odorifera: Cloning, Expression, and Characterization.
title_sort Novel Long-Term Phytase from Serratia odorifera: Cloning, Expression, and Characterization.
dc.creator.none.fl_str_mv Salaet, Ignasi
Marquès, Ramon
Yance Chávez, Tula del Carmen
Macías Vidal, Judit
Giménez Zaragoza, David
Aligué i Alemany, Rosa Maria
author Salaet, Ignasi
author_facet Salaet, Ignasi
Marquès, Ramon
Yance Chávez, Tula del Carmen
Macías Vidal, Judit
Giménez Zaragoza, David
Aligué i Alemany, Rosa Maria
author_role author
author2 Marquès, Ramon
Yance Chávez, Tula del Carmen
Macías Vidal, Judit
Giménez Zaragoza, David
Aligué i Alemany, Rosa Maria
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Clonatge
Biotecnologia alimentària
Cloning
Food biotechnology
topic Clonatge
Biotecnologia alimentària
Cloning
Food biotechnology
description The appA-So gene, encoding a phytase from Serratia odorifera, was cloned and heterologously expressed in Komagataella phaffii. The open reading frame of appA-So comprised 1281 bp that encoded a 426-amino acid protein, including a 27-amino acid signal peptide. The encoded phytase, AppA-So, showed 52% homology with other histidine acid phosphatases. The purified recombinant phytase showed optimal activity at 55 °C and pH 4.5, exhibiting enzymatic activity between pH 3.7 and 5.8, with a specific activity of 1123 U/mg at pH 4.5 and 37 °C. The AppA-So protein retained more than 85% of its initial activity after incubation in different pH conditions (pH 2.5-6.5) at 37 °C for 3 h. AppA-So activity was maintained over time and displayed a low Michaelis-Menten constant (Km) of 0.093 g/L. To the best of our knowledge, this is the first report of the cloning and characterization of the phytase from S. odorifera. Comparison of AppA-So with other well-known phytases suggests that the S. odorifera phytase has the lowest Km and highest stable activity over time, making it very suitable for use in the animal feed industry.
publishDate 2021
dc.date.none.fl_str_mv 2021
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/184112
url https://hdl.handle.net/2445/184112
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: https://doi.org/10.1021/acsfoodscitech.0c00074
Food Science and Technology, 2021, vol. 1, p. 689-697
dc.rights.none.fl_str_mv (c) Salaet, Ignasi et al., 2021
info:eu-repo/semantics/openAccess
rights_invalid_str_mv (c) Salaet, Ignasi et al., 2021
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Sociedade Brasileira de Ciência e Tecnologia de Alimentos
publisher.none.fl_str_mv Sociedade Brasileira de Ciência e Tecnologia de Alimentos
dc.source.none.fl_str_mv Articles publicats en revistes (Biomedicina)
reponame:Dipòsit Digital de la UB
instname:Universidad de Barcelona
instname_str Universidad de Barcelona
reponame_str Dipòsit Digital de la UB
collection Dipòsit Digital de la UB
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869405292867878912
score 15.301629

Similares en LA Referencia