New trends for a classical enzyme: Papain, a biotechnological success story in the food industry
Background In recent years, proteases have arisen as standard biocatalysts in many industrial processes in different fields, such as pharmaceutical, medicine, detergent manufacturing and food science. Among them, papain is undoubtedly one of the most frequently studied and widely used proteases in t...
- Autores:
-
Fernandez Lucas, Jesus
Castañeda Valbuena, Daniel
Hormigo, Daniel
- Tipo de recurso:
- Article of journal
- Fecha de publicación:
- 2017
- Institución:
- Corporación Universidad de la Costa
- Repositorio:
- REDICUC - Repositorio CUC
- Idioma:
- eng
- OAI Identifier:
- oai:repositorio.cuc.edu.co:11323/1609
- Acceso en línea:
- https://hdl.handle.net/11323/1609
https://repositorio.cuc.edu.co/
- Palabra clave:
- Biocatalysis
Cysteine proteases
Enzyme biotechnology
Immobilization
Industrial processes
Papain
- Rights
- openAccess
- License
- Atribución – No comercial – Compartir igual
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dc.title.eng.fl_str_mv |
New trends for a classical enzyme: Papain, a biotechnological success story in the food industry |
title |
New trends for a classical enzyme: Papain, a biotechnological success story in the food industry |
spellingShingle |
New trends for a classical enzyme: Papain, a biotechnological success story in the food industry Biocatalysis Cysteine proteases Enzyme biotechnology Immobilization Industrial processes Papain |
title_short |
New trends for a classical enzyme: Papain, a biotechnological success story in the food industry |
title_full |
New trends for a classical enzyme: Papain, a biotechnological success story in the food industry |
title_fullStr |
New trends for a classical enzyme: Papain, a biotechnological success story in the food industry |
title_full_unstemmed |
New trends for a classical enzyme: Papain, a biotechnological success story in the food industry |
title_sort |
New trends for a classical enzyme: Papain, a biotechnological success story in the food industry |
dc.creator.fl_str_mv |
Fernandez Lucas, Jesus Castañeda Valbuena, Daniel Hormigo, Daniel |
dc.contributor.author.spa.fl_str_mv |
Fernandez Lucas, Jesus Castañeda Valbuena, Daniel Hormigo, Daniel |
dc.subject.eng.fl_str_mv |
Biocatalysis Cysteine proteases Enzyme biotechnology Immobilization Industrial processes Papain |
topic |
Biocatalysis Cysteine proteases Enzyme biotechnology Immobilization Industrial processes Papain |
description |
Background In recent years, proteases have arisen as standard biocatalysts in many industrial processes in different fields, such as pharmaceutical, medicine, detergent manufacturing and food science. Among them, papain is undoubtedly one of the most frequently studied and widely used proteases in the food industry around the world. However, the latest advances in recombinant papain expression systems, genetically engineered biocatalysts, new purification and isolation strategies, and enzymatic immobilization will enhance the development of new applications of papain, as well as improve and optimize classical applications. Scope and approach This review addresses not only the latest advances in classic applications, such as meat tenderization and protein hydrolysates, but also the most innovative applications in different industries such as food, animal feed, bioactive peptides production, water treatment, baking and brewing, among many others. In addition, papain is a perfect example of a successful industrial enzyme that covers all the steps of the biocatalytic cycle that are necessary for the industrial implementation of any biocatalyst. This cycle includes the production and extraction of the enzyme concerned (from natural or recombinant sources), functional and structural characterization, genetic improvement, immobilization and, finally, industrial application. This review describes the complete biocatalytic cycle of papain. Key findings and conclusions Papain is clearly a case of industrial and commercial success over the last 40 years. The key to this success has been continual biotechnological and process engineering innovation, which has opened up a new range of possibilities for this exciting biocatalyst. However, further efforts are needed in protein engineering and characterization of new mutants to reach the full potential of this enzyme. |
publishDate |
2017 |
dc.date.issued.none.fl_str_mv |
2017-08-23 |
dc.date.accessioned.none.fl_str_mv |
2018-11-21T13:13:05Z |
dc.date.available.none.fl_str_mv |
2018-11-21T13:13:05Z |
dc.type.spa.fl_str_mv |
Artículo de revista |
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http://purl.org/coar/resource_type/c_2df8fbb1 |
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http://purl.org/coar/resource_type/c_6501 |
dc.type.content.spa.fl_str_mv |
Text |
dc.type.driver.spa.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.redcol.spa.fl_str_mv |
http://purl.org/redcol/resource_type/ART |
dc.type.version.spa.fl_str_mv |
info:eu-repo/semantics/acceptedVersion |
format |
http://purl.org/coar/resource_type/c_6501 |
status_str |
acceptedVersion |
dc.identifier.issn.spa.fl_str_mv |
09242244 |
dc.identifier.uri.spa.fl_str_mv |
https://hdl.handle.net/11323/1609 |
dc.identifier.doi.spa.fl_str_mv |
DOI: 10.1016/j.tifs.2017.08.017 |
dc.identifier.instname.spa.fl_str_mv |
Corporación Universidad de la Costa |
dc.identifier.reponame.spa.fl_str_mv |
REDICUC - Repositorio CUC |
dc.identifier.repourl.spa.fl_str_mv |
https://repositorio.cuc.edu.co/ |
identifier_str_mv |
09242244 DOI: 10.1016/j.tifs.2017.08.017 Corporación Universidad de la Costa REDICUC - Repositorio CUC |
url |
https://hdl.handle.net/11323/1609 https://repositorio.cuc.edu.co/ |
dc.language.iso.none.fl_str_mv |
eng |
language |
eng |
dc.rights.spa.fl_str_mv |
Atribución – No comercial – Compartir igual |
dc.rights.accessrights.spa.fl_str_mv |
info:eu-repo/semantics/openAccess |
dc.rights.coar.spa.fl_str_mv |
http://purl.org/coar/access_right/c_abf2 |
rights_invalid_str_mv |
Atribución – No comercial – Compartir igual http://purl.org/coar/access_right/c_abf2 |
eu_rights_str_mv |
openAccess |
institution |
Corporación Universidad de la Costa |
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Fernandez Lucas, JesusCastañeda Valbuena, DanielHormigo, Daniel2018-11-21T13:13:05Z2018-11-21T13:13:05Z2017-08-2309242244https://hdl.handle.net/11323/1609DOI: 10.1016/j.tifs.2017.08.017Corporación Universidad de la CostaREDICUC - Repositorio CUChttps://repositorio.cuc.edu.co/Background In recent years, proteases have arisen as standard biocatalysts in many industrial processes in different fields, such as pharmaceutical, medicine, detergent manufacturing and food science. Among them, papain is undoubtedly one of the most frequently studied and widely used proteases in the food industry around the world. However, the latest advances in recombinant papain expression systems, genetically engineered biocatalysts, new purification and isolation strategies, and enzymatic immobilization will enhance the development of new applications of papain, as well as improve and optimize classical applications. Scope and approach This review addresses not only the latest advances in classic applications, such as meat tenderization and protein hydrolysates, but also the most innovative applications in different industries such as food, animal feed, bioactive peptides production, water treatment, baking and brewing, among many others. In addition, papain is a perfect example of a successful industrial enzyme that covers all the steps of the biocatalytic cycle that are necessary for the industrial implementation of any biocatalyst. This cycle includes the production and extraction of the enzyme concerned (from natural or recombinant sources), functional and structural characterization, genetic improvement, immobilization and, finally, industrial application. This review describes the complete biocatalytic cycle of papain. Key findings and conclusions Papain is clearly a case of industrial and commercial success over the last 40 years. The key to this success has been continual biotechnological and process engineering innovation, which has opened up a new range of possibilities for this exciting biocatalyst. However, further efforts are needed in protein engineering and characterization of new mutants to reach the full potential of this enzyme.Fernandez Lucas, Jesus-3f36c351-7522-42ea-8605-cd7e804a6387-0Castañeda Valbuena, Daniel-548e8ef8-d787-43cc-812d-4e4c88e90d57-0Hormigo, Daniel-915adee9-292d-4836-8d92-b79ac158d173-0engAtribución – No comercial – Compartir igualinfo:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2BiocatalysisCysteine proteasesEnzyme biotechnologyImmobilizationIndustrial processesPapainNew trends for a classical enzyme: Papain, a biotechnological success story in the food industryArtículo de revistahttp://purl.org/coar/resource_type/c_6501http://purl.org/coar/resource_type/c_2df8fbb1Textinfo:eu-repo/semantics/articlehttp://purl.org/redcol/resource_type/ARTinfo:eu-repo/semantics/acceptedVersionPublicationORIGINALNew trends for a classical enzyme.pdfNew trends for a classical enzyme.pdfapplication/pdf196679https://repositorio.cuc.edu.co/bitstreams/27ff55ff-f627-4c6d-860f-0122877aa934/downloadcd9ce2548520b2263b6478a065a813d9MD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://repositorio.cuc.edu.co/bitstreams/ba096b3a-5802-42c3-90cc-fb64a64db794/download8a4605be74aa9ea9d79846c1fba20a33MD52THUMBNAILNew trends for a classical enzyme.pdf.jpgNew trends for a classical enzyme.pdf.jpgimage/jpeg52799https://repositorio.cuc.edu.co/bitstreams/2da412d0-6e12-4c93-8a69-6011fee19393/download996831bef134f446414511de869bf577MD54TEXTNew trends for a classical enzyme.pdf.txtNew trends for a classical enzyme.pdf.txttext/plain2212https://repositorio.cuc.edu.co/bitstreams/da1786a8-bed3-4c25-885e-184309af1998/downloadbc061b8890bbfa1112c22f8bef3963f6MD5511323/1609oai:repositorio.cuc.edu.co:11323/16092024-09-17 14:08:59.168open.accesshttps://repositorio.cuc.edu.coRepositorio de la Universidad de la Costa CUCrepdigital@cuc.edu.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 |