Superactivity of alpha-chymotrypsin with biological buffers, TRIS, TES, TAPS, and TAPSO in aqueous solutions

Detalhes bibliográficos
Autor(a) principal: Gupta, Bhupender S.
Data de Publicação: 2014
Outros Autores: Taha, Mohamed, Lee, Ming-Jer
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10773/19270
Resumo: Biological buffers are always considered as non-toxic, biocompatible and green compounds. Therefore, we analyzed the catalytic activity of a commercial enzyme alpha-chymotrypsin (alpha-CT) in aqueous solutions of some common biological buffers (TRIS, TES, TAPS, and TAPSO) at pH 8 and T = 25 degrees C. It is found that the increase of the buffer concentration enhanced the catalytic activity of enzyme alpha-CT, and the tendency follows the order of TRIS > TES > TAPS > TAPSO. Especially in the presence of TRIS, the catalytic activity enhanced 5.5 fold.
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spelling Superactivity of alpha-chymotrypsin with biological buffers, TRIS, TES, TAPS, and TAPSO in aqueous solutionsBOVINE SERUM-ALBUMINIONIC LIQUIDSORGANIC MEDIAWATERSTABILITYENZYMEFLUORESCENCESTABILIZATIONCOMPLEXESPROTEINSBiological buffers are always considered as non-toxic, biocompatible and green compounds. Therefore, we analyzed the catalytic activity of a commercial enzyme alpha-chymotrypsin (alpha-CT) in aqueous solutions of some common biological buffers (TRIS, TES, TAPS, and TAPSO) at pH 8 and T = 25 degrees C. It is found that the increase of the buffer concentration enhanced the catalytic activity of enzyme alpha-CT, and the tendency follows the order of TRIS > TES > TAPS > TAPSO. Especially in the presence of TRIS, the catalytic activity enhanced 5.5 fold.ROYAL SOC CHEMISTRY2017-12-07T19:06:56Z2014-01-01T00:00:00Z2014info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10773/19270eng2046-206910.1039/c4ra09434dGupta, Bhupender S.Taha, MohamedLee, Ming-Jerinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-02-22T11:37:22Zoai:ria.ua.pt:10773/19270Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T02:54:04.602592Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Superactivity of alpha-chymotrypsin with biological buffers, TRIS, TES, TAPS, and TAPSO in aqueous solutions
title Superactivity of alpha-chymotrypsin with biological buffers, TRIS, TES, TAPS, and TAPSO in aqueous solutions
spellingShingle Superactivity of alpha-chymotrypsin with biological buffers, TRIS, TES, TAPS, and TAPSO in aqueous solutions
Gupta, Bhupender S.
BOVINE SERUM-ALBUMIN
IONIC LIQUIDS
ORGANIC MEDIA
WATER
STABILITY
ENZYME
FLUORESCENCE
STABILIZATION
COMPLEXES
PROTEINS
title_short Superactivity of alpha-chymotrypsin with biological buffers, TRIS, TES, TAPS, and TAPSO in aqueous solutions
title_full Superactivity of alpha-chymotrypsin with biological buffers, TRIS, TES, TAPS, and TAPSO in aqueous solutions
title_fullStr Superactivity of alpha-chymotrypsin with biological buffers, TRIS, TES, TAPS, and TAPSO in aqueous solutions
title_full_unstemmed Superactivity of alpha-chymotrypsin with biological buffers, TRIS, TES, TAPS, and TAPSO in aqueous solutions
title_sort Superactivity of alpha-chymotrypsin with biological buffers, TRIS, TES, TAPS, and TAPSO in aqueous solutions
author Gupta, Bhupender S.
author_facet Gupta, Bhupender S.
Taha, Mohamed
Lee, Ming-Jer
author_role author
author2 Taha, Mohamed
Lee, Ming-Jer
author2_role author
author
dc.contributor.author.fl_str_mv Gupta, Bhupender S.
Taha, Mohamed
Lee, Ming-Jer
dc.subject.por.fl_str_mv BOVINE SERUM-ALBUMIN
IONIC LIQUIDS
ORGANIC MEDIA
WATER
STABILITY
ENZYME
FLUORESCENCE
STABILIZATION
COMPLEXES
PROTEINS
topic BOVINE SERUM-ALBUMIN
IONIC LIQUIDS
ORGANIC MEDIA
WATER
STABILITY
ENZYME
FLUORESCENCE
STABILIZATION
COMPLEXES
PROTEINS
description Biological buffers are always considered as non-toxic, biocompatible and green compounds. Therefore, we analyzed the catalytic activity of a commercial enzyme alpha-chymotrypsin (alpha-CT) in aqueous solutions of some common biological buffers (TRIS, TES, TAPS, and TAPSO) at pH 8 and T = 25 degrees C. It is found that the increase of the buffer concentration enhanced the catalytic activity of enzyme alpha-CT, and the tendency follows the order of TRIS > TES > TAPS > TAPSO. Especially in the presence of TRIS, the catalytic activity enhanced 5.5 fold.
publishDate 2014
dc.date.none.fl_str_mv 2014-01-01T00:00:00Z
2014
2017-12-07T19:06:56Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10773/19270
url http://hdl.handle.net/10773/19270
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 2046-2069
10.1039/c4ra09434d
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv ROYAL SOC CHEMISTRY
publisher.none.fl_str_mv ROYAL SOC CHEMISTRY
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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