Laccase-catalyzed cross-linking of BSA mediated by tyrosine
Autor(a) principal: | |
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Data de Publicação: | 2021 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/1822/68034 |
Resumo: | Tyrosine was explored as a cross-linking agent to form cross-linked bovine serum albumin (BSA) using laccase as a catalyst. Liquid chromatography-mass spectrometry (LC-MS) and fluorescence spectra indicated that tyrosine can be mainly oxidized to be dityrosine. Spectra analysis and molecular weight were used to characterize the BSA treated with tyrosine and laccase. Both SDS-PAGE and size exclusion chromatography confirmed the formation of cross-linked BSA, while most of the protein products existed as BSA–tyrosine conjugates. The MALDI-TOF analysis revealed that five tyrosine units were grafted on one BSA monomer, however one cross-linked BSA consists of two BSA monomers and 18 tyrosine. Furthermore, the content of the amino acid of BSA was identified using amino acid analysis, among those the percentage of lysine presented a visible decline from 12.36% to 11.43%, corresponding to 4-5 lysine residues. The pure and modified BSA were hydrolyzed by trypsin and the corresponding peptides were obtained. Different mass of five peptides from LC-MS spectra after hydrolysis indicated that tyrosine could react with Lys-136, Lys-204, Lys-224, Lys-322 and Lys-537 in BSA, promoting the formation of BSA–tyrosine conjugates and cross-linked BSA. |
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Laccase-catalyzed cross-linking of BSA mediated by tyrosineCross-linkingBovine serum albuminTyrosineLaccaseEngenharia e Tecnologia::Biotecnologia IndustrialScience & TechnologyTyrosine was explored as a cross-linking agent to form cross-linked bovine serum albumin (BSA) using laccase as a catalyst. Liquid chromatography-mass spectrometry (LC-MS) and fluorescence spectra indicated that tyrosine can be mainly oxidized to be dityrosine. Spectra analysis and molecular weight were used to characterize the BSA treated with tyrosine and laccase. Both SDS-PAGE and size exclusion chromatography confirmed the formation of cross-linked BSA, while most of the protein products existed as BSA–tyrosine conjugates. The MALDI-TOF analysis revealed that five tyrosine units were grafted on one BSA monomer, however one cross-linked BSA consists of two BSA monomers and 18 tyrosine. Furthermore, the content of the amino acid of BSA was identified using amino acid analysis, among those the percentage of lysine presented a visible decline from 12.36% to 11.43%, corresponding to 4-5 lysine residues. The pure and modified BSA were hydrolyzed by trypsin and the corresponding peptides were obtained. Different mass of five peptides from LC-MS spectra after hydrolysis indicated that tyrosine could react with Lys-136, Lys-204, Lys-224, Lys-322 and Lys-537 in BSA, promoting the formation of BSA–tyrosine conjugates and cross-linked BSA.This study was supported by Chinese Government Scholarship under China Scholar Council (NO. 201906790043) and “the Fundamental Research Funds for the Central Universities (NO. JUSRP52007A). This study was also supported by the Portuguese Foundation for Science and Technology (FCT) under the scope of the strategic funding of UIDB/04469/2020 unit and BioTecNorte operation (NORTE-01-0145-FEDER-000004) funded by the European Regional Development Fund under the scope of Norte2020 - Programa Operacional Regional do Norte.Elsevier B.V.Universidade do MinhoYu LiSu, JingCavaco-Paulo, Artur2021-012021-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/68034engY. Li, J. Su and A. Cavaco-Paulo, Laccase-catalyzed crosslinking of BSA mediated by tyrosine, International Journal of Biological Macromolecules (2021), https://doi.org/10.1016/j.ijbiomac.2020.10.2370141-813010.1016/j.ijbiomac.2020.10.23733147436https://www.sciencedirect.com/science/article/abs/pii/S0141813020348893info: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:RCAAP2023-07-21T12:07:55Zoai:repositorium.sdum.uminho.pt:1822/68034Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:59:00.631624Repositório 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 |
Laccase-catalyzed cross-linking of BSA mediated by tyrosine |
title |
Laccase-catalyzed cross-linking of BSA mediated by tyrosine |
spellingShingle |
Laccase-catalyzed cross-linking of BSA mediated by tyrosine Yu Li Cross-linking Bovine serum albumin Tyrosine Laccase Engenharia e Tecnologia::Biotecnologia Industrial Science & Technology |
title_short |
Laccase-catalyzed cross-linking of BSA mediated by tyrosine |
title_full |
Laccase-catalyzed cross-linking of BSA mediated by tyrosine |
title_fullStr |
Laccase-catalyzed cross-linking of BSA mediated by tyrosine |
title_full_unstemmed |
Laccase-catalyzed cross-linking of BSA mediated by tyrosine |
title_sort |
Laccase-catalyzed cross-linking of BSA mediated by tyrosine |
author |
Yu Li |
author_facet |
Yu Li Su, Jing Cavaco-Paulo, Artur |
author_role |
author |
author2 |
Su, Jing Cavaco-Paulo, Artur |
author2_role |
author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Yu Li Su, Jing Cavaco-Paulo, Artur |
dc.subject.por.fl_str_mv |
Cross-linking Bovine serum albumin Tyrosine Laccase Engenharia e Tecnologia::Biotecnologia Industrial Science & Technology |
topic |
Cross-linking Bovine serum albumin Tyrosine Laccase Engenharia e Tecnologia::Biotecnologia Industrial Science & Technology |
description |
Tyrosine was explored as a cross-linking agent to form cross-linked bovine serum albumin (BSA) using laccase as a catalyst. Liquid chromatography-mass spectrometry (LC-MS) and fluorescence spectra indicated that tyrosine can be mainly oxidized to be dityrosine. Spectra analysis and molecular weight were used to characterize the BSA treated with tyrosine and laccase. Both SDS-PAGE and size exclusion chromatography confirmed the formation of cross-linked BSA, while most of the protein products existed as BSA–tyrosine conjugates. The MALDI-TOF analysis revealed that five tyrosine units were grafted on one BSA monomer, however one cross-linked BSA consists of two BSA monomers and 18 tyrosine. Furthermore, the content of the amino acid of BSA was identified using amino acid analysis, among those the percentage of lysine presented a visible decline from 12.36% to 11.43%, corresponding to 4-5 lysine residues. The pure and modified BSA were hydrolyzed by trypsin and the corresponding peptides were obtained. Different mass of five peptides from LC-MS spectra after hydrolysis indicated that tyrosine could react with Lys-136, Lys-204, Lys-224, Lys-322 and Lys-537 in BSA, promoting the formation of BSA–tyrosine conjugates and cross-linked BSA. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-01 2021-01-01T00:00:00Z |
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/1822/68034 |
url |
http://hdl.handle.net/1822/68034 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Y. Li, J. Su and A. Cavaco-Paulo, Laccase-catalyzed crosslinking of BSA mediated by tyrosine, International Journal of Biological Macromolecules (2021), https://doi.org/10.1016/j.ijbiomac.2020.10.237 0141-8130 10.1016/j.ijbiomac.2020.10.237 33147436 https://www.sciencedirect.com/science/article/abs/pii/S0141813020348893 |
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 |
Elsevier B.V. |
publisher.none.fl_str_mv |
Elsevier B.V. |
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 |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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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 |
repository.mail.fl_str_mv |
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1799132381494378496 |