The immobilization of penicillin G acylase on modified TiO2 with various micro-environments

Immobilization of penicillin G acylase (PGA) on carriers is an effective strategy for running away from the drawbacks of free PGA. In this work, modified TiO2 was employed as a carrier for the immobilization of PGA. Firstly, TiO2 was used as a nucleus and modified by two different approaches, one-st...

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Detalles Bibliográficos
Autores: Liu, Chunli, Wang, Xudong, Chen, Zhenbin, Zhou, Yongshan, Ruso Beiras, Juan Manuel, Hu, Dongdong, Liu, Zhen, Liao, Yiliang
Tipo de recurso: artículo
Fecha de publicación:2021
País:España
Institución:Universidad de Santiago de Compostela (USC)
Repositorio:Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela
Idioma:inglés
OAI Identifier:oai:minerva.usc.gal:10347/44206
Acceso en línea:https://hdl.handle.net/10347/44206
Access Level:acceso abierto
Palabra clave:Modified TiO2
Penicillin G acylase
Micro-environments
Catalytic performance
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spelling The immobilization of penicillin G acylase on modified TiO2 with various micro-environmentsLiu, ChunliWang, XudongChen, ZhenbinZhou, YongshanRuso Beiras, Juan ManuelHu, DongdongLiu, ZhenLiao, YiliangModified TiO2Penicillin G acylaseMicro-environmentsCatalytic performanceImmobilization of penicillin G acylase (PGA) on carriers is an effective strategy for running away from the drawbacks of free PGA. In this work, modified TiO2 was employed as a carrier for the immobilization of PGA. Firstly, TiO2 was used as a nucleus and modified by two different approaches, one-step modification and two-step modification, to construct and regulate the micro-environment of carrier, particularly by changing the type of functional immobilization groups, and the arm-length of immobilization sites. In the one-step modification approach, TiO2 was altered by glutaraldehyde, 3-glycidoxypropyltrimethoxysilane (3-GCDPTMS) and 3-aminopropyltriethoxysilane (3-APTMS), separately; while in the two-step modification approach, primary TiO2 was firstly altered with a small amount of glutaraldehyde or 3-GCDPTMS, then followed by a secondary modification process using glutaraldehyde and 3-GCDPTMS, respectively. Secondly, the influence of the micro-environments of carrier on the catalytic performance of immobilized PGA, in terms of enzyme loading capacity (ELC), enzyme activity (EA) and activity retention ratio (EAR) was investigated. Results revealed that PGA immobilized on carrier modified by 3-GCDPTMS, with a graft rate of 30 % had the best performance, which had an ELC of 10,800 U, EA of 14,900 U/g. Both of the functional group and arm-length of immobilization site had influence on the catalytic performance of immobilized PGA, and the functional groups of immobilization site was the most essential one responsible for stabilizing PGA and improving its catalytic activity. Then PGA immobilized carrier with longer arm-length had better catalytic performance.ElsevierUniversidade de Santiago de Compostela. Departamento de Física Aplicada20212021-02-1620212021-02-16journal articlehttp://purl.org/coar/resource_type/c_6501AMhttp://purl.org/coar/version/c_ab4af688f83e57aainfo:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/10347/44206reponame:Minerva. Repositorio Institucional de la Universidad de Santiago de Compostelainstname:Universidad de Santiago de Compostela (USC)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2Attribution-NonCommercial-NoDerivatives 4.0 Internationalhttp://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccessoai:minerva.usc.gal:10347/442062026-06-15T12:47:27Z
dc.title.none.fl_str_mv The immobilization of penicillin G acylase on modified TiO2 with various micro-environments
title The immobilization of penicillin G acylase on modified TiO2 with various micro-environments
spellingShingle The immobilization of penicillin G acylase on modified TiO2 with various micro-environments
Liu, Chunli
Modified TiO2
Penicillin G acylase
Micro-environments
Catalytic performance
title_short The immobilization of penicillin G acylase on modified TiO2 with various micro-environments
title_full The immobilization of penicillin G acylase on modified TiO2 with various micro-environments
title_fullStr The immobilization of penicillin G acylase on modified TiO2 with various micro-environments
title_full_unstemmed The immobilization of penicillin G acylase on modified TiO2 with various micro-environments
title_sort The immobilization of penicillin G acylase on modified TiO2 with various micro-environments
dc.creator.none.fl_str_mv Liu, Chunli
Wang, Xudong
Chen, Zhenbin
Zhou, Yongshan
Ruso Beiras, Juan Manuel
Hu, Dongdong
Liu, Zhen
Liao, Yiliang
author Liu, Chunli
author_facet Liu, Chunli
Wang, Xudong
Chen, Zhenbin
Zhou, Yongshan
Ruso Beiras, Juan Manuel
Hu, Dongdong
Liu, Zhen
Liao, Yiliang
author_role author
author2 Wang, Xudong
Chen, Zhenbin
Zhou, Yongshan
Ruso Beiras, Juan Manuel
Hu, Dongdong
Liu, Zhen
Liao, Yiliang
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade de Santiago de Compostela. Departamento de Física Aplicada
dc.subject.none.fl_str_mv Modified TiO2
Penicillin G acylase
Micro-environments
Catalytic performance
topic Modified TiO2
Penicillin G acylase
Micro-environments
Catalytic performance
description Immobilization of penicillin G acylase (PGA) on carriers is an effective strategy for running away from the drawbacks of free PGA. In this work, modified TiO2 was employed as a carrier for the immobilization of PGA. Firstly, TiO2 was used as a nucleus and modified by two different approaches, one-step modification and two-step modification, to construct and regulate the micro-environment of carrier, particularly by changing the type of functional immobilization groups, and the arm-length of immobilization sites. In the one-step modification approach, TiO2 was altered by glutaraldehyde, 3-glycidoxypropyltrimethoxysilane (3-GCDPTMS) and 3-aminopropyltriethoxysilane (3-APTMS), separately; while in the two-step modification approach, primary TiO2 was firstly altered with a small amount of glutaraldehyde or 3-GCDPTMS, then followed by a secondary modification process using glutaraldehyde and 3-GCDPTMS, respectively. Secondly, the influence of the micro-environments of carrier on the catalytic performance of immobilized PGA, in terms of enzyme loading capacity (ELC), enzyme activity (EA) and activity retention ratio (EAR) was investigated. Results revealed that PGA immobilized on carrier modified by 3-GCDPTMS, with a graft rate of 30 % had the best performance, which had an ELC of 10,800 U, EA of 14,900 U/g. Both of the functional group and arm-length of immobilization site had influence on the catalytic performance of immobilized PGA, and the functional groups of immobilization site was the most essential one responsible for stabilizing PGA and improving its catalytic activity. Then PGA immobilized carrier with longer arm-length had better catalytic performance.
publishDate 2021
dc.date.none.fl_str_mv 2021
2021-02-16
2021
2021-02-16
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
AM
http://purl.org/coar/version/c_ab4af688f83e57aa
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/10347/44206
url https://hdl.handle.net/10347/44206
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution-NonCommercial-NoDerivatives 4.0 International
http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution-NonCommercial-NoDerivatives 4.0 International
http://creativecommons.org/licenses/by-nc-nd/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela
instname:Universidad de Santiago de Compostela (USC)
instname_str Universidad de Santiago de Compostela (USC)
reponame_str Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela
collection Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,811543

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