Stabilization study of tetrameric kluyveromyces lactis β-galactosidase by immobilization on immobead: thermal, physico-chemical, textural and catalytic properties
Autor(a) principal: | |
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Data de Publicação: | 2019 |
Outros Autores: | , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UFRGS |
Texto Completo: | http://hdl.handle.net/10183/262355 |
Resumo: | We investigated the immobilization of a tetrameric Kluyveromyces lactis β-galactosidase (EC: 3.2.1.23) (KL-Gal) on Immobead 150 using different support modification strategies. Immobead support was modified using an acid solution of H2SO4:HNO3 (3:1) (Immobead-Ac) or 5 % (v/v) glutaraldehyde (Immobead-Glu). Its unmodified form (Immobead) was also tested. Immobilization yields and efficiencies were evaluated by testing protein loads from 10 to 200 mg.g-1 support. The thermal, physico-chemical, textural and catalytic properties of the supports (modified and unmodified) and their derivatives (Immobead-KL-Gal, Immobead-Ac-KL-Gal and Immobead-Glu-KL-Gal) were analyzed. The highest immobilization yields and efficiencies were achieved with a protein load of 100 mg.g-1 support. Surface and pore areas of the Immobead support were greatly decreased after modification. Michaelis constant of the immobilized β-galactosidase increased in the derivatives. Maximum velocity decreased approximately 2.8 times for Immobead-KL-Gal and Immobead-Glu-KL-Gal, and approximately 1.4 times for Immobead-Ac-KL-Gal. In batch processes, the three derivatives could be reused successfully at least 15 times, maintaining high residual enzymatic activity during the lactose hydrolysis (in both cheese whey and milk). The tetrameric K. lactis β-galactosidase immobilized on Immobead supports via the tested treatments was stabilized and is an alternative tool for lactose hydrolysis in the dairy industry. |
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Gennari, AdrianoMobayed, Francielle H.Rafael, Ruan da SilvaCatto, André LuisBenvenutti, Edilson ValmirRodrigues, Rafael CostaSperotto, Raul AntonioVolpato, GiandraSouza, Claucia Fernanda Volken de2023-07-19T03:40:29Z20190104-6632http://hdl.handle.net/10183/262355001168677We investigated the immobilization of a tetrameric Kluyveromyces lactis β-galactosidase (EC: 3.2.1.23) (KL-Gal) on Immobead 150 using different support modification strategies. Immobead support was modified using an acid solution of H2SO4:HNO3 (3:1) (Immobead-Ac) or 5 % (v/v) glutaraldehyde (Immobead-Glu). Its unmodified form (Immobead) was also tested. Immobilization yields and efficiencies were evaluated by testing protein loads from 10 to 200 mg.g-1 support. The thermal, physico-chemical, textural and catalytic properties of the supports (modified and unmodified) and their derivatives (Immobead-KL-Gal, Immobead-Ac-KL-Gal and Immobead-Glu-KL-Gal) were analyzed. The highest immobilization yields and efficiencies were achieved with a protein load of 100 mg.g-1 support. Surface and pore areas of the Immobead support were greatly decreased after modification. Michaelis constant of the immobilized β-galactosidase increased in the derivatives. Maximum velocity decreased approximately 2.8 times for Immobead-KL-Gal and Immobead-Glu-KL-Gal, and approximately 1.4 times for Immobead-Ac-KL-Gal. In batch processes, the three derivatives could be reused successfully at least 15 times, maintaining high residual enzymatic activity during the lactose hydrolysis (in both cheese whey and milk). The tetrameric K. lactis β-galactosidase immobilized on Immobead supports via the tested treatments was stabilized and is an alternative tool for lactose hydrolysis in the dairy industry.application/pdfengBrazilian journal of chemical engineering [recurso eletrônico]. São Paulo. Vol. 36, n. 04 (Oct 2019),p. 1403-1417GlutaraldehydeAcid solutionBatch hydrolysisYeastStabilization study of tetrameric kluyveromyces lactis β-galactosidase by immobilization on immobead: thermal, physico-chemical, textural and catalytic propertiesinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/otherinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UFRGSinstname:Universidade Federal do Rio Grande do Sul (UFRGS)instacron:UFRGSTEXT001168677.pdf.txt001168677.pdf.txtExtracted Texttext/plain63176http://www.lume.ufrgs.br/bitstream/10183/262355/2/001168677.pdf.txt6f317a8c27640b07b985e944c466447aMD52ORIGINAL001168677.pdfTexto completo (inglês)application/pdf4905758http://www.lume.ufrgs.br/bitstream/10183/262355/1/001168677.pdf759a7f1cb4785b65454a62ffc211280fMD5110183/2623552023-07-20 03:35:51.554132oai:www.lume.ufrgs.br:10183/262355Repositório de PublicaçõesPUBhttps://lume.ufrgs.br/oai/requestopendoar:2023-07-20T06:35:51Repositório Institucional da UFRGS - Universidade Federal do Rio Grande do Sul (UFRGS)false |
dc.title.pt_BR.fl_str_mv |
Stabilization study of tetrameric kluyveromyces lactis β-galactosidase by immobilization on immobead: thermal, physico-chemical, textural and catalytic properties |
title |
Stabilization study of tetrameric kluyveromyces lactis β-galactosidase by immobilization on immobead: thermal, physico-chemical, textural and catalytic properties |
spellingShingle |
Stabilization study of tetrameric kluyveromyces lactis β-galactosidase by immobilization on immobead: thermal, physico-chemical, textural and catalytic properties Gennari, Adriano Glutaraldehyde Acid solution Batch hydrolysis Yeast |
title_short |
Stabilization study of tetrameric kluyveromyces lactis β-galactosidase by immobilization on immobead: thermal, physico-chemical, textural and catalytic properties |
title_full |
Stabilization study of tetrameric kluyveromyces lactis β-galactosidase by immobilization on immobead: thermal, physico-chemical, textural and catalytic properties |
title_fullStr |
Stabilization study of tetrameric kluyveromyces lactis β-galactosidase by immobilization on immobead: thermal, physico-chemical, textural and catalytic properties |
title_full_unstemmed |
Stabilization study of tetrameric kluyveromyces lactis β-galactosidase by immobilization on immobead: thermal, physico-chemical, textural and catalytic properties |
title_sort |
Stabilization study of tetrameric kluyveromyces lactis β-galactosidase by immobilization on immobead: thermal, physico-chemical, textural and catalytic properties |
author |
Gennari, Adriano |
author_facet |
Gennari, Adriano Mobayed, Francielle H. Rafael, Ruan da Silva Catto, André Luis Benvenutti, Edilson Valmir Rodrigues, Rafael Costa Sperotto, Raul Antonio Volpato, Giandra Souza, Claucia Fernanda Volken de |
author_role |
author |
author2 |
Mobayed, Francielle H. Rafael, Ruan da Silva Catto, André Luis Benvenutti, Edilson Valmir Rodrigues, Rafael Costa Sperotto, Raul Antonio Volpato, Giandra Souza, Claucia Fernanda Volken de |
author2_role |
author author author author author author author author |
dc.contributor.author.fl_str_mv |
Gennari, Adriano Mobayed, Francielle H. Rafael, Ruan da Silva Catto, André Luis Benvenutti, Edilson Valmir Rodrigues, Rafael Costa Sperotto, Raul Antonio Volpato, Giandra Souza, Claucia Fernanda Volken de |
dc.subject.eng.fl_str_mv |
Glutaraldehyde Acid solution Batch hydrolysis Yeast |
topic |
Glutaraldehyde Acid solution Batch hydrolysis Yeast |
description |
We investigated the immobilization of a tetrameric Kluyveromyces lactis β-galactosidase (EC: 3.2.1.23) (KL-Gal) on Immobead 150 using different support modification strategies. Immobead support was modified using an acid solution of H2SO4:HNO3 (3:1) (Immobead-Ac) or 5 % (v/v) glutaraldehyde (Immobead-Glu). Its unmodified form (Immobead) was also tested. Immobilization yields and efficiencies were evaluated by testing protein loads from 10 to 200 mg.g-1 support. The thermal, physico-chemical, textural and catalytic properties of the supports (modified and unmodified) and their derivatives (Immobead-KL-Gal, Immobead-Ac-KL-Gal and Immobead-Glu-KL-Gal) were analyzed. The highest immobilization yields and efficiencies were achieved with a protein load of 100 mg.g-1 support. Surface and pore areas of the Immobead support were greatly decreased after modification. Michaelis constant of the immobilized β-galactosidase increased in the derivatives. Maximum velocity decreased approximately 2.8 times for Immobead-KL-Gal and Immobead-Glu-KL-Gal, and approximately 1.4 times for Immobead-Ac-KL-Gal. In batch processes, the three derivatives could be reused successfully at least 15 times, maintaining high residual enzymatic activity during the lactose hydrolysis (in both cheese whey and milk). The tetrameric K. lactis β-galactosidase immobilized on Immobead supports via the tested treatments was stabilized and is an alternative tool for lactose hydrolysis in the dairy industry. |
publishDate |
2019 |
dc.date.issued.fl_str_mv |
2019 |
dc.date.accessioned.fl_str_mv |
2023-07-19T03:40:29Z |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/other |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10183/262355 |
dc.identifier.issn.pt_BR.fl_str_mv |
0104-6632 |
dc.identifier.nrb.pt_BR.fl_str_mv |
001168677 |
identifier_str_mv |
0104-6632 001168677 |
url |
http://hdl.handle.net/10183/262355 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartof.pt_BR.fl_str_mv |
Brazilian journal of chemical engineering [recurso eletrônico]. São Paulo. Vol. 36, n. 04 (Oct 2019),p. 1403-1417 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
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application/pdf |
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