Possibilities for recycling cellulases after use in celllase processing - part I: effects of end-product inhibition, thermal and mechanical deactivation, and cellulase depletion by adsorption

Detalhes bibliográficos
Autor(a) principal: Azevedo, Helena S.
Data de Publicação: 2002
Outros Autores: Bishop, David, Paulo, Artur Cavaco
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: https://hdl.handle.net/1822/2656
Resumo: Preliminary recycling experiments with cellulase enzymes after cotton treatments at 50°C showed that activity remaining in the treatment liquors was reduced by about 80% after five recycling steps. The potential problems of end-product inhibition, thermal and mechanical deactivation, and the loss of some components of the cellulase complex by preferential and or irreversible adsorption to cotton substrates were studied. End-product inhibition studies showed that the build-up of cellobiose and glucose would be expected to cause no more than 40% activity loss after five textile treatment cycles. Thermal and mechanical treatments of cellulases suggested that the enzymes start to be deactivated at 60°C and agitation levels similar to those used in textile processing did not cause significant enzyme deactivation. Analysis of cellulase solutions, by fast protein liquid chromatography, before and after adsorption on cotton fabrics, suggested that the cellobiohydrolase II (Cel6A) content of the cellulase complex was reduced, relative to the other components, by preferential adsorption. This would lead to a marked reduction in activity after several treatment cycles and top-up with pure cellobiohydrolase II would be necessary unless this component is easily recoverable from the treated fabric.
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spelling Possibilities for recycling cellulases after use in celllase processing - part I: effects of end-product inhibition, thermal and mechanical deactivation, and cellulase depletion by adsorptionCellulasesTextile processingEnzyme recyclingAdsorptionDeactivationDepletionInhibitionPreliminary recycling experiments with cellulase enzymes after cotton treatments at 50°C showed that activity remaining in the treatment liquors was reduced by about 80% after five recycling steps. The potential problems of end-product inhibition, thermal and mechanical deactivation, and the loss of some components of the cellulase complex by preferential and or irreversible adsorption to cotton substrates were studied. End-product inhibition studies showed that the build-up of cellobiose and glucose would be expected to cause no more than 40% activity loss after five textile treatment cycles. Thermal and mechanical treatments of cellulases suggested that the enzymes start to be deactivated at 60°C and agitation levels similar to those used in textile processing did not cause significant enzyme deactivation. Analysis of cellulase solutions, by fast protein liquid chromatography, before and after adsorption on cotton fabrics, suggested that the cellobiohydrolase II (Cel6A) content of the cellulase complex was reduced, relative to the other components, by preferential adsorption. This would lead to a marked reduction in activity after several treatment cycles and top-up with pure cellobiohydrolase II would be necessary unless this component is easily recoverable from the treated fabric.(undefined)Humana PressUniversidade do MinhoAzevedo, Helena S.Bishop, DavidPaulo, Artur Cavaco2002-042002-04-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/1822/2656engAzevedo, H., Bishop, D. & Cavaco-Paulo, A. Possibilities for recycling cellulases after use in cotton processing. Appl Biochem Biotechnol 101, 61–75 (2002). https://doi.org/10.1385/ABAB:101:1:610273-228910.1385/ABAB:101:1:6112008867https://link.springer.com/article/10.1385/ABAB:101:1:61info: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:RCAAP2023-07-21T12:47:25Zoai:repositorium.sdum.uminho.pt:1822/2656Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:45:31.904696Repositório 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 Possibilities for recycling cellulases after use in celllase processing - part I: effects of end-product inhibition, thermal and mechanical deactivation, and cellulase depletion by adsorption
title Possibilities for recycling cellulases after use in celllase processing - part I: effects of end-product inhibition, thermal and mechanical deactivation, and cellulase depletion by adsorption
spellingShingle Possibilities for recycling cellulases after use in celllase processing - part I: effects of end-product inhibition, thermal and mechanical deactivation, and cellulase depletion by adsorption
Azevedo, Helena S.
Cellulases
Textile processing
Enzyme recycling
Adsorption
Deactivation
Depletion
Inhibition
title_short Possibilities for recycling cellulases after use in celllase processing - part I: effects of end-product inhibition, thermal and mechanical deactivation, and cellulase depletion by adsorption
title_full Possibilities for recycling cellulases after use in celllase processing - part I: effects of end-product inhibition, thermal and mechanical deactivation, and cellulase depletion by adsorption
title_fullStr Possibilities for recycling cellulases after use in celllase processing - part I: effects of end-product inhibition, thermal and mechanical deactivation, and cellulase depletion by adsorption
title_full_unstemmed Possibilities for recycling cellulases after use in celllase processing - part I: effects of end-product inhibition, thermal and mechanical deactivation, and cellulase depletion by adsorption
title_sort Possibilities for recycling cellulases after use in celllase processing - part I: effects of end-product inhibition, thermal and mechanical deactivation, and cellulase depletion by adsorption
author Azevedo, Helena S.
author_facet Azevedo, Helena S.
Bishop, David
Paulo, Artur Cavaco
author_role author
author2 Bishop, David
Paulo, Artur Cavaco
author2_role author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Azevedo, Helena S.
Bishop, David
Paulo, Artur Cavaco
dc.subject.por.fl_str_mv Cellulases
Textile processing
Enzyme recycling
Adsorption
Deactivation
Depletion
Inhibition
topic Cellulases
Textile processing
Enzyme recycling
Adsorption
Deactivation
Depletion
Inhibition
description Preliminary recycling experiments with cellulase enzymes after cotton treatments at 50°C showed that activity remaining in the treatment liquors was reduced by about 80% after five recycling steps. The potential problems of end-product inhibition, thermal and mechanical deactivation, and the loss of some components of the cellulase complex by preferential and or irreversible adsorption to cotton substrates were studied. End-product inhibition studies showed that the build-up of cellobiose and glucose would be expected to cause no more than 40% activity loss after five textile treatment cycles. Thermal and mechanical treatments of cellulases suggested that the enzymes start to be deactivated at 60°C and agitation levels similar to those used in textile processing did not cause significant enzyme deactivation. Analysis of cellulase solutions, by fast protein liquid chromatography, before and after adsorption on cotton fabrics, suggested that the cellobiohydrolase II (Cel6A) content of the cellulase complex was reduced, relative to the other components, by preferential adsorption. This would lead to a marked reduction in activity after several treatment cycles and top-up with pure cellobiohydrolase II would be necessary unless this component is easily recoverable from the treated fabric.
publishDate 2002
dc.date.none.fl_str_mv 2002-04
2002-04-01T00:00:00Z
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 https://hdl.handle.net/1822/2656
url https://hdl.handle.net/1822/2656
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Azevedo, H., Bishop, D. & Cavaco-Paulo, A. Possibilities for recycling cellulases after use in cotton processing. Appl Biochem Biotechnol 101, 61–75 (2002). https://doi.org/10.1385/ABAB:101:1:61
0273-2289
10.1385/ABAB:101:1:61
12008867
https://link.springer.com/article/10.1385/ABAB:101:1:61
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 Humana Press
publisher.none.fl_str_mv Humana Press
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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