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
Autor(a) principal: | |
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Data de Publicação: | 2002 |
Outros Autores: | , |
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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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 |
repository.mail.fl_str_mv |
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1799133020987326464 |