Celluclast and Cellic® CTec2: Saccharification / fermentation of wheat straw, solid-liquid partition and potential of enzyme recycling by alkaline washing

Detalhes bibliográficos
Autor(a) principal: Rodrigues, Ana Cristina Costa
Data de Publicação: 2015
Outros Autores: Haven, Mai Østergaard, Lindedam, Jane, Felby, Claus, Gama, F. M.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/1822/37151
Resumo: The hydrolysis/fermentation of wheat straw and the adsorption/desorption/deactivation of cellulases were studied using Cellic® CTec2 (Cellic) and Celluclast mixed with Novozyme 188. The distribution of enzymes cellobiohydrolase I (Cel7A), endoglucanase I (Cel7B) and -glucosidase of the two formulations between the residual substrate and supernatant during the course of enzymatic hydrolysis and fermentation was investigated. The potential of recyclability using alkaline wash was also studied. The efficiency of hydrolysis with an enzyme load of 10 FPU/g cellulose reached >98 % using Cellic® CTec2, while for Celluclast a conversion of 52 % and 81 %, was observed without and with -glucosidase supplementation, respectively. The decrease of Cellic® CTec2 activity observed along the process was related to deactivation of Cel7A rather than of Cel7B and -glucosidase. The adsorption/desorption profiles during hydrolysis/fermentation revealed that a large fraction of active enzymes remained adsorbed to the solid residue throughout the process. Surprisingly, this was the case of Cel7A and -glucosidase from Cellic, which remained adsorbed to the solid fraction along the entire process. Alkaline washing was used to recover the enzymes from the solid residue. This method allowed efficient recovery of Celluclast enzymes; however, this may be achieved only when minor amounts of cellulose remain present. Regarding the Cellic formulation, neither the presence of cellulose nor lignin restricted an efficient desorption of the enzymes at alkaline pH. This work shows that the recycling strategy must be customized for each particular formulation, since the enzymes found e.g.in Cellic and Celluclast bear quite different behaviour regarding the solid-liquid distribution, stability and cellulose and lignin affinity.
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spelling Celluclast and Cellic® CTec2: Saccharification / fermentation of wheat straw, solid-liquid partition and potential of enzyme recycling by alkaline washingCellulasesEnzyme activity stabilityAdsorption/DesorptionEnzyme recyclingCiências Naturais::Ciências BiológicasEngenharia e Tecnologia::Biotecnologia IndustrialScience & TechnologyThe hydrolysis/fermentation of wheat straw and the adsorption/desorption/deactivation of cellulases were studied using Cellic® CTec2 (Cellic) and Celluclast mixed with Novozyme 188. The distribution of enzymes cellobiohydrolase I (Cel7A), endoglucanase I (Cel7B) and -glucosidase of the two formulations between the residual substrate and supernatant during the course of enzymatic hydrolysis and fermentation was investigated. The potential of recyclability using alkaline wash was also studied. The efficiency of hydrolysis with an enzyme load of 10 FPU/g cellulose reached >98 % using Cellic® CTec2, while for Celluclast a conversion of 52 % and 81 %, was observed without and with -glucosidase supplementation, respectively. The decrease of Cellic® CTec2 activity observed along the process was related to deactivation of Cel7A rather than of Cel7B and -glucosidase. The adsorption/desorption profiles during hydrolysis/fermentation revealed that a large fraction of active enzymes remained adsorbed to the solid residue throughout the process. Surprisingly, this was the case of Cel7A and -glucosidase from Cellic, which remained adsorbed to the solid fraction along the entire process. Alkaline washing was used to recover the enzymes from the solid residue. This method allowed efficient recovery of Celluclast enzymes; however, this may be achieved only when minor amounts of cellulose remain present. Regarding the Cellic formulation, neither the presence of cellulose nor lignin restricted an efficient desorption of the enzymes at alkaline pH. This work shows that the recycling strategy must be customized for each particular formulation, since the enzymes found e.g.in Cellic and Celluclast bear quite different behaviour regarding the solid-liquid distribution, stability and cellulose and lignin affinity.P7 KACELLE (Kalundborg Cellulosic Ethanol, Grant no. 239379) project for supporting this work. FCT Strategic Project of UID/BIO/ 04469/2013 unit, the project RECI/BBB-EBI/0179/2012 (FCOMP- 01-0124-FEDER-027462) and the Project “BioEnv—Biotechnology and Bioengineering for a sustainable world”, REF. NORTE-07-0124- FEDER-000048, co-funded by the Programa Operacional Regional do Norte (ON.2—O Novo Norte), QREN, FEDER.Elsevier B.V.Universidade do MinhoRodrigues, Ana Cristina CostaHaven, Mai ØstergaardLindedam, JaneFelby, ClausGama, F. M.2015-112015-11-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/37151engRodrigues, A.; Haven, Mai Østergaard; Lindedam, Jane; Felby, Claus; Gama, F. M., Celluclast and Cellic® CTec2: Saccharification / fermentation of wheat straw, solid-liquid partition and potential of enzyme recycling by alkaline washing. Enzyme and Microbial Technology, 79-80, 70-77, 20150141-02290141-022910.1016/j.enzmictec.2015.06.01926320717http://www.sciencedirect.com/science/article/pii/S0141022915300211info: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:RCAAP2023-07-21T12:21:09Zoai:repositorium.sdum.uminho.pt:1822/37151Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:14:21.218288Repositório 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 Celluclast and Cellic® CTec2: Saccharification / fermentation of wheat straw, solid-liquid partition and potential of enzyme recycling by alkaline washing
title Celluclast and Cellic® CTec2: Saccharification / fermentation of wheat straw, solid-liquid partition and potential of enzyme recycling by alkaline washing
spellingShingle Celluclast and Cellic® CTec2: Saccharification / fermentation of wheat straw, solid-liquid partition and potential of enzyme recycling by alkaline washing
Rodrigues, Ana Cristina Costa
Cellulases
Enzyme activity stability
Adsorption/Desorption
Enzyme recycling
Ciências Naturais::Ciências Biológicas
Engenharia e Tecnologia::Biotecnologia Industrial
Science & Technology
title_short Celluclast and Cellic® CTec2: Saccharification / fermentation of wheat straw, solid-liquid partition and potential of enzyme recycling by alkaline washing
title_full Celluclast and Cellic® CTec2: Saccharification / fermentation of wheat straw, solid-liquid partition and potential of enzyme recycling by alkaline washing
title_fullStr Celluclast and Cellic® CTec2: Saccharification / fermentation of wheat straw, solid-liquid partition and potential of enzyme recycling by alkaline washing
title_full_unstemmed Celluclast and Cellic® CTec2: Saccharification / fermentation of wheat straw, solid-liquid partition and potential of enzyme recycling by alkaline washing
title_sort Celluclast and Cellic® CTec2: Saccharification / fermentation of wheat straw, solid-liquid partition and potential of enzyme recycling by alkaline washing
author Rodrigues, Ana Cristina Costa
author_facet Rodrigues, Ana Cristina Costa
Haven, Mai Østergaard
Lindedam, Jane
Felby, Claus
Gama, F. M.
author_role author
author2 Haven, Mai Østergaard
Lindedam, Jane
Felby, Claus
Gama, F. M.
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Rodrigues, Ana Cristina Costa
Haven, Mai Østergaard
Lindedam, Jane
Felby, Claus
Gama, F. M.
dc.subject.por.fl_str_mv Cellulases
Enzyme activity stability
Adsorption/Desorption
Enzyme recycling
Ciências Naturais::Ciências Biológicas
Engenharia e Tecnologia::Biotecnologia Industrial
Science & Technology
topic Cellulases
Enzyme activity stability
Adsorption/Desorption
Enzyme recycling
Ciências Naturais::Ciências Biológicas
Engenharia e Tecnologia::Biotecnologia Industrial
Science & Technology
description The hydrolysis/fermentation of wheat straw and the adsorption/desorption/deactivation of cellulases were studied using Cellic® CTec2 (Cellic) and Celluclast mixed with Novozyme 188. The distribution of enzymes cellobiohydrolase I (Cel7A), endoglucanase I (Cel7B) and -glucosidase of the two formulations between the residual substrate and supernatant during the course of enzymatic hydrolysis and fermentation was investigated. The potential of recyclability using alkaline wash was also studied. The efficiency of hydrolysis with an enzyme load of 10 FPU/g cellulose reached >98 % using Cellic® CTec2, while for Celluclast a conversion of 52 % and 81 %, was observed without and with -glucosidase supplementation, respectively. The decrease of Cellic® CTec2 activity observed along the process was related to deactivation of Cel7A rather than of Cel7B and -glucosidase. The adsorption/desorption profiles during hydrolysis/fermentation revealed that a large fraction of active enzymes remained adsorbed to the solid residue throughout the process. Surprisingly, this was the case of Cel7A and -glucosidase from Cellic, which remained adsorbed to the solid fraction along the entire process. Alkaline washing was used to recover the enzymes from the solid residue. This method allowed efficient recovery of Celluclast enzymes; however, this may be achieved only when minor amounts of cellulose remain present. Regarding the Cellic formulation, neither the presence of cellulose nor lignin restricted an efficient desorption of the enzymes at alkaline pH. This work shows that the recycling strategy must be customized for each particular formulation, since the enzymes found e.g.in Cellic and Celluclast bear quite different behaviour regarding the solid-liquid distribution, stability and cellulose and lignin affinity.
publishDate 2015
dc.date.none.fl_str_mv 2015-11
2015-11-01T00:00:00Z
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/1822/37151
url http://hdl.handle.net/1822/37151
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Rodrigues, A.; Haven, Mai Østergaard; Lindedam, Jane; Felby, Claus; Gama, F. M., Celluclast and Cellic® CTec2: Saccharification / fermentation of wheat straw, solid-liquid partition and potential of enzyme recycling by alkaline washing. Enzyme and Microbial Technology, 79-80, 70-77, 2015
0141-0229
0141-0229
10.1016/j.enzmictec.2015.06.019
26320717
http://www.sciencedirect.com/science/article/pii/S0141022915300211
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
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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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