Characterisation and application of glycanases secreted by aspergillus terreus CCMI 498 and trichoderma viride CCMI 84 for enzymatic deinking of mixed office wastepaper

Detalhes bibliográficos
Autor(a) principal: Marques, S.
Data de Publicação: 2003
Outros Autores: Pala, H., Alves, L., Amaral-Collaço, M. T., Gama, F. M., Gírio, F. M.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: https://hdl.handle.net/1822/1485
Resumo: Two enzymatic extracts obtained from xylan-grown Aspergillus terreus CCMI 498 and cellulose-grown Trichoderma viride CCMI 84 were characterised for different glycanase activities. Both strains produce extracellular endoxylanase and endoglucanase enzymes. The enzymes optimal activity was found in the temperature range of 45-60 ºC. Endoglucanase systems show identical activity profiles towards temperature, regardless of the strain and inducing substrate. Conversely, the endoxylanases produced by both strains showed maximal activity at different pH values (from 4.5 to 5.5), being the more acidic xylanase produced by T. viride grown on cellulose. The endoglucanase activities have an optimum pH at 4.5-5.0. The endoxylanase and endoglucanase activities exhibited high stability at 50 ºC and pH 5.0. Mannanase, β-xylosidase, and amylase activities were also found, being the first two activities only present for T. viride extract. These two enzymatic extracts were used for mixed office wastepaper (MOW) deinking. When the enzymatic extract from T. viride was used, a further increase of 24% in ink removal was obtained by comparison with the control. Both enzymes contributed to the improvement of the paper strength properties and the obtained results clearly indicate that the effective use of enzymes for deinking can also contribute to the pulp and paper properties improvement.
id RCAP_1d3687af1acbe971f0e632fe5a033490
oai_identifier_str oai:repositorium.sdum.uminho.pt:1822/1485
network_acronym_str RCAP
network_name_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository_id_str 7160
spelling Characterisation and application of glycanases secreted by aspergillus terreus CCMI 498 and trichoderma viride CCMI 84 for enzymatic deinking of mixed office wastepaperHemicellulaseEndoglucanaseAmylaseEnzymatic deinkingAspergillus terreusTrichoderma virideScience & TechnologyTwo enzymatic extracts obtained from xylan-grown Aspergillus terreus CCMI 498 and cellulose-grown Trichoderma viride CCMI 84 were characterised for different glycanase activities. Both strains produce extracellular endoxylanase and endoglucanase enzymes. The enzymes optimal activity was found in the temperature range of 45-60 ºC. Endoglucanase systems show identical activity profiles towards temperature, regardless of the strain and inducing substrate. Conversely, the endoxylanases produced by both strains showed maximal activity at different pH values (from 4.5 to 5.5), being the more acidic xylanase produced by T. viride grown on cellulose. The endoglucanase activities have an optimum pH at 4.5-5.0. The endoxylanase and endoglucanase activities exhibited high stability at 50 ºC and pH 5.0. Mannanase, β-xylosidase, and amylase activities were also found, being the first two activities only present for T. viride extract. These two enzymatic extracts were used for mixed office wastepaper (MOW) deinking. When the enzymatic extract from T. viride was used, a further increase of 24% in ink removal was obtained by comparison with the control. Both enzymes contributed to the improvement of the paper strength properties and the obtained results clearly indicate that the effective use of enzymes for deinking can also contribute to the pulp and paper properties improvement.PRAXIS/BIO/1133/95. BIC/3087/96, BD/3253/96.Elsevier ScienceUniversidade do MinhoMarques, S.Pala, H.Alves, L.Amaral-Collaço, M. T.Gama, F. M.Gírio, F. M.20032003-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/1822/1485engMarques, S., Pala, H., Alves, L., Amaral-Collaço, M. T., Gama, F. M., & Gı́rio, F. M. (2003, February). Characterisation and application of glycanases secreted by Aspergillus terreus CCMI 498 and Trichoderma viride CCMI 84 for enzymatic deinking of mixed office wastepaper. Journal of Biotechnology. Elsevier BV. http://doi.org/10.1016/s0168-1656(02)00247-x0168-165610.1016/S0168-1656(02)00247-X12443852info: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:RCAAP2023-07-21T12:23:28Zoai:repositorium.sdum.uminho.pt:1822/1485Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:17:12.255332Repositório 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 Characterisation and application of glycanases secreted by aspergillus terreus CCMI 498 and trichoderma viride CCMI 84 for enzymatic deinking of mixed office wastepaper
title Characterisation and application of glycanases secreted by aspergillus terreus CCMI 498 and trichoderma viride CCMI 84 for enzymatic deinking of mixed office wastepaper
spellingShingle Characterisation and application of glycanases secreted by aspergillus terreus CCMI 498 and trichoderma viride CCMI 84 for enzymatic deinking of mixed office wastepaper
Marques, S.
Hemicellulase
Endoglucanase
Amylase
Enzymatic deinking
Aspergillus terreus
Trichoderma viride
Science & Technology
title_short Characterisation and application of glycanases secreted by aspergillus terreus CCMI 498 and trichoderma viride CCMI 84 for enzymatic deinking of mixed office wastepaper
title_full Characterisation and application of glycanases secreted by aspergillus terreus CCMI 498 and trichoderma viride CCMI 84 for enzymatic deinking of mixed office wastepaper
title_fullStr Characterisation and application of glycanases secreted by aspergillus terreus CCMI 498 and trichoderma viride CCMI 84 for enzymatic deinking of mixed office wastepaper
title_full_unstemmed Characterisation and application of glycanases secreted by aspergillus terreus CCMI 498 and trichoderma viride CCMI 84 for enzymatic deinking of mixed office wastepaper
title_sort Characterisation and application of glycanases secreted by aspergillus terreus CCMI 498 and trichoderma viride CCMI 84 for enzymatic deinking of mixed office wastepaper
author Marques, S.
author_facet Marques, S.
Pala, H.
Alves, L.
Amaral-Collaço, M. T.
Gama, F. M.
Gírio, F. M.
author_role author
author2 Pala, H.
Alves, L.
Amaral-Collaço, M. T.
Gama, F. M.
Gírio, F. M.
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Marques, S.
Pala, H.
Alves, L.
Amaral-Collaço, M. T.
Gama, F. M.
Gírio, F. M.
dc.subject.por.fl_str_mv Hemicellulase
Endoglucanase
Amylase
Enzymatic deinking
Aspergillus terreus
Trichoderma viride
Science & Technology
topic Hemicellulase
Endoglucanase
Amylase
Enzymatic deinking
Aspergillus terreus
Trichoderma viride
Science & Technology
description Two enzymatic extracts obtained from xylan-grown Aspergillus terreus CCMI 498 and cellulose-grown Trichoderma viride CCMI 84 were characterised for different glycanase activities. Both strains produce extracellular endoxylanase and endoglucanase enzymes. The enzymes optimal activity was found in the temperature range of 45-60 ºC. Endoglucanase systems show identical activity profiles towards temperature, regardless of the strain and inducing substrate. Conversely, the endoxylanases produced by both strains showed maximal activity at different pH values (from 4.5 to 5.5), being the more acidic xylanase produced by T. viride grown on cellulose. The endoglucanase activities have an optimum pH at 4.5-5.0. The endoxylanase and endoglucanase activities exhibited high stability at 50 ºC and pH 5.0. Mannanase, β-xylosidase, and amylase activities were also found, being the first two activities only present for T. viride extract. These two enzymatic extracts were used for mixed office wastepaper (MOW) deinking. When the enzymatic extract from T. viride was used, a further increase of 24% in ink removal was obtained by comparison with the control. Both enzymes contributed to the improvement of the paper strength properties and the obtained results clearly indicate that the effective use of enzymes for deinking can also contribute to the pulp and paper properties improvement.
publishDate 2003
dc.date.none.fl_str_mv 2003
2003-01-01T00:00:00Z
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/1822/1485
url https://hdl.handle.net/1822/1485
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Marques, S., Pala, H., Alves, L., Amaral-Collaço, M. T., Gama, F. M., & Gı́rio, F. M. (2003, February). Characterisation and application of glycanases secreted by Aspergillus terreus CCMI 498 and Trichoderma viride CCMI 84 for enzymatic deinking of mixed office wastepaper. Journal of Biotechnology. Elsevier BV. http://doi.org/10.1016/s0168-1656(02)00247-x
0168-1656
10.1016/S0168-1656(02)00247-X
12443852
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 Science
publisher.none.fl_str_mv Elsevier Science
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
_version_ 1799132623987015680