Application of new oxidoreductases in bleaching of kraft pulp

Bibliographic Details
Main Author: Silva, Andreia de Freitas
Publication Date: 2014
Format: Master thesis
Language: eng
Source: Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
Download full: http://hdl.handle.net/10773/14266
Summary: Pulp bleaching is one of the most important and expensive processes in the pulp and paper industry. Along the years this technology has gone through several changes in order to reduce the ecological risks and the production costs. The aim of this work is to study the application of a new oxidoreductase, produced by Novozymes A/S, in ECF and TCF bleaching of oxygen pre-bleached Eucalyptus kraft pulp and then to compare the bleaching performance of this enzyme with other oxidoreductases already studied or commercialized by the company. The oxidoreductase used in this study was primarily the NS-51002 laccase (and its variants) of which culture broths were purified. The laccase-mediator system and the incubation conditions were optimized. Then the NS-51002 laccase bleaching performance was compared with other enzymes like Novozym 51003 laccase and NS-51004 and NS-51113 peroxidases. The best enzyme proved to be the NS-51113 peroxidase, which was also optimized in terms of application conditions. Besides the enzymatic stages, the dosage of chemical used in the alkaline extraction stage was also optimized. Afterwards, the NS-51002 laccase and the NS-51113 peroxidase were implemented in several ECF and TCF bleaching sequences. To study the effect of the enzymes and chemicals on bleaching a number of properties were measured in different parts of the sequence, such as: ISO brightness; kappa number; hexenuronic acid content; viscosity; pH, residual hydrogen peroxide and COD in the pulp filtrates. Using the sequence DEpDP (90,5%) as reference, it was concluded that the implementation of an enzymatic stage with xylanase in the beginning of the sequence, i.e. XDEpDP (91,1%), enhanced the pulp brightness. Furthermore, some sequences using the NS-51113 peroxidase as the L stage proved to be quite effective from the bleaching point of view, allowing to reach 90±0,5 of ISO brightness, in particular the sequence XLEpDP (89,5%).
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spelling Application of new oxidoreductases in bleaching of kraft pulpEngenharia químicaPasta de papel kraft - BranqueamentoLacasePeroxidaseEnzimasPulp bleaching is one of the most important and expensive processes in the pulp and paper industry. Along the years this technology has gone through several changes in order to reduce the ecological risks and the production costs. The aim of this work is to study the application of a new oxidoreductase, produced by Novozymes A/S, in ECF and TCF bleaching of oxygen pre-bleached Eucalyptus kraft pulp and then to compare the bleaching performance of this enzyme with other oxidoreductases already studied or commercialized by the company. The oxidoreductase used in this study was primarily the NS-51002 laccase (and its variants) of which culture broths were purified. The laccase-mediator system and the incubation conditions were optimized. Then the NS-51002 laccase bleaching performance was compared with other enzymes like Novozym 51003 laccase and NS-51004 and NS-51113 peroxidases. The best enzyme proved to be the NS-51113 peroxidase, which was also optimized in terms of application conditions. Besides the enzymatic stages, the dosage of chemical used in the alkaline extraction stage was also optimized. Afterwards, the NS-51002 laccase and the NS-51113 peroxidase were implemented in several ECF and TCF bleaching sequences. To study the effect of the enzymes and chemicals on bleaching a number of properties were measured in different parts of the sequence, such as: ISO brightness; kappa number; hexenuronic acid content; viscosity; pH, residual hydrogen peroxide and COD in the pulp filtrates. Using the sequence DEpDP (90,5%) as reference, it was concluded that the implementation of an enzymatic stage with xylanase in the beginning of the sequence, i.e. XDEpDP (91,1%), enhanced the pulp brightness. Furthermore, some sequences using the NS-51113 peroxidase as the L stage proved to be quite effective from the bleaching point of view, allowing to reach 90±0,5 of ISO brightness, in particular the sequence XLEpDP (89,5%).O branqueamento da pasta de papel é um dos processos mais importantes e dispendiosos da indústria da pasta e papel. Ao longo dos anos esta tecnologia atravessou várias alterações no sentido de reduzir os riscos ecológicos e os custos de produção. O objetivo deste trabalho é efetuar um estudo sobre a aplicação de uma nova oxidorredutase, produzida pela Novozymes A/S, em branqueamento ECF e TCF usando pasta kraft de Eucalyptus pré-branqueada com oxigénio e, posteriormente comparar o desempenho desta enzima com o de outras oxidorredutases já estudadas ou comercializadas pela empresa. A oxidorredutase usada neste estudo foi primeiramente a lacase NS-51002 (e as suas variantes), cujo meio de cultura foi purificado. O sistema lacase-mediador e as condições de incubação foram otimizados. De seguida, o desempenho da lacase NS-51002 no branqueamento foi comparado com o de outras enzimas, tais como a lacase Novozym 51003 e as peroxidases NS-51004 e NS-51113. A peroxidase NS-51113 demonstrou ser a melhor enzima, assim sendo também foi otimizada em termos de condições de aplicação. Para além dos estágios enzimáticos, também foi otimizado a carga de químicos do estágio de extração alcalina. Seguidamente, a lacase NS-51002 e a peroxidase NS-51113 peroxidase foram implementadas em várias sequências de branqueamento ECF e TCF. De modo a estudar o efeito das enzimas e químicos no branqueamento, foram determinadas algumas propriedades em diferentes partes da sequência, tais como: brancura ISO; número kappa; teor de ácidos hexenuronicos; viscosidade; pH, teor residual de peróxido de hidrogénio e CQO nos filtrados da pasta. Usando a sequência DEpDP (90,5%) como referência, foi possível concluir que a implementação de um estágio enzimático com xilanase no início da sequência, i.e. XDEpDP (91,1%), aumentou a brancura da pasta. Além disso, algumas sequências que usam a peroxidase NS-51113 como estágio L provaram ser bastante eficazes sob o ponto de vista do branqueamento, permitindo alcançar uma brancura ISO de 90±0,5, em particular a sequência XLEpDP (89,5%).Universidade de Aveiro2018-07-20T14:00:49Z2014-11-28T00:00:00Z2014-11-282016-11-28T14:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesisapplication/pdfhttp://hdl.handle.net/10773/14266TID:201565978engSilva, Andreia de Freitasinfo:eu-repo/semantics/openAccessreponame:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiainstacron:RCAAP2024-05-06T03:54:17Zoai:ria.ua.pt:10773/14266Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireinfo@rcaap.ptopendoar:https://opendoar.ac.uk/repository/71602025-05-28T13:50:18.523765Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiafalse
dc.title.none.fl_str_mv Application of new oxidoreductases in bleaching of kraft pulp
title Application of new oxidoreductases in bleaching of kraft pulp
spellingShingle Application of new oxidoreductases in bleaching of kraft pulp
Silva, Andreia de Freitas
Engenharia química
Pasta de papel kraft - Branqueamento
Lacase
Peroxidase
Enzimas
title_short Application of new oxidoreductases in bleaching of kraft pulp
title_full Application of new oxidoreductases in bleaching of kraft pulp
title_fullStr Application of new oxidoreductases in bleaching of kraft pulp
title_full_unstemmed Application of new oxidoreductases in bleaching of kraft pulp
title_sort Application of new oxidoreductases in bleaching of kraft pulp
author Silva, Andreia de Freitas
author_facet Silva, Andreia de Freitas
author_role author
dc.contributor.author.fl_str_mv Silva, Andreia de Freitas
dc.subject.por.fl_str_mv Engenharia química
Pasta de papel kraft - Branqueamento
Lacase
Peroxidase
Enzimas
topic Engenharia química
Pasta de papel kraft - Branqueamento
Lacase
Peroxidase
Enzimas
description Pulp bleaching is one of the most important and expensive processes in the pulp and paper industry. Along the years this technology has gone through several changes in order to reduce the ecological risks and the production costs. The aim of this work is to study the application of a new oxidoreductase, produced by Novozymes A/S, in ECF and TCF bleaching of oxygen pre-bleached Eucalyptus kraft pulp and then to compare the bleaching performance of this enzyme with other oxidoreductases already studied or commercialized by the company. The oxidoreductase used in this study was primarily the NS-51002 laccase (and its variants) of which culture broths were purified. The laccase-mediator system and the incubation conditions were optimized. Then the NS-51002 laccase bleaching performance was compared with other enzymes like Novozym 51003 laccase and NS-51004 and NS-51113 peroxidases. The best enzyme proved to be the NS-51113 peroxidase, which was also optimized in terms of application conditions. Besides the enzymatic stages, the dosage of chemical used in the alkaline extraction stage was also optimized. Afterwards, the NS-51002 laccase and the NS-51113 peroxidase were implemented in several ECF and TCF bleaching sequences. To study the effect of the enzymes and chemicals on bleaching a number of properties were measured in different parts of the sequence, such as: ISO brightness; kappa number; hexenuronic acid content; viscosity; pH, residual hydrogen peroxide and COD in the pulp filtrates. Using the sequence DEpDP (90,5%) as reference, it was concluded that the implementation of an enzymatic stage with xylanase in the beginning of the sequence, i.e. XDEpDP (91,1%), enhanced the pulp brightness. Furthermore, some sequences using the NS-51113 peroxidase as the L stage proved to be quite effective from the bleaching point of view, allowing to reach 90±0,5 of ISO brightness, in particular the sequence XLEpDP (89,5%).
publishDate 2014
dc.date.none.fl_str_mv 2014-11-28T00:00:00Z
2014-11-28
2016-11-28T14:00:00Z
2018-07-20T14:00:49Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
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dc.identifier.uri.fl_str_mv http://hdl.handle.net/10773/14266
TID:201565978
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dc.publisher.none.fl_str_mv Universidade de Aveiro
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