Cargando…

Cellulases adsorb reversibly on biomass lignin

Adsorption of cellulases onto lignin is considered a major factor in retarding enzymatic cellulose degradation of lignocellulosic biomass. However, the adsorption mechanisms and kinetics are not well understood for individual types of cellulases. This study examines the binding affinity, kinetics of...

Descripción completa

Detalles Bibliográficos
Autores principales: Djajadi, Demi T., Pihlajaniemi, Ville, Rahikainen, Jenni, Kruus, Kristiina, Meyer, Anne S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6282830/
https://www.ncbi.nlm.nih.gov/pubmed/30132790
http://dx.doi.org/10.1002/bit.26820
_version_ 1783379074902654976
author Djajadi, Demi T.
Pihlajaniemi, Ville
Rahikainen, Jenni
Kruus, Kristiina
Meyer, Anne S.
author_facet Djajadi, Demi T.
Pihlajaniemi, Ville
Rahikainen, Jenni
Kruus, Kristiina
Meyer, Anne S.
author_sort Djajadi, Demi T.
collection PubMed
description Adsorption of cellulases onto lignin is considered a major factor in retarding enzymatic cellulose degradation of lignocellulosic biomass. However, the adsorption mechanisms and kinetics are not well understood for individual types of cellulases. This study examines the binding affinity, kinetics of adsorption, and competition of four monocomponent cellulases of Trichoderma reesei during adsorption onto lignin. TrCel7A, TrCel6A, TrCel7B, and TrCel5A were radiolabeled for adsorption experiments on lignin‐rich residues (LRRs) isolated from hydrothermally pretreated spruce (L‐HPS) and wheat straw (L‐HPWS), respectively. On the basis of adsorption isotherms fitted to the Langmuir model, the ranking of binding affinities was TrCel5A >  TrCel6A >  TrCel7B >  TrCel7A on both types of LRRs. The enzymes had a higher affinity to the L‐HPS than to the L‐HPWS. Adsorption experiments with dilution after 1 and 24 hr and kinetic modeling were performed to quantify any irreversible binding over time. Models with reversible binding parameters fitted well and can explain the results obtained. The adsorption constants obtained from the reversible models agreed with the fitted Langmuir isotherms and suggested that reversible adsorption–desorption existed at equilibrium. Competitive binding experiments showed that individual types of cellulases competed for binding sites on the lignin and the adsorption data fitted the Langmuir adsorption model. Overall, the data strongly indicate that the adsorption of cellulases onto lignin is reversible and the findings have implications for the development of more efficient cellulose degrading enzymes.
format Online
Article
Text
id pubmed-6282830
institution National Center for Biotechnology Information
language English
publishDate 2018
publisher John Wiley and Sons Inc.
record_format MEDLINE/PubMed
spelling pubmed-62828302018-12-11 Cellulases adsorb reversibly on biomass lignin Djajadi, Demi T. Pihlajaniemi, Ville Rahikainen, Jenni Kruus, Kristiina Meyer, Anne S. Biotechnol Bioeng ARTICLES Adsorption of cellulases onto lignin is considered a major factor in retarding enzymatic cellulose degradation of lignocellulosic biomass. However, the adsorption mechanisms and kinetics are not well understood for individual types of cellulases. This study examines the binding affinity, kinetics of adsorption, and competition of four monocomponent cellulases of Trichoderma reesei during adsorption onto lignin. TrCel7A, TrCel6A, TrCel7B, and TrCel5A were radiolabeled for adsorption experiments on lignin‐rich residues (LRRs) isolated from hydrothermally pretreated spruce (L‐HPS) and wheat straw (L‐HPWS), respectively. On the basis of adsorption isotherms fitted to the Langmuir model, the ranking of binding affinities was TrCel5A >  TrCel6A >  TrCel7B >  TrCel7A on both types of LRRs. The enzymes had a higher affinity to the L‐HPS than to the L‐HPWS. Adsorption experiments with dilution after 1 and 24 hr and kinetic modeling were performed to quantify any irreversible binding over time. Models with reversible binding parameters fitted well and can explain the results obtained. The adsorption constants obtained from the reversible models agreed with the fitted Langmuir isotherms and suggested that reversible adsorption–desorption existed at equilibrium. Competitive binding experiments showed that individual types of cellulases competed for binding sites on the lignin and the adsorption data fitted the Langmuir adsorption model. Overall, the data strongly indicate that the adsorption of cellulases onto lignin is reversible and the findings have implications for the development of more efficient cellulose degrading enzymes. John Wiley and Sons Inc. 2018-10-16 2018-12 /pmc/articles/PMC6282830/ /pubmed/30132790 http://dx.doi.org/10.1002/bit.26820 Text en © 2018 The Authors. Biotechnology and Bioengineering Published by Wiley Periodicals, Inc. This is an open access article under the terms of the http://creativecommons.org/licenses/by-n/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes.
spellingShingle ARTICLES
Djajadi, Demi T.
Pihlajaniemi, Ville
Rahikainen, Jenni
Kruus, Kristiina
Meyer, Anne S.
Cellulases adsorb reversibly on biomass lignin
title Cellulases adsorb reversibly on biomass lignin
title_full Cellulases adsorb reversibly on biomass lignin
title_fullStr Cellulases adsorb reversibly on biomass lignin
title_full_unstemmed Cellulases adsorb reversibly on biomass lignin
title_short Cellulases adsorb reversibly on biomass lignin
title_sort cellulases adsorb reversibly on biomass lignin
topic ARTICLES
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6282830/
https://www.ncbi.nlm.nih.gov/pubmed/30132790
http://dx.doi.org/10.1002/bit.26820
work_keys_str_mv AT djajadidemit cellulasesadsorbreversiblyonbiomasslignin
AT pihlajaniemiville cellulasesadsorbreversiblyonbiomasslignin
AT rahikainenjenni cellulasesadsorbreversiblyonbiomasslignin
AT kruuskristiina cellulasesadsorbreversiblyonbiomasslignin
AT meyerannes cellulasesadsorbreversiblyonbiomasslignin