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Adsorption of proteins involved in hydrolysis of lignocellulose on lignins and hemicelluloses.

Identifieur interne : 002805 ( Main/Exploration ); précédent : 002804; suivant : 002806

Adsorption of proteins involved in hydrolysis of lignocellulose on lignins and hemicelluloses.

Auteurs : Nidhi Pareek [Suède] ; Thomas Gillgren ; Leif J. Jönsson

Source :

RBID : pubmed:24045193

Descripteurs français

English descriptors

Abstract

Protein adsorption onto eight lignocellulosic substances (six lignin preparations and two hemicelluloses) was investigated at pH 4.8 and at two different temperatures (4°C and 45°C). The kinetics of the adsorption of cellulase, xylanase, and β-glucosidase were determined by enzyme activity measurements. The maximum adsorption capacities, the affinity constants and the binding strengths varied widely and were typically higher for the lignins than for the carbohydrates. As indicated by BET and gel permeation chromatography, different substances had widely different surface area, pore size, weight average molecular weight, and polydispersity index, but these properties were difficult to relate to protein binding. In most cases, an increase in temperature from 4°C to 45°C and a low content of carboxylic acid groups, as indicated by Fourier-Transform Infra-Red (FTIR) spectroscopy, resulted in increased protein adsorption capacity, which suggests that hydrophobic interactions play an important role.

DOI: 10.1016/j.biortech.2013.08.121
PubMed: 24045193


Affiliations:


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<nlm:affiliation>Department of Chemistry, Umeå University, SE-901 87 Umeå, Sweden.</nlm:affiliation>
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<term>Adsorption (MeSH)</term>
<term>Cellulase (metabolism)</term>
<term>Chromatography, Gel (MeSH)</term>
<term>Endo-1,4-beta Xylanases (metabolism)</term>
<term>Fagus (chemistry)</term>
<term>Hydrolysis (MeSH)</term>
<term>Kinetics (MeSH)</term>
<term>Lignin (metabolism)</term>
<term>Molecular Weight (MeSH)</term>
<term>Picea (chemistry)</term>
<term>Polysaccharides (metabolism)</term>
<term>Populus (chemistry)</term>
<term>Porosity (MeSH)</term>
<term>Proteins (metabolism)</term>
<term>Spectroscopy, Fourier Transform Infrared (MeSH)</term>
<term>Temperature (MeSH)</term>
<term>Time Factors (MeSH)</term>
<term>beta-Glucosidase (metabolism)</term>
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<keywords scheme="KwdFr" xml:lang="fr">
<term>Adsorption (MeSH)</term>
<term>Cellulase (métabolisme)</term>
<term>Chromatographie sur gel (MeSH)</term>
<term>Cinétique (MeSH)</term>
<term>Endo-1,4-beta xylanases (métabolisme)</term>
<term>Facteurs temps (MeSH)</term>
<term>Fagus (composition chimique)</term>
<term>Hydrolyse (MeSH)</term>
<term>Lignine (métabolisme)</term>
<term>Masse moléculaire (MeSH)</term>
<term>Picea (composition chimique)</term>
<term>Polyosides (métabolisme)</term>
<term>Populus (composition chimique)</term>
<term>Porosité (MeSH)</term>
<term>Protéines (métabolisme)</term>
<term>Spectroscopie infrarouge à transformée de Fourier (MeSH)</term>
<term>Température (MeSH)</term>
<term>bêta-Glucosidase (métabolisme)</term>
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<term>Cellulase</term>
<term>Endo-1,4-beta Xylanases</term>
<term>Lignin</term>
<term>Polysaccharides</term>
<term>Proteins</term>
<term>beta-Glucosidase</term>
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<term>Populus</term>
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<term>Populus</term>
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<term>Cellulase</term>
<term>Endo-1,4-beta xylanases</term>
<term>Lignine</term>
<term>Polyosides</term>
<term>Protéines</term>
<term>bêta-Glucosidase</term>
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<term>Adsorption</term>
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<term>Hydrolysis</term>
<term>Kinetics</term>
<term>Molecular Weight</term>
<term>Porosity</term>
<term>Spectroscopy, Fourier Transform Infrared</term>
<term>Temperature</term>
<term>Time Factors</term>
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<term>Adsorption</term>
<term>Chromatographie sur gel</term>
<term>Cinétique</term>
<term>Facteurs temps</term>
<term>Hydrolyse</term>
<term>Masse moléculaire</term>
<term>Porosité</term>
<term>Spectroscopie infrarouge à transformée de Fourier</term>
<term>Température</term>
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<front>
<div type="abstract" xml:lang="en">Protein adsorption onto eight lignocellulosic substances (six lignin preparations and two hemicelluloses) was investigated at pH 4.8 and at two different temperatures (4°C and 45°C). The kinetics of the adsorption of cellulase, xylanase, and β-glucosidase were determined by enzyme activity measurements. The maximum adsorption capacities, the affinity constants and the binding strengths varied widely and were typically higher for the lignins than for the carbohydrates. As indicated by BET and gel permeation chromatography, different substances had widely different surface area, pore size, weight average molecular weight, and polydispersity index, but these properties were difficult to relate to protein binding. In most cases, an increase in temperature from 4°C to 45°C and a low content of carboxylic acid groups, as indicated by Fourier-Transform Infra-Red (FTIR) spectroscopy, resulted in increased protein adsorption capacity, which suggests that hydrophobic interactions play an important role. </div>
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<Title>Bioresource technology</Title>
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<AbstractText>Protein adsorption onto eight lignocellulosic substances (six lignin preparations and two hemicelluloses) was investigated at pH 4.8 and at two different temperatures (4°C and 45°C). The kinetics of the adsorption of cellulase, xylanase, and β-glucosidase were determined by enzyme activity measurements. The maximum adsorption capacities, the affinity constants and the binding strengths varied widely and were typically higher for the lignins than for the carbohydrates. As indicated by BET and gel permeation chromatography, different substances had widely different surface area, pore size, weight average molecular weight, and polydispersity index, but these properties were difficult to relate to protein binding. In most cases, an increase in temperature from 4°C to 45°C and a low content of carboxylic acid groups, as indicated by Fourier-Transform Infra-Red (FTIR) spectroscopy, resulted in increased protein adsorption capacity, which suggests that hydrophobic interactions play an important role. </AbstractText>
<CopyrightInformation>Copyright © 2013 The Authors. Published by Elsevier Ltd.. All rights reserved.</CopyrightInformation>
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<Keyword MajorTopicYN="N">Protein adsorption</Keyword>
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