SPECIFIC INTERACTION ACTING AT A CELLULOSE-BINDING DOMAIN/CELLULOSE INTERFACE FOR PAPERMAKING APPLICATION

Specific and strong cellulose-binding characteristics were utilized for promoting retention of additives in contaminated papermaking systems. Cellulose-binding domain (CBD) of cellulase derived from Trichoderma viride was separated by digestion with papain, and then introduced into anionic polyacry...

Full description

Bibliographic Details
Main Authors: Shingo Yokota, Kumiko Matsuo, Takuya Kitaoka, Hiroyuki Wariishi
Format: Article
Language:English
Published: North Carolina State University 2008-11-01
Series:BioResources
Subjects:
Online Access:http://ojs.cnr.ncsu.edu/index.php/BioRes/article/viewFile/BioRes_03_4_1030_Yokota_MKW_Cellulose_Binding_Domain_Cellulose_Interface/255
id doaj-b334ad60c29246c79e6d09a396e9fc58
record_format Article
spelling doaj-b334ad60c29246c79e6d09a396e9fc582020-11-25T00:54:35ZengNorth Carolina State UniversityBioResources1930-21262008-11-013410301041SPECIFIC INTERACTION ACTING AT A CELLULOSE-BINDING DOMAIN/CELLULOSE INTERFACE FOR PAPERMAKING APPLICATIONShingo YokotaKumiko MatsuoTakuya KitaokaHiroyuki WariishiSpecific and strong cellulose-binding characteristics were utilized for promoting retention of additives in contaminated papermaking systems. Cellulose-binding domain (CBD) of cellulase derived from Trichoderma viride was separated by digestion with papain, and then introduced into anionic polyacrylamide (A-PAM) through a condensation reaction using water-soluble carbodiimide. The CBD-modified A-PAM (CBD-A-PAM) showed good retention on pulp fibers, resulting in high tensile strength paper sheets. The effect remained almost unchanged in the presence of model interfering substances such as ligninsulfonate and Ca2+ ions, whereas commercial cationic paper-strengthening polymer became ineffective. The cellulose-binding force of CBD was quantitatively determined by atomic force microscopy (AFM) in the liquid state. Histidine-tagged CBD protein was obtained using Escherichia coli via an expression of CBD derived from Cellulomonas fimi, and immobilized on a gold-coated AFM probe. A strong attractive force was detected only at a CBD/cellulose interface, even when Ca2+ ions were present in high concentration. Direct estimation of CBD affinity for cellulose substrate by AFM would provide significant information on the interfacial interactions useful for the functional design of papermaking additives.http://ojs.cnr.ncsu.edu/index.php/BioRes/article/viewFile/BioRes_03_4_1030_Yokota_MKW_Cellulose_Binding_Domain_Cellulose_Interface/255Cellulose-binding domainRetentionPapermaking additiveInterfering substancesAtomic force microscopyForce curve measurement
collection DOAJ
language English
format Article
sources DOAJ
author Shingo Yokota
Kumiko Matsuo
Takuya Kitaoka
Hiroyuki Wariishi
spellingShingle Shingo Yokota
Kumiko Matsuo
Takuya Kitaoka
Hiroyuki Wariishi
SPECIFIC INTERACTION ACTING AT A CELLULOSE-BINDING DOMAIN/CELLULOSE INTERFACE FOR PAPERMAKING APPLICATION
BioResources
Cellulose-binding domain
Retention
Papermaking additive
Interfering substances
Atomic force microscopy
Force curve measurement
author_facet Shingo Yokota
Kumiko Matsuo
Takuya Kitaoka
Hiroyuki Wariishi
author_sort Shingo Yokota
title SPECIFIC INTERACTION ACTING AT A CELLULOSE-BINDING DOMAIN/CELLULOSE INTERFACE FOR PAPERMAKING APPLICATION
title_short SPECIFIC INTERACTION ACTING AT A CELLULOSE-BINDING DOMAIN/CELLULOSE INTERFACE FOR PAPERMAKING APPLICATION
title_full SPECIFIC INTERACTION ACTING AT A CELLULOSE-BINDING DOMAIN/CELLULOSE INTERFACE FOR PAPERMAKING APPLICATION
title_fullStr SPECIFIC INTERACTION ACTING AT A CELLULOSE-BINDING DOMAIN/CELLULOSE INTERFACE FOR PAPERMAKING APPLICATION
title_full_unstemmed SPECIFIC INTERACTION ACTING AT A CELLULOSE-BINDING DOMAIN/CELLULOSE INTERFACE FOR PAPERMAKING APPLICATION
title_sort specific interaction acting at a cellulose-binding domain/cellulose interface for papermaking application
publisher North Carolina State University
series BioResources
issn 1930-2126
publishDate 2008-11-01
description Specific and strong cellulose-binding characteristics were utilized for promoting retention of additives in contaminated papermaking systems. Cellulose-binding domain (CBD) of cellulase derived from Trichoderma viride was separated by digestion with papain, and then introduced into anionic polyacrylamide (A-PAM) through a condensation reaction using water-soluble carbodiimide. The CBD-modified A-PAM (CBD-A-PAM) showed good retention on pulp fibers, resulting in high tensile strength paper sheets. The effect remained almost unchanged in the presence of model interfering substances such as ligninsulfonate and Ca2+ ions, whereas commercial cationic paper-strengthening polymer became ineffective. The cellulose-binding force of CBD was quantitatively determined by atomic force microscopy (AFM) in the liquid state. Histidine-tagged CBD protein was obtained using Escherichia coli via an expression of CBD derived from Cellulomonas fimi, and immobilized on a gold-coated AFM probe. A strong attractive force was detected only at a CBD/cellulose interface, even when Ca2+ ions were present in high concentration. Direct estimation of CBD affinity for cellulose substrate by AFM would provide significant information on the interfacial interactions useful for the functional design of papermaking additives.
topic Cellulose-binding domain
Retention
Papermaking additive
Interfering substances
Atomic force microscopy
Force curve measurement
url http://ojs.cnr.ncsu.edu/index.php/BioRes/article/viewFile/BioRes_03_4_1030_Yokota_MKW_Cellulose_Binding_Domain_Cellulose_Interface/255
work_keys_str_mv AT shingoyokota specificinteractionactingatacellulosebindingdomaincelluloseinterfaceforpapermakingapplication
AT kumikomatsuo specificinteractionactingatacellulosebindingdomaincelluloseinterfaceforpapermakingapplication
AT takuyakitaoka specificinteractionactingatacellulosebindingdomaincelluloseinterfaceforpapermakingapplication
AT hiroyukiwariishi specificinteractionactingatacellulosebindingdomaincelluloseinterfaceforpapermakingapplication
_version_ 1725233632641024000