Specific Interaction Acting at a Cellulose-binding Domain/cellulose Interface for Papermaking Application
نویسندگان
چکیده
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 Ca 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 Ca 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.
منابع مشابه
KORRIGAN1 Interacts Specifically with Integral Components of the Cellulose Synthase Machinery
Cellulose is synthesized by the so called rosette protein complex and the catalytic subunits of this complex are the cellulose synthases (CESAs). It is thought that the rosette complexes in the primary and secondary cell walls each contains at least three different non-redundant cellulose synthases. In addition to the CESA proteins, cellulose biosynthesis almost certainly requires the action of...
متن کاملAtomic force microscopy study of cellulose surface interaction controlled by cellulose binding domains.
Colloidal probe microscopy has been used to study the interaction between model cellulose surfaces and the role of cellulose binding domain (CBD), peptides specifically binding to cellulose, in interfacial interaction of cellulose surfaces modified with CBDs. The interaction between pure cellulose surfaces in aqueous electrolyte solution is dominated by double layer repulsive forces with the ra...
متن کاملCrystal structure of a bacterial family-III cellulose-binding domain: a general mechanism for attachment to cellulose.
The crystal structure of a family-III cellulose-binding domain (CBD) from the cellulosomal scaffoldin subunit of Clostridium thermocellum has been determined at 1.75 A resolution. The protein forms a nine-stranded beta sandwich with a jelly roll topology and binds a calcium ion. conserved, surface-exposed residues map into two defined surfaces located on opposite sides of the molecule. One of t...
متن کاملMatrix-assisted refolding of single-chain Fv- cellulose binding domain fusion proteins.
We describe a method for the isolation of recombinant single-chain antibodies in a biologically active form. The single-chain antibodies are fused to a cellulose binding domain as a single-chain protein that accumulates as insoluble inclusion bodies upon expression in Escherichia coli. The inclusion bodies are then solubilized and denatured by an appropriate chaotropic solvent, then reversibly ...
متن کاملCharacterization of the cellulose-binding domain of the Clostridium cellulovorans cellulose-binding protein A.
Cellulose-binding protein A (CbpA), a component of the cellulase complex of Clostridium cellulovorans, contains a unique sequence which has been demonstrated to be a cellulose-binding domain (CBD). The DNA coding for this putative CBD was subcloned into pET-8c, an Escherichia coli expression vector. The protein produced under the direction of the recombinant plasmid, pET-CBD, had a high affinit...
متن کامل