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Enzyme immobilization using the cellulose-binding domain of a Cellulomonas fimi exoglucanase

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TLDR
It is believed that the cellulose-binding domain (CBDCex) of Cex offers a simple, inexpensive and widely applicable method of enzyme immobilization.
Abstract
We have constructed a fusion between the gene (abg) for a β-glucosidase (Abg) of an Agrobacterium sp. and part of the gene (cex) for an exoglucanase (Cex) of Cellulomonas fimi. The abg-cex fusion encodes a fusion protein (Abg-CBDCex) with the cellulose-binding properties of Cex and β-glucosidase activity of Abg. The fusion protein retained 42 percent of its β-glucosidase activity when bound to cellulose. The binding was stable enough to allow continuous hydrolysis of substrate by the enzyme without detectable leaching of the enzyme from the cellulose. We believe that the cellulose-binding domain (CBDCex) of Cex offers a simple, inexpensive and widely applicable method of enzyme immobilization.

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Cellulases and related enzymes in biotechnology

TL;DR: The present article is an overview of the biotechnological state-of-the-art for cellulases and related enzymes.
Journal ArticleDOI

The biological degradation of cellulose

TL;DR: The study of cellulolytic enzymes at the molecular level has revealed some of the features that contribute to their activity and an increasing number of three-dimensional structures are becoming available for cellulases and xylanases belonging to different families, which will provide paradigms for molecular modeling of related enzymes.
Journal ArticleDOI

Strategies for achieving high-level expression of genes in Escherichia coli.

TL;DR: Progress in the understanding of several biological processes promises to broaden the usefulness of Escherichia coli as a tool for gene expression and the remarkable increase in the availability of fusion partners offers a wide range of tools for improved protein folding, solubility, protection from proteases, yield, and secretion into the culture medium.
Journal ArticleDOI

Cellulose degrading enzymes and their potential industrial applications.

TL;DR: This review summarizes the present state of knowledge on microbial cellulases and their applications and concludes that the tremendous commercial potential of cellulase components remains the driving force for research in this area.
Journal ArticleDOI

Why are ruminal cellulolytic bacteria unable to digest cellulose at low pH

TL;DR: In this paper, gene reconstruction offers a means of converting Prevotella ruminicola into a ruminal bacterium that can digest cellulose at low pH and degrades the cellulose derivative, carboxymethylcellulose.
References
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Journal ArticleDOI

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Book

Molecular Cloning: A Laboratory Manual

TL;DR: Molecular Cloning has served as the foundation of technical expertise in labs worldwide for 30 years as mentioned in this paper and has been so popular, or so influential, that no other manual has been more widely used and influential.
Journal Article

Cleavage of structural proteins during the assemble of the head of bacterio-phage T4

U. K. Laemmli
- 01 Jan 1970 - 
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
Journal ArticleDOI

DNA sequencing with chain-terminating inhibitors

TL;DR: A new method for determining nucleotide sequences in DNA is described, which makes use of the 2',3'-dideoxy and arabinon nucleoside analogues of the normal deoxynucleoside triphosphates, which act as specific chain-terminating inhibitors of DNA polymerase.
Book

Antibodies: A Laboratory Manual

Ed Harlow, +1 more
TL;DR: A second edition of Antibodies: A Laboratory Manual is being published in September 2013, Revised, extended and updated by Edward Greenfield of the Dana-Farber Cancer Center, the material has been recast with extensive new information and new chapters have been added.
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