Elsevier

Journal of Biotechnology

Volume 57, Issues 1–3, 16 September 1997, Pages 15-28
Journal of Biotechnology

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The roles and function of cellulose-binding domains

https://doi.org/10.1016/S0168-1656(97)00087-4Get rights and content

Abstract

Most cellulolytic enzymes consist of distinct catalytic and cellulose-binding domains (CBDs). Similar domain structures are also found in enzymes degrading other insoluble carbohydrates such as raw starch and chitin. Such binding domains improve the binding and facilitate the activity of the catalytic domain on the insoluble but not on soluble substrates. Based on their amino acid sequence similarities, the CBDs have been divided into several different families. Structure determination and subsequent mutagenesis studies have revealed that CBDs rely on several aromatic amino acids for binding to the cellulose surfaces. The CBDs binding to crystalline cellulose have different topologies but share similar rigid backbone structures for correct positioning of the side chains required for the substrate recognition and binding. CBDs represent ideal affinity tags for specific immobilisation of various other proteins to cellulose. Furthermore, improved understanding and control of their action will be important for the improvement of the biotechnological value of cellulolytic enzymes.

References (119)

  • N.R. Gilkes et al.

    Precise excision of the cellulose binding domains from two Cellulomonas fimi cellulases by a homologous protease and the effect on catalysis

    J. Biol. Chem.

    (1988)
  • N.R. Gilkes et al.

    The adsorption of a bacterial cellulase and its two isolated domains to crystalline cellulose

    J. Biol. Chem.

    (1992)
  • N.R. Gilkes et al.

    Visualisation of the adsorption of a endo-β -1,4-glucanase and its isolated cellulose-binding domain to crystalline cellulose

    Int. J. Biol. Macromol.

    (1993)
  • J.M. Greenwood et al.

    Fusion to an endoglucanase allows alkaline phosphatase to bind to cellulose

    FEBS Lett.

    (1989)
  • B. Henrissat et al.

    Possible adsorption sites of cellulases on crystallline cellulose

    FEBS Lett.

    (1988)
  • L.S. Jackson et al.

    Enzyme recovery from secondary fiber treated with cellulase and xylanase

    J. Biotechnol.

    (1996)
  • J. Knowles et al.

    Cellulase families and their genes

    Trends Biotechnol.

    (1987)
  • M.L. Langsford et al.

    Glycosylation of bacterial cellulases prevents proteolytic cleavage between functional domains

    FEBS Lett.

    (1987)
  • M. Linder et al.

    The difference in affinity between two fungal cellulose-binding domains is dominated by a single amino acid substitution

    FEBS Lett.

    (1995)
  • M. Linder et al.

    Characterisation of a double cellulose-binding domain: synergistic high-affinity binding to cellulose

    J. Biol. Chem.

    (1996)
  • A. Meinke et al.

    Enhancement of the endo-β-1,4-glucanase activity of an exocellobiohydrolase by deletion of a surface loop

    J. Biol. Chem.

    (1995)
  • E. Ong et al.

    The cellulose-binding domains of cellulases: tools for biotechnology

    Trends. Biotechnol.

    (1989)
  • E. Ong et al.

    Enzyme immobilisation using a cellulose-binding domain: properties of a β-glucosidase fusion protein

    Enzyme Microb. Technol.

    (1991)
  • T. Reinikainen et al.

    Comparison of the adsorption properties of a single-chain antibody fragment fused to a fungal or a bacterial cellulose-binding domain

    Enzyme Microb. Technol.

    (1997)
  • M. Saloheimo et al.

    EGIII, a new endoglucanase from Trichoderma reesei: characterisation of both the gene and enzyme

    Gene

    (1988)
  • H. Shen et al.

    Deletion of the linker connecting the catalytic and cellulose-binding domains of endoglucanase A (CenA) of Cellulomonas fimi alters its conformation and catalytic activity

    J. Biol. Chem.

    (1991)
  • V. Sild et al.

    Effect of potential binding site overlap to binding of cellulase to cellulose: a two-dimensional simulation

    FEBS Lett.

    (1996)
  • M. Sogaard et al.

    Site-directed mutagenesis of histidine 93, aspartic acid 180, glutamic acid 205, and aspartic acid 291 at the active site and tryptophan 279 at the raw starch binding site in barley α-amylasel

    J. Biol. Chem.

    (1993)
  • M. Srisodsuk et al.

    Role of the interdomain linker peptide of Trichoderma reesei cellobiohydrolase I in its interaction with crystalline cellulose

    J. Biol. Chem.

    (1993)
  • J. Ståhlberg et al.

    Trichoderma reesei has no true exo-cellulase: all intact and truncated cellulases produce new reducing end groups on cellulose

    Biochim. Biopys. Acta

    (1993)
  • P.M. Abuja et al.

    Structural and functional domains of cellobiohydrolase I from Trichoderma reesei

    Eur. Biophys. J.

    (1988)
  • R.H. Atalla

    The structures of native cellulose

  • E.A. Bayer et al.

    The cellulosome: A cell surface organelle for the adhesion to and degradation of cellulose

  • G. Beldman et al.

    Adsorption and kinetic behavior of purified endoglucanases and exoglucanases from Trichoderma viride

    Biotechnol. Bioeng.

    (1987)
  • P. Birch et al.

    Substrate-dependant differential splicing of introns in the regions encoding the cellulose binding domains of two exocellobiohydrolase I-like genes in Phanerochaete chrysosporium

    Appl. Environ. Microbiol.

    (1995)
  • H. Blaak et al.

    Binding and substrate specificities of a Streptomyces olivaceoviridis chitinase in comparison with its proteolytically processed form

    Eur. J. Biochem.

    (1995)
  • G. Black et al.

    A modular xylanase containing a novel non-catalytic xylan-specific binding domain

    Biochem. J.

    (1995)
  • M.R. Bray et al.

    Probing the role of tryptophan residues in a cellulose-binding domain by chemical modification

    Protein Sci.

    (1996)
  • E. Brun et al.

    Overproduction, purification and characterisation of the cellulosebinding domain of the Erwinia chrysamthemi secreted endoglucanase EGZ

    Eur. J. Biochem.

    (1995)
  • H. Chanzy

    Aspects of cellulose structure

  • J.B. Coutinho et al.

    The binding of Cellulomonas fimi endoglucanase C (CenC) to cellulose and Sephadex is mediated by the N-terminal repeats

    Mol. Microbiol.

    (1992)
  • J.B. Coutinho et al.

    The nature of the cellulose-binding domain affects the activities of a bacterial endoglucanase on different forms of cellulose

    FEMS Microbiol. Lett.

    (1993)
  • J.B. Coutinho et al.

    Structure-function relationships in the catalytic and starch binding domains of glucoamylase

    Protein. Eng.

    (1994)
  • A.L. Creagh et al.

    Binding of the cellulose-binding domain of exoglucanase Cex from Cellulomonas fimi to insoluble microcrystalline cellulose is entropically driven

  • M.J. Daniels

    Using biological enzymes for papermaking

    Paper Technol.

    (1992)
  • S. Denman et al.

    Characterisation of a Neocallimastix patriciarum cellulase cDNA (CelA) homologous to Trichoderma reesei cellobiohydrolase II

    Appl. Environ. Microbiol.

    (1996)
  • R. Dijkerman et al.

    Adsorption characteristics of cellulolytic enzymes from the anaerobic fungus Piromyces sp. strain E2 on microcrystalline cellulose

    Appl. Environ. Microbiol.

    (1996)
  • N. Din et al.

    The cellulose-binding domain of endoglucanase A (CenA) from Cellulomonas fimi: evidence for the involvement of tryptophan residues in binding

    Mol. Microbiol.

    (1994)
  • N. Din et al.

    Cl-Cx revisited: intramolecular synergism in a cellulase

  • C. Divne et al.

    The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei

    Science

    (1994)
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    Present address: Kungliga Tekniska Högskolan, Department of Biochemistry and Biotechnology; S-10044 Stockholm, Sweden.

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