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Carbohydrate-binding modules recognize fine substructures of cellulose

TitleCarbohydrate-binding modules recognize fine substructures of cellulose
Publication TypeJournal Article
Year of Publication2002
AuthorsMcLean, BW, Boraston, AB, Brouwer, D, Sanaie, N, Fyfe, CA, Warren, RAJ, Kilburn, DG, Haynes, CA
JournalJournal of Biological Chemistry
Volume277
Pagination50245-50254
Date PublishedDec
Type of ArticleArticle
ISBN Number0021-9258
KeywordsBACTERIAL, CELLULASE, CRYSTALLINE CELLULOSE, DOMAIN, EXOGLUCANASE, FIMI CENC, NMR-SPECTROSCOPY, PROTEIN-A, SPECIFICITY, TRYPTOPHAN RESIDUES, XYLANASE 10A
Abstract

Competition isotherms are used to identify the set of cellulose substructures to which cellulose binding modules (CBMs) from families 2a, 3, 4, 9, and 17 bind. The experiments are based on coupling a unique fluorescent tag to each CBM in a manner that does not alter the natural binding properties of the CBM and therefore allows the surface and solution concentrations of each CBM to be monitored as a function of time and composition. Adsorption and surface exchange of like or competing CBMs are monitored using a range of cellulose preparations varying in both crystallinity and provenance. CBMs from families 2a, 3,4,9, and 17 are shown to recognize different physical forms of prepared cellulose. The demonstration of the very fine binding specificity of cellulose-specific CBMs implies that the polysaccharide targets of CBMs extend down to the resolution of cellulose microstructures.

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