title: The cellulosome--a treasure-trove for biotechnology.
abstract: The cellulases of many cellulolytic bacteria are organized into discrete multienzyme complexes, called cellulosomes. The multiple subunits of cellulosomes are composed of numerous functional domains, which interact with each other and with the cellulosic substrate. One of these subunits comprises a distinctive new class of noncatalytic scaffolding polypeptide, which selectively integrates the various cellulase and xylanase subunits into the cohesive complex. Intelligent application of cellulosome hybrids and chimeric constructs of cellulosomal domains should enable better use of cellulosic biomass and may offer a wide range of novel applications in research, medicine and industry.
authors.affiliation: Department of Biophysics, Weizmann Institute of Science, Rehovot, Israel.
authors.forename: E A
authors.initials: EA
authors.lastname: Bayer
authors.forename: E
authors.initials: E
authors.lastname: Morag
authors.forename: R
authors.initials: R
authors.lastname: Lamed
mesh_terms: D001419:Bacteria / Q000201:enzymology; D001709:Biotechnology; D002480:Cellulase / Q000737:chemistry / Q000378:metabolism; D002482:Cellulose / Q000378:metabolism; D005658:Fungi / Q000201:enzymology; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000378:metabolism; D008031:Lignin / Q000378:metabolism; D009097:Multienzyme Complexes / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D043325:Xylan Endo-1,3-beta-Xylosidase
chemical_list: D009097:Multienzyme Complexes; C036909:lignocellulose; D002482:Cellulose; D008031:Lignin; D006026:Glycoside Hydrolases; D043325:Xylan Endo-1,3-beta-Xylosidase; D002480:Cellulase