title: Cleavage of cellulose by a CBM33 protein.
abstract: Bacterial proteins categorized as family 33 carbohydrate-binding modules (CBM33) were recently shown to cleave crystalline chitin, using a mechanism that involves hydrolysis and oxidation. We show here that some members of the CBM33 family cleave crystalline cellulose as demonstrated by chromatographic and mass spectrometric analyses of soluble products released from Avicel or filter paper on incubation with CelS2, a CBM33-containing protein from Streptomyces coelicolor A3(2). These enzymes act synergistically with cellulases and may thus become important tools for efficient conversion of lignocellulosic biomass. Fungal proteins classified as glycoside hydrolase family 61 that are known to act synergistically with cellulases are likely to use a similar mechanism.
authors: Department of Chemistry Biotechnology and Food Science, Norwegian University of Life Sciences, Aas, Norway.
authors: Zarah
authors: Z
authors: Forsberg
authors: Gustav
authors: G
authors: Vaaje-Kolstad
authors: Bjørge
authors: B
authors: Westereng
authors: Anne C
authors: AC
authors: Bunæs
authors: Yngve
authors: Y
authors: Stenstrøm
authors: Alasdair
authors: A
authors: MacKenzie
authors: Morten
authors: M
authors: Sørlie
authors: Svein J
authors: SJ
authors: Horn
authors: Vincent G H
authors: VG
authors: Eijsink
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism*; D044602:Cellulases / Q000378:metabolism; D002482:Cellulose / Q000378:metabolism*; D005656:Fungal Proteins / Q000378:metabolism; D048372:Streptomyces coelicolor / Q000201:enzymology
chemical_list: D001426:Bacterial Proteins; D005656:Fungal Proteins; D002482:Cellulose; D044602:Cellulases