Journal
PROTEIN SCIENCE
Volume 20, Issue 9, Pages 1479-1483Publisher
WILEY-BLACKWELL
DOI: 10.1002/pro.689
Keywords
CBM33; cellulose oxidation; GH61; cellulose degradation
Categories
Funding
- VISTA Program [6505]
- Norwegian Research Council [190965/S60190877/S60196885/F20]
Ask authors/readers for more resources
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
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available