Revealing Nature’s Cellulase Diversity: The Digestion Mechanism of Caldicellulosiruptor bescii CelA-Reference-Cited by-同舟云学术

Revealing Nature’s Cellulase Diversity: The Digestion Mechanism of Caldicellulosiruptor bescii CelA

Published:2013-12-20 Issue:6165 Volume:342 Page:1513-1516
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Brunecky Roman¹,Alahuhta Markus¹,Xu Qi¹,Donohoe Bryon S.¹,Crowley Michael F.¹,Kataeva Irina A.²,Yang Sung-Jae²,Resch Michael G.¹,Adams Michael W. W.²,Lunin Vladimir V.¹,Himmel Michael E.¹,Bomble Yannick J.¹

Affiliation:

1. Biosciences Center, National Renewable Energy Laboratory, 15013 Denver West Parkway, Golden, CO 80401, USA.

2. Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA.

Abstract

An Enzyme Drill Cellulase enzymes degrade the cell walls of plants by breaking down cellulose into its constituent sugar fragments and thus have attracted interest for biofuels production. Using transmission electron microscopy Brunecky et al. (p. 1513 ; see the Perspective by

Berlin

) discovered that an especially active cellulase, CelA, from Caldicellulosiruptor bescii bacteria does not move along the surface of the substrate, but drills into the cellulose to form cavities.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference35 articles.

1. Genome sequencing and analysis of the biomass-degrading fungus Trichoderma reesei (syn. Hypocrea jecorina)

2. The Cellulosomes: Multienzyme Machines for Degradation of Plant Cell Wall Polysaccharides

3. Cellulosomes: plant-cell-wall-degrading enzyme complexes

4. Genome Sequence of the Anaerobic, Thermophilic, and Cellulolytic Bacterium “ Anaerocellum thermophilum ” DSM 6725

5. Use of Label-Free Quantitative Proteomics To Distinguish the Secreted Cellulolytic Systems of Caldicellulosiruptor bescii and Caldicellulosiruptor obsidiansis

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