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A Biological Nanomachine at Work: Watching the Cellulosome Degrade Crystalline Cellulose
Author(s) -
Manuel Eibinger,
Thomas Ganner,
Harald Plank,
Bernd Nidetzky
Publication year - 2020
Publication title -
acs central science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.893
H-Index - 76
eISSN - 2374-7951
pISSN - 2374-7943
DOI - 10.1021/acscentsci.0c00050
Subject(s) - cellulosome , cellulase , clostridium thermocellum , cellulose , bioconversion , cellulosic ethanol , substrate (aquarium) , chemistry , supramolecular chemistry , nanotechnology , materials science , chemical engineering , biochemistry , organic chemistry , molecule , biology , ecology , fermentation , engineering
The cellulosome is a supramolecular multienzymatic protein complex that functions as a biological nanomachine of cellulosic biomass degradation. How the megadalton-size cellulosome adapts to a solid substrate is central to its mechanism of action and is also key for its efficient use in bioconversion applications. We report time-lapse visualization of crystalline cellulose degradation by individual cellulosomes from Clostridium thermocellum by atomic force microscopy. Upon binding to cellulose, the cellulosomes switch to elongated, even filamentous shapes and morph these dynamically at below 1 min time scale according to requirements of the substrate surface under attack. Compared with noncomplexed cellulases that peel off material while sliding along crystalline cellulose surfaces, the cellulosomes remain bound locally for minutes and remove the material lying underneath. The consequent roughening up of the surface leads to an efficient deconstruction of cellulose nanocrystals both from the ends and through fissions within. Distinct modes of cellulose nanocrystal deconstruction by nature's major cellulase systems are thus revealed.

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