What is "cellulosome"

n. (context enzyme English) A complex of enzymes that degrade the polysaccharide surface of cells and mediate cell attachment

Cellulosomes are multi-enzyme complexes. The cellulosomes are associated with the cell surface and mediate cell attachment to the insoluble substrate and degrade it to soluble products which are then absorbed. Cellulosome complexes are intricate multi-enzyme machines produced by many cellulolytic microorganisms (cellulosome producing bacteria are listed below). They are designed by the microorganisms for efficient degradation of plant cell wall polysaccharides, notably cellulose—the most abundant organic polymer on Earth. 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, a large glycoprotein, which we called "scaffoldin", comprises a distinctive new class of non-catalytic scaffolding polypeptide. The scaffoldin subunit selectively integrates the various cellulases and xylanase subunits into the cohesive complex, by combining its "cohesin" domains with a typical "dockerin" domain present on each of the subunit enzymes. The scaffoldin of some cellulosomes, an example being that of C. thermocellum, contains a carbohydrate-binding module that adheres cellulose to the cellulosomal complex.

Cellulosomes exist as extracellular complexes that are either attached to the cell wall of bacteria or free in solution, where the insoluble substrate can be broken down into soluble products and taken up by the cell. The large size and heterogeneity of cellulosomes from the best-characterized organisms (i.e., C. thermocellum, C. cellulolyticum, and C. cellulovorans) have greatly complicated efforts to probe cellulosome structure and function. Other cellulosome systems (such as those from Acetivibrio cellulolyticus and Ruminococcus flavefaciens) appear to be even more intricate.

The cellulosome consists of a multi-functional integrating subunit (called scaffoldin), responsible for organizing the various cellulolytic subunits (e.g., the enzymes) into the complex. Within a cellulosome, multiple endoglucanases, cellobiohydrolases, xylanases and other degradative enzymes work synergistically to attack heterogeneous, insoluble cellulose substrates. This is accomplished by the interaction of two complementary classes of module, located on the two separate types of interacting subunits, i.e., a cohesin module on the scaffoldin and a dockerin module on each enzymatic subunit. The high-affinity cohesin-dockerin interaction defines the cellulosome structure. Attachment of the cellulosome to its substrate is mediated by a scaffoldin-borne cellulose-binding module (CBM) that comprises part of the scaffoldin subunit. Much of our understanding of its catalytic components, architecture, and mechanisms of attachment to the bacterial cell and to cellulose, has been derived from the study of Clostridium thermocellum.

Applications: Intelligent application of cellulosome hybrids and chimeric constructs ("nanosomes") of cellulosomal domains should enable better use of cellulosic biomass and may offer a wide range of novel applications.