Degradation of microcrystalline cellulose: Synergism between different endoglucanases of Cellulomonas sp. ATCC 21399

Abstract

Three immunologically and enzymatically distinct endoglucanases of Cellulomonas sp. ATCC 21399 were purified previously. Endoglucanase A and endoglucanase B acted synergistically on microcrystalline cellulose (Avicel), whereas no synergistic action was observed between endoglucanase A and endoglucanase C or between endoglucanase B or endoglucanase C. Only endoglucanase A was capable of hydrolyzing Avicel when acting alone and this enzyme resulted in "short fiber formation" when acting on Avicel. The end product of hydrolysis of acid swollen Avicel produced by the three endoglucanases was in all cases dominated by cellobiose and showed lower content of glucose and cellotriose. Higher cellodextrins appeared as transient end products. The results indicate that the function of endoglucanase A in the cellulase system of Cellulomonas might be very similar to the function of the cellobiohydrolases of Trichoderma reesei.

The Complete Genome of Teredinibacter turnerae T7901: An Intracellular Endosymbiont of Marine Wood-Boring Bivalves (Shipworms)

“…For example, endoglucanases and cellobiohydrolases are thought to display synergism because the former produces substrate (reducing ends) that can be degraded by the latter. Indeed, such synergism has been observed between naturally co-occurring endoglucanases and exoglucanases or accessory enzymes such as cellodextrinases and cellobiases in Fibrobacter [29], Clostridium [30], Cellulomonas [31] and fungi [32]. Moreover, cellulases and cellulase complexes (synthetic cellulosomes) engineered to contain multiple enzymatic specificities also display synergistic activity against cellulose [33] and complex plant substrates [34], [35].…”

Synergistic interactions among ?-laminarinase, ?-1,4-glucanase, and ?-glucosidase from the hyperthermophilic archaeonPyrococcus furiosus during hydrolysis of ?-1,4-, ?-1,3-, and mixed-linked polysaccharides

“…Thus far, numerous cellulose degradation studies have been done to elucidate the nature of the endoglucanase (endo)/exoglucanase (exo), endo/endo, and exo/ exo cellulase interactions (Ashadi et al, 1996;Baker et al, 1995;Irwin et al, 1993;Nidetzky et al, 1994Nidetzky et al, , 1995Philippidis et al, 1993;Poulsen and Petersen, 1992;Rouland et al, 1988;Stalbrand et al, 1998). Glycosyl hydrolases degrading noncellulosic substrates, such as ␤-1,3-glucanases and chitinases, have also been examined for their capacity to work in a concerted manner to function as fungicides (Mauch et al, 1988;Jongedijk et al, 1995;Schirmböck et al, 1994;Strittmatter and Wegener, 1993).…”

Rationale for Particle Size Effect on Rates of Enzymatic Saccharification of Microcrystalline Cellulose

“…One aspect of concern with regard to any "standard" substrate is the extent and consequence of variations among different preparations. This is a particularly interesting question with reference to the average particle size of MCC substrates, since preparations differing with respect to particle size are commercially available and widely used (Tomme et al 1990;Poulsen and Petersen 1992;Medve et al 1994;Penner and Liaw 1994;Bothwell et ai. 1997) without reference to this parameter.…”