Proteomic analysis of the cellulose bound fraction of the
crude extracellular enzyme revealed a multi-species lignocellulolytic
enzyme system composed mainly of extracellular glycosyl
hydrolases and cellulosomal components in different glycosyl
hydrolase families, including scaffolding proteins and cellulolytic/
hemicellulolytic modules closely related to those described
from Clostridium josui [26] and Clostridium cellulyticum [27–29]
(Table 4). Hemicellulase enzymes were also identified, including
a glycosyl hydrolase family 10 (xylanase) closely related to
a cell-bound multi-domain xylanase from C. josui [30] and -
l-arabinofuranosidase from Thermobacillus xylanolyticus [31]. An
endo--1,3-1,4-glucanase similar to the Bacillus amyloliquefaciensrelated
synthetic construct [32] was also identified. The result thus
revealed a multi-species enzyme system composed of lignocellulolytic
enzymes from anaerobic and facultative anaerobic bacteria
working cooperatively on degradation of cellulosic substrates in
the system.