cellulosilyticum ruminicola gen. nov., sp. nov., isolated from the rumen of yak, and reclassification of clostridium lentocellum as cellulosilyticum lentocellum comb. nov. | an obligate anaerobic, gram-staining-negative, mesophilic, cellulolytic bacterium, strain h1(t), was isolated from the rumen content of yak. cells were straight to slightly curved rods, 0.8-1.0 x 3.0-4.0 microm in size, non-motile and encapsulated with mucous materials. elliptical and terminal spores that swelled the cells were produced occasionally. the strain grew at 25-45 degrees c (optimum, 38 degrees c) and ph 6.0-7.8 (optimum, ph 6.7). cellulose, cellobiose, xylan, xylose and maltose were ... | 2010 | 19661493 |
cellulosilyticum ruminicola, a newly described rumen bacterium that possesses redundant fibrolytic-protein-encoding genes and degrades lignocellulose with multiple carbohydrate- borne fibrolytic enzymes. | cellulosilyticum ruminicola h1 is a newly described bacterium isolated from yak (bos grunniens) rumen and is characterized by its ability to grow on a variety of hemicelluloses and degrade cellulosic materials. in this study, we performed the whole-genome sequencing of c. ruminicola h1 and observed a comprehensive set of genes encoding the enzymes essential for hydrolyzing plant cell wall. the corresponding enzymatic activities were also determined in strain h1; these included endoglucanases, ce ... | 2010 | 20400560 |
cbm3d, a novel sub-family of family 3 carbohydrate binding module identified in cel48a exoglucanase of cellulosilyticum ruminicola. | previously, we found that exoglucanase cel48a from cellulosilyticum ruminicola h1 bound intensively to avicel; however, no known carbohydrate binding module (cbm) was observed in the protein. bioinformatics suggested that a c-terminal fragment of 127 amino acids, named the cellulosilyticum-specific paralogous module (cpm), could function for binding. cpm-appended proteins are all putative (hemi)cellulases from cellulosilyticum spp. in the present work, we demonstrated that cel48a without the cpm ... | 2011 | 21803997 |
three feruloyl esterases in cellulosilyticum ruminocola h1 act synergistically to hydrolyze esterified polysaccharides. | feruloyl esterases (faes) constitute a subclass of carboxyl esterases that specially hydrolyze the ester linkages between ferulate and polysaccharides in plant cell walls. until now, the described microbial faes were mainly from fungi. in this study, we reported that cellulosilyticum ruminocola h1, a previously described fibrolytic rumen bacterium, possesses three differing active feruloyl esterases, faei, faeii, and faeiii. phylogenetic analysis classified the described bacterial faes into two ... | 2011 | 21764976 |
[cell density mediated cellulases synthesis in cellulosilyticum ruminicola]. | cellulosilyticum ruminicola h1 is an anaerobic cellulolytic bacterium isolated from the rumen content of yak. previously, we found that strain h1 lost growth on filter paper cellulose after several subcultures. the growth on cellulose cannot be restored until a few transfers in the cellobiose-containing medium. this is contrary to the knowledge that microbial cellulases synthesis is induced by the substrate while repressed by the metabolites, e. g. cellobiose, but provides a hint of cell-density ... | 2012 | 23236840 |