Purification, characterization, and mode of action of endoxylanases 1 and 2 from Fibrobacter succigenes S85

Article Abstract:

Two endoxylynases (1, 4-beta-D-xylanohydrolases) from Fibrobacter succinogenees S85 were purified and characterized. The enzymes were grown on crystalline cellulose and purified to apparent electrophoretic homogeneity by column chromatography. Results showed that endoxylanase 1 was a basic protein of 53.7 kDa and exhibited arabinose-debranching activity. On the other hand, endoxylanase 2 with 66. kDa showed xyland-hydrolyzing activity and significant activity towards carboxymethyl cellulose. Both enzymes were observed to have important functions in in vivo plant cell digestion by F. succinogenes.

Bacteria

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A cold-active glucanase from the ruminal bacterium Fibrobacter succinogenes S85

Article Abstract:

The influence of temperature on the enzymatic activity, thermal stability and structure of the CelG enzyme from the mesophilic anaerobe Fibrobacter succinogenes S85 has been studied. F. succinogenes S85 is one of the major cellulolytic organisms in the rumen but none of its cellulases has been described as cold-active so far. Results of comparative experiments reveal that CelG is a cold-active enzyme with superior catalytic properties. It has a lower temperature optimum of 25 degrees C and retains 70% of its maximum activity at 0 degrees C.

Gram-negative bacteria, Bacterial genetics, Anaerobic bacteria

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Catalytic properties of the cellulose-binding endoglucanase F from Fibrobacter succinogenes S85

Article Abstract:

The celF gene from the predominant cellulolytic ruminal bacterium Fibrobacter succinogenes encodes a 118.3-kDa cellulose-binding endoglucanase called endoglucanase F (EGF). This enzyme has an N-terminal cellulose-binding domain and a C-terminal catalytic domain. The purified catalytic domain exhibits an activity profile typical of an endoglucanase with highly catalytic activity on carboxymethyl cellulose and barley beta-glucan.

Cellulose

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