Characterization of EngF from Clostridium cellulovorans and identification of a novel cellulose binding domain

Article Abstract:

The noncellulosomal endoglucanase F (EngF) from Clostridium cellulovorans contains cellulose binding domains (CBDs), with some or all of the highly conserved C-terminal sequences comprising a new type of CBD family. This was concluded in a study of the physical and enzymatic properties of EngF. According to results of binding studies, the K(sub D) and the maximum amount of protein bound for acid-swollen cellulose were 1.8 micron and 7.1 (mu)mol/g of cellulose, respectively. Binding site is between amino acid residues 356 and 557.

Research, Analysis, Binding sites (Biochemistry), Active sites (Biochemistry)

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Isolation and characterization of Clostridium butyricum DSM 5431 mutants with increased resistance to 1,3-propanediol and altered production of acids

Article Abstract:

Isolated Clostridium butyricum DSM 5431 mutants have increased resistance to glycerol and 1,3-propanediol (1,3-PD) and produce more biomass compared to the wild type. The wild-type strain produces more acid than the mutant strain and releases more acetic acid than butyrate. In contrast to the wild type, the mutants use more NADH to form 1,3-PD. The mutant strains have low levels of hydrogenase and NADH-ferrodoxin activities and an increased level of ferrodoxin-NAD+ reductase activity.

Mutation (Biology), Mutation, Acetic acid

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Characteristics of a new cellulolytic Clostridium sp. isolated from pig intestinal tract

Article Abstract:

Two out of six pigs fed and rectally infused with Clostrdium longisporum yielded fecal samples containing a new species of Clostridium. This isolate had very different phenotypic characteristics from C. longisporum, and it was not known whether the initial inoculum was a contributing factor in its occurence or establishment. The new isolate, designated Clostridium sp strain 54408, was able to degrade the cell calls of alfalfa, bromegrass and switchgrass.

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