Studies on the rumen flagellate Neocallimastix frontalis.

Cloning, sequencing, and expression of an endoglucanase gene from the rumen anaerobic fungus Neocallimastix frontalis MCH3.

A cDNA clone encoding an endo-1,4-beta-glucanase from a rumen fungus, Neocallimastix frontalis MCH3, was isolated. The nucleotide sequence showed that the gene, celA, encoded a multidomain enzyme containing a family 5 catalytic domain and a reiterated sequence that is involved in the association of a multienzyme complex, the cellulosome. The enzyme expressed in Escherichia coli showed the highe...

The rumen flagellate Callimastix frontalis: does sequestration occur?

Distribution of radioactivity of 14C-amino acids added to the medium in cells and metabolites in cultures of rumen fungi.

A mixture of L-(U-14C) amino acids was added to cultures of 11 strains of rumen anaerobic fungi belonging to Neocallimastix frontalis, Neocallimastix joyonii, Sphaeromonas communis and Piromonas communis. Fungi were grown in a complex medium with glucose for 4 days. The radioactivity was found in cellular protein (27.7-65.3% of the total radioactivity recovered), lactate (16.9-41.8%), volatile ...

Characterization of Heterologously Expressed Acetyl Xylan Esterase1 Isolated from the Anaerobic Rumen Fungus Neocallimastix frontalis PMA02

Acetyl xylan esterase (AXE), which hydrolyzes the ester linkages of the naturally acetylated xylan and thus known to have an important role for hemicellulose degradation, was isolated from the anaerobic rumen fungus Neocallimastix frontatlis PMA02, heterologously expressed in Escherichi coli (E.coli) and characterized. The full-length cDNA encoding NfAXE1 was 1,494 bp, of which 978 bp constitut...

Purification and characterization of two 1,4-beta-xylan endohydrolases from the rumen fungus Neocallimastix frontalis.

Two beta-endoxylanases produced by Neocallimastix frontalis have been purified by ammonium sulfate precipitation, gel filtration, and ion-exchange chromatography. Xylanase I is a nonglycosylated protein with an apparent molecular mass of 45 kDa. Xylanase II is a glycoprotein with an apparent molecular mass of 70 kDa. The pH optima of these enzymes were 5.5 and 6, respectively, and the temperatu...