Article Abstract:
The highly active xylanase (XynA) signal peptide of the fungus Aureobasidium pullulans is an efficient posttranslational processor of the xynA product and helps in the secretion of xylanase in Saccharomyces cerevisiae. The peptide is about three times more effective than the S. cerevisiae invertase or mating alpha-factor pheromone. XynA increases the efficiency of secretion while transcription and translation are unaffected. The S. cerevisiae clones with cDNA and genomic DNA have no activity in culture media and a little xylanase activity in cell-associated fractions.
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Article Abstract:
The cellulases and xylanases of the polycentric anaerobic fungus, Orpinomyces strain PC-2, are 80 to 85% identical to the corresponding enzymes of the monocentric anaerobic fungus, Neocallimastix patriciarum. The enzymes contain a catalytic as well as a noncatalytic repeated peptide domain. The Orpinomyces xylanase consists of one catalytic domain, whereas the N. xylanase contains two similar catalytic domains. Antibodies against the catalytic region react with both the Orpinomyces and N. patriciarum xylanases.
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Article Abstract:
A 1,067-bp cDNA, called AxeA, from Orpinomyces sp strain PC-2 was cloned, sequenced, purified and characterized. The gene contained an open reading frame of 939 bp encoding a polypeptide of 313 amino acid residues having a calculated mass of 34,845 Da. The enzyme lacked a noncatalytic repeated peptide domain found at the carboxy terminus of at the Neocallimastix BnaA. Results reveal that AxeA and BnaA may represent a new family of hydrolases.
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