Record number :
Title of article :
Cloning, characterisation and expression analysis of α-glucuronidase from the thermophilic fungus Talaromyces emersonii
Author/Authors :
M.N. Heneghan، نويسنده , , L. McLoughlin، نويسنده , , P.G. Murray، نويسنده , , M.G. Tuohy، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2007
Pages :
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Abstract :
The aguA gene encoding α-glucuronidase was isolated from the thermophilic fungus Talaromyces emersonii by degenerate PCR. AguA has no introns and consists of an open reading frame of 2511 bp, encoding a putative protein of 837 amino acids. The N-terminus of the protein contains a putative signal peptide of 17 amino acids yielding a mature protein of 820 amino acids with a predicted molecular mass of 91.6 kDa. Twenty putative N-glycosylation sites and four O-glycosylation were identified. The T. emersonii α-glucuronidase falls into glycosyl hydrolase family 67, showing approximately 63% identity to similar enzymes from other fungi. Analysis of the aguA promoter revealed several possible regulatory motifs including two XlnR and a CreA binding site. Enzyme activity was optimal at 50 °C and pH 5. Enzyme production was investigated on a range of carbon sources and showed induction on beechwood, oat spelt and birchwood xylan, and repression by glucose or glucuronic acid.
Keywords :
Talaromyces emersonii , ?-Glucuronidase , Hemicellulase , Glycosyl hydrolase
Journal title :
Enzyme and Microbial Technology
Link To Document :