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The zygomycete fungus  Lichtheimia ramosa  H71D, isolated from sugarcane bagasse compost, was identified by applying phylogenetic analysis based on the DNA sequence of the Internal Transcribed Spacer (ITS), and subsequent secondary structure analysis of ITS2.  L. ramosa  H71D was able to grow over a wide range of temperatures (25–45 °C), manifesting optimal growth at 37 °C. A 64 kDa xylanase (named  Lr XynA) was purified from the culture supernatant of  L. ramosa  H71D grown on 2% carboxymethylcellulose (CMC), as the only carbon source.  Lr XynA displayed optimal activity at pH 6 and temperature of 65 °C. The enzyme retained more than 50% of its maximal activity over a broad range of pH values (4.5–7.5). Enzyme half-life (t ½ ) times at 55, 65 and 75 °C were 80, 25, and 8 min, respectively.  Lr XynA showed higher affinity ( k    M   of 2.87 mg/mL) and catalytic efficiency ( k    cat  / k    M   of 0.651 mg s/mL) towards Beechwood xylan in comparison to other substrates such as Birchwood xylan, Oat-spelt xylan, CMC, Avicel and Solka floc. The predominant final products from  Lr XynA-mediated hydrolysis of Beechwood xylan were xylobiose and xylotriose, suggesting that the enzyme is an endo-β-1,4 xylanase. Scanning electron microscopy (SEM) imaging of sugar cane bagasse (SCB) treated with  Lr XynA, alone or in combination with commercial cellulases, showed a positive effect on the hydrolysis of SCB. To our knowledge, this is the first report focusing on the biochemical and functional characterization of an endo-β-1,4 xylanase from the thermotolerant and fast-growing fungus  Lichtheimia ramosa.

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Taxonomic identification of the thermotolerant and fast-growing fungus Lichtheimia ramosa H71D and biochemical characterization of the thermophilic xylanase LrXynA