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Examinando por Autor "Eyzaguirre, J."

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    The endoxylanases from family 11: Computer analysis of protein sequences reveals important structural and phylogenetic relationships
    (Elsevier, 2002-03) Sapag, A.; Wouters, J.; Lambert, C.; De Ioannes, P.; Eyzaguirre, J.; Depiereux, E.
    Eighty-two amino acid sequences of the catalytic domains of mature endoxylanases belonging to family 11 have been aligned using the programs MATCHBOX and CLUSTAL. The sequences range in length from 175 to 233 residues. The two glutamates acting as catalytic residues are conserved in all sequences. A very good correlation is found between the presence (at position 100) of an asparagine in the so-called 'alkaline' xylanases, or an aspartic acid in those with a more acidic pH optimum. Four boxes defining segments of highest similarity were detected; they correspond to regions of defined secondary structure: B5, B6, B8 and the carboxyl end of the alpha helix, respectively. Cysteine residues are not common in these sequences (0.7% of all residues), and disulfide bridges are not important in explaining the stability of several thermophilic xylanases. The alignment allows the classification of the enzymes in groups according to sequence similarity. Fungal and bacterial enzymes were found to form mostly separate clusters of higher similarity.
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    The xylanolytic enzyme system from the genus Penicillium
    (Elsevier, 2006-06) Chavez, R.; Bull, P.; Eyzaguirre, J.
    In nature, there are numerous microorganisms that efficiently degrade xylan, a major component of lignocellulose. In particular, filamentous fungi have demonstrated a great capability for secreting a wide range of xylanases, being the genus Aspergillus and Trichoderma the most extensively studied and reviewed among the xylan-producing fungi. However, an important amount of information about the production and genetics of xylanases from fungi of the genus Penicillium has accumulated in recent years. A great number of Penicillia are active producers of xylanolytic enzymes, and the use of xylanases from these species has acquired growing importance in biotechnological applications. This review summarizes our current knowledge about the properties, genetics, expression and biotechnological potential of xylanases from the genus Penicillium.