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Author(s)
Basidiomycetes are able to biodegrade waste and
xenobiotic molecules through the production of extracellular enzymes.
For example, white-rot fungi produce lignin-degrading enzymes which are
capable of efficiently decolorizing dye solutions. Many mushrooms also
produce lectins, a group of proteins which bind specifically to the
carbohydrates in glycoconjugates. Several fungal lectins target their
specificities towards oligosaccharides present in mammalian
glycoproteins, thus constituting excellent ligands for the preparation
of affinity adsorbents useful in isolation and characterization of these
glycoproteins. In this study we isolated and characterized two
different proteins, a lectin and a laccase, present in extracts from Punctularia atropurpurascens.
The lectin isolated from the mycelium extract, was immobilized on
activated-Sepharose and used to evaluate the interaction with three
glycoproteins. The adsorbent was able to efficiently adsorb and elute
bovine lactoferrin, constituting a promising tool for the purification
of this glycoprotein. In vitro experiments revealed that the lectin also
exhibited antimicrobial activity against Aspergillus niger. Laccase activity was detected in the extracellular extract from P. atropurpurascens.
This enzyme, in both soluble and immobilized forms, was able to degrade
Remazol Brilliant Blue R and Acid Blue 25 dyes. The biological
activities found in this fungus demonstrate its potential for various
biotechnological applications.
KEYWORDS
Cite this paper
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