Lecanicillium muscarium CCFEE 5003, isolated in Continental Antarctica, is a powerful producer of extracellular cold-tolerant enzymes. Chitin-hydrolyzing enzymes seems to be the principal extracellular catalytic activities of this psychrotolerant fungus. The production of chitinolytic activities is induced by chitin and other polysaccharides and is submitted to catabolite repression. The chitinolytic system of L. muscarium consists of a number of different proteins having various molecular weights and diverse biochemical characteristics, but their most significant trait is the marked cold-tolerance. L. muscarium and selected strains of the biocontrol agent of pathogenic fungi Trichoderma harzianum, have been compared for their ability to produce chitinolytic enzymes at different temperatures. At low temperatures the Antarctic strain was definitely much more efficient. Moreover, the fungus was able to exert a strong mycoparasitic action against various other fungi and oomycetes at low temperatures. The parasitic role of this organism appeared related to the production of cell wall degrading enzymes being the release of extracellular chitinolytic enzymes a key event in the mycoparasitic process. Due to the mentioned characteristics, L. muscarium could have an important role for potential applications such as the degradation of chitin-rich materials at low temperature and the biocontrol of pathogenic organisms in cold environments. For these reasons and in view of future industrial application, the production of chitinolytic enzymes by the Antarctic fungus has been up-scaled and optimised in bench-top bioreactor.
Keywords: Continental Antarctica; Lecanicillium muscarium; chitinolytic enzymes; cold-tolerant enzymes.