José M. Lora

TL;DR: Three proteins which display chitinase activity were purified from the supernatants of Trichoderma harzianum CECT 2413 grown in minimal medium supplemented with Chitin as the sole carbon source, suggesting that each protein is encoded by a different gene.

TL;DR: A cDNA of Trichoderma harzianum (chit42), coding for an endochitinase of 42 kDa, has been cloned using synthetic oligonucleotides corresponding to aminoacid sequences of the purified chit inase, revealing post-translational processing of a putative signal peptide and a second peptide of 12 amino acids.

TL;DR: A gene (chit33) from the mycoparasitic fungus Trichoderma harzianum, coding for a chitinase of 33 kDa, has been isolated and characterized and enzyme characteristics suggest a nutritional, rather than a morphogenetic, role for this chit inase.

TL;DR: The cell-wall degrading enzymes β-glucanase and chitinase have been suggested to be essential for the mycoparasitic action of Trichoderma species against plant fungal pathogens, and their production in different carbon sources showed an increase parallel to increasing concentrations of either pustulan or chitIn, although the extent of this increase varied with the different enzymes.

TL;DR: The first genomic and cE)NA clones encoding a β-1,6-endoglucanase gene are described, successfully produced in Saccharomyces cerevisiae upon construction of a transcriptional fusion of the cDNA with a yeast promoter.