Identification and characterization of the Trichoderma harzianum gene encoding alpha-1,3-glucanase involved in streptococcal mutan degradation.

Inhibition of Trichoderma Species from Growth and Zoospore Production of Phytophthora Drechsleri and Their Effects on Hydrolytic Enzymes

Understanding the function of Trichoderma species in the control of Phytophthora drechsleri in pistachio orchards is very important.  In this study, the effects of liquid extra-cellular secretions and volatile compounds secreted by 27 isolates of Trichoderma harzianum, T. crassum, T. koningii, T.aureoviride, T. asperellum, T. brevicompactum, T.longibrachiatum and T. virens were investigated on ...

Parallel formation and synergism of hydrolytic enzymes and peptaibol antibiotics, molecular mechanisms involved in the antagonistic action of Trichoderma harzianum against phytopathogenic fungi.

Chitinase, beta-1,3-glucanase, and protease activities were formed when Trichoderma harzianum mycelia, grown on glucose as the sole carbon source, were transferred to fresh medium containing cell walls of Botrytis cinerea. Chitobiohydrolase, endochitinase, and beta-1,3-glucanase activities were immunologically detected in culture supernatants by Western blotting (immunoblotting), and the first ...

Aspartyl protease from Trichoderma harzianum CECT 2413: cloning and characterization.

A gene that encodes an extracellular aspartyl protease from Trichoderma harzianum CECT 2413, papA, has been isolated and characterized. Based on several conserved regions of other fungal acid proteases, primers were designed to amplify a probe that was used to isolate the papA gene from a genomic library of T. harzianum. papA was an intronless ORF which encoded a polypeptide of 404 aa, includin...

An Antifungal Exo- -1,3-Glucanase (AGN13.1) from the Biocontrol Fungus Trichoderma harzianum

Purification and properties of an α-(1 → 3)-glucanase (EC 3.2.1.84) from Trichoderma harzianum and its use for reduction of artificial dental plaque accumulation.

Extracellular α-(1 → 3)-glucanase (mutanase, EC 3.2.1.84) produced by Trichoderma harzianum CCM F-340 was purified to homogeneity by ultrafiltration followed by ion exchange and hydrophobic interaction chromatography, and final chromatofocusing. The enzyme was recovered with an 18.4-fold increase in specific activity and a yield of 4.3%. Some properties of the α-(1 → 3)-glucanase were investiga...