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Trichoderma harzianum
About: Trichoderma harzianum is a research topic. Over the lifetime, 4731 publications have been published within this topic receiving 96796 citations.
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TL;DR: A Trichoderma harzianum isolate, which was able to antagonize in field the phytopathogen Crinipellis perniciosa, the causal agent of witches' broom disease of cocoa, produces several hydrolytic enzymes.
Abstract: A Trichoderma harzianum isolate (1051), which was able to antagonize in field the phytopathogen Crinipellis perniciosa, the causal agent of witches' broom disease of cocoa, produces several hydrolytic enzymes. A chitinase, with molecular mass of about 37 kDA, which was secreted by the Trichoderma in the culture medium containing chitin, was partially purified by gel filtration followed by hydrophobic chromatography. The optimal pH and temperature for chitin hydrolysis by the partially purified enzyme were 4.0 and 37 °C, respectively. Chitobiose, laminarin, cellulosic substrates including aryl-glucosides, xylan, starch and β-galactomannan were not hydrolysed by the enzyme. Remarkably, the partially purified enzyme drastically affected the cell wall of the phytopathogen C. perniciosa in vitro.
59 citations
TL;DR: Four fungicides and two biological agents were evaluated for their eYcacy against gummy stem blight disease incidence and fruit yield in Weld conditions and Pseudomonas Xuorescens applied as pure culture and formulation at the rate of 8 and 10 g kg i1 signiWcantly reduced the disease incidence.
59 citations
TL;DR: The extensive secretome analysis of T. harzianum highlights the importance of this fungus as a rich source of hydrolytic enzymes for bioconversion and biocontrol applications.
Abstract: Trichoderma harzianum is a mycoparasitic filamentous fungus that produces and secretes a wide range of extracellular hydrolytic enzymes used in cell wall degradation. Due to its potential in biomass conversion, T. harzianum draws great attention from biofuel and biocontrol industries and research. Here, we report an extensive secretome analysis of T. harzianum. The fungus was grown on cellulose medium, and its secretome was analyzed by a combination of enzymology, 2DE, MALDI-MS and -MS/MS (Autoflex II), and LC-MS/MS (LTQ-Orbitrap XL). A total of 56 proteins were identified using high-resolution MS. Interestingly, although cellulases were found, the major hydrolytic enzymes secreted in the cellulose medium were chitinases and endochitinases, which may reflect the biocontrol feature of T. harzianum. The glycoside hydrolase family, including chitinases (EC 3.2.1.14), endo-N-acetylglucosaminidases (EC 3.2.1.96), hexosaminidases (EC 3.2.1.52), galactosidases (EC 3.2.1.23), xylanases (EC 3.2.1.8), exo-1,3-glucanases (EC 3.2.1.58), endoglucanases (EC 3.2.1.4), xylosidases (EC 3.2.1.37), α-L-arabinofuranosidase (EC 3.2.1.55), N-acetylhexosaminidases (EC 3.2.1.52), and other enzymes represented 51.36% of the total secretome. Few representatives were classified in the protease family (8.90%). Others (17.60%) are mostly intracellular proteins. A considerable part of the secretome was composed of hypothetical proteins (22.14%), probably because of the absence of an annotated T. harzianum genome. The T. harzianum secretome composition highlights the importance of this fungus as a rich source of hydrolytic enzymes for bioconversion and biocontrol applications.
59 citations
TL;DR: P pH regulation is mediated by the transcriptional factor Pac1 (homologous to PacC regulator in other fungi), encoded by pac1 whose expression increases with pH, which modulates T. harzianum antifungal activity since wild type and mutants inhibit several phytopathogenic fungal strains at various degrees in different assays.
58 citations
TL;DR: An extracellular serine protease producing fungi were isolated from the effluent sample collected from a sago industry in Salem and was identified as Graphium putredinis and Trichoderma harzianum.
Abstract: An extracellular serine protease producing fungi were isolated from the effluent sample collected from a sago industry in Salem and was identified as Graphium putredinis and Trichoderma harzianum. Intergenerically developed fusant produced high amounts of protease in soya bean meal amended minimal medium than the parents, G. putredinis and T. harzianum. The enzyme was purified by Sephadex G 100 column chromatography. The proteases of G. putredinis and T. harzianum had optimum pH and temperature of 7.0–8.0 and 50–60 °C respectively. At 37 and 60 °C, the parental proteases were respectively stable for 1 day and 15 min and the fusant was stable for 2 days and 10 min. The Km and Vmax were 0.65, 1.25 and 0.40 mg/ml and 2.00, 1.60 and 2.60 IU/mg protein for G. putredinis, T. harzianum and fusant respectively with a molecular weight of 31, 20 and 33 kDa. The effect of metal ions showed that, at 5 mM concentration of Hg2+, the residual protease activity of parent and fusant was 5.47, 2.48 and 9.76% respectively; Cu2+, Ca2+ and Zn2+ did not greatly affect the enzyme activity. In 5 mM EDTA showed residual activity between 60.76 and 85.66%. PMSF (2 mM) completely inhibited the protease activity of all the three fungi studied. All the three fungal enzymes retained maximum residual activity of 66.00, 63.80 and 76.74% with the commercial detergent Rin Advanced. With Kite, all the enzymes had more or less same level of residual activity (54–55%). With SDS and sodium perborate (0.2%) the residual activities were 58.25–73.82 and 61.58–70.24% respectively. Wash performance analysis revealed that fusant protease with Rin Advanced at 60 °C yielded good result.
58 citations