Showing papers on "Trichoderma longibrachiatum published in 2003"

Characterization of an Inducible Chlorophenol O-Methyltransferase from Trichoderma longibrachiatum Involved in the Formation of Chloroanisoles and Determination of Its Role in Cork Taint of Wines

Abstract: A novel S-adenosyl-l-methionine (SAM)-dependent methyltransferase catalyzing the O methylation of several chlorophenols and other halogenated phenols was purified 220-fold to apparent homogeneity from mycelia of Trichoderma longibrachiatum CECT 20431. The enzyme could be identified in partially purified protein preparations by direct photolabeling with [methyl-3H]SAM, and this reaction was prevented by previous incubation with S-adenosylhomocysteine. Gel filtration indicated that the Mr was 112,000, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that the enzyme was composed of two subunits with molecular weights of approximately 52,500. The enzyme had a pH optimum between 8.2 and 8.5 and an optimum temperature of 28°C, with a pI of 4.9. The Km values for 2,4,6-trichlorophenol and SAM were 135.9 ± 12.8 and 284.1 ± 35.1 μM, respectively. S-Adenosylhomocysteine acted as a competitive inhibitor, with a Ki of 378.9 ± 45.4 μM. The methyltransferase was also strongly inhibited by low concentrations of several metal ions, such as Cu2+, Hg2+, Zn2+, and Ag+, and to a lesser extent by p-chloromercuribenzoic acid, but it was not significantly affected by several thiols or other thiol reagents. The methyltransferase was specifically induced by several chlorophenols, especially if they contained three or more chlorine atoms in their structures. Substrate specificity studies showed that the activity was also specific for halogenated phenols containing fluoro, chloro, or bromo substituents, whereas other hydroxylated compounds, such as hydroxylated benzoic acids, hydroxybenzaldehydes, phenol, 2-metoxyphenol, and dihydroxybenzene, were not methylated.

Allergic Fungal Sinusitis Associated with Trichoderma longibrachiatum

Abstract: We describe allergic fungal sinusitis caused by Trichoderma longibrachiatum in a patient with a history of atopy and asthma. A Gram stain of a sinus biopsy specimen was initially thought to contain yeast cells, but when Trichoderma was recovered in culture, these cells were subsequently recognized as chlamydospores. The patient was successfully managed with a combination of sinus lavage, oral corticosteroids, itraconazole, and allergen immunotherapy. This case also points out that careful scrutiny of direct smears is required to ensure that fungal structures are not misinterpreted.

A Novel NAD-Dependent Dehydrogenase, Highly Specific for 1,5-Anhydro-d-Glucitol, from Trichoderma longibrachiatum Strain 11-3

Abstract: A novel NAD-dependent dehydrogenase highly specific for 1,5-anhydro-d-glucitol (1,5-AG) was found in the cell extract of an imperfect fungus, Trichoderma longibrachiatum strain 11-3. This fungus used 1,5-AG as a sole carbon source for growth and transformed 1,5-AG into glucose. 1,5-AG dehydrogenase (AGH) was purified to homogeneity, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The molecular mass of the purified enzyme was estimated to be 36 and 141 kDa by SDS-PAGE and by gel filtration, respectively, suggesting that the enzyme was homotetrameric. The enzyme was highly specific for 1,5-AG and did not exhibit activity with any sugar or sugar alcohol tested in this study other than 1,5-AG. A linear relationship between the initial rate of the enzyme reaction and the concentration of 1,5-AG at the physiological level was observed. The presence of glucose in abundance did not interfere with the relationship. The optimum temperature for the enzyme reaction was 50°C, and the enzyme was stable at temperatures up to 70°C. These results suggested that AGH is a novel enzyme and is useful for specifically diagnosing diabetes mellitus.