Trichoderma longibrachiatum

About: Trichoderma longibrachiatum is a research topic. Over the lifetime, 452 publications have been published within this topic receiving 10591 citations.

Antibacterial Activities of the Extracts of Sponge-Associated Fungus Trichoderma longibrachiatum against Pathogenic Bacteria

Abstract: This study aims to explore the antibacterial potential of a sponge-associated fungus Trichoderma longibrachiatum isolated from Ternate waters, North Maluku, Eastern Indonesia. Various culture media were used to stimulate the production of secondary metabolites in T. longibrachiatum. The isolate was cultured in various media for 6-9 days. Then, the antibacterial activities of the ethyl acetate extracts were assayed against pathogenic bacteria of Multi-Drug Resistant (MDR) strain (Pseudomonas aeruginosa, Staphylococcus aureus, Klebsiella pneumoniae, and Bacillus cereus). The results showed that all extracts had similar profiles on the thin layer chromatography. However, two of the most potent extracts were produced from the PCA and MEA media for 9 days. These extracts inhibited methicillin-resistant S. aureus (MRSA) (12.48 mm and 12.27 mm); B. cereus (12.11 mm and 12.12 mm); K. pneumoniae (12.40 mm and 10.76 mm); and P. aeruginosa (11.59 mm and 8.69 mm) at concentrations 500 mg/disc. In conclusion, the fungus T. longibrachiatum that was cultured in PCA and MEA media had the potential to produce antibacterial compounds against MDR pathogens and both had similar compounds. Meanwhile, the ethyl acetate extracts from fungus cultured in the TPA and TA media were inactive against all tested bacteria

Mutualistic interaction with Trichoderma longibrachiatum UENF-F476 boosted plant growth-promotion of Serratia marcescens UENF-22GI

Abstract: BACKGROUND A plethora of bacteria-fungal interactions occurs on the extended fungal hyphae network in soil. The mycosphere of saprophytic fungi can serve as a bacterial niche boosting their survival, dispersion, and activity. Such ecological concepts can be converted to bioproducts for sustainable agriculture. Accordingly, we tested the hypothesis that the well-characterized beneficial bacterium Serratia marcescens UENF-22GI can enhance their plant growth-promoting properties by combination with Trichoderma longibrachiatum UENF-F476. RESULTS The colony and cell interactions demonstrated S. marcescens and T. longibrachiatum compatibility. Bacteria cells were able to attach, forming aggregates-biofilms and migrates through fungal hyphae network. Bacterial migration through growing hyphae was confirmed using two-compartment Petri dishes assay. Fungal inoculation increased the bacteria survival rates into the vermicompost substrate over the experimental time. Also, in vitro indolic compound, phosphorus, and zinc solubilization bacteria activities increased in the presence of the fungus. In line with the ecophysiological bacteria fitness, tomato and papaya plantlet growth was boosted by bacteria-fungi combination applied under plant nursery conditions. CONCLUSION Mutualistic interaction between mycosphere-colonizing bacterium S. marcescens UENF-22GI and the saprotrophic fungi T. longibrachiatum UENF-F467 increased the ecological fitness of the bacteria alongside with beneficial potential for plant growth. A proper combination and delivery of compatible beneficial bacteria-fungus represent an open avenue for biological enrichment of plant substrates technologies in agricultural systems.

PURIFICATION, CHARACTERISATION AND CLONING OF -1,3 GLUCANASE GENE FROM Trichoderma harzinum

Abstract: Dual culture technique was used to evaluate the effect of three species of Trichoderma that showed a potential control of Fusarium oxysporium. Trichoderma harzianum showed maximum growth inhibition (79.3%) followed by Trichoderma viridi (68.5%) and Trichoderma longibrachiatum (44.3%). β-1,3-glucanases was purified from Trichoderma harzianum to homogeneity by ion exchange chromatography on DEAE-Sephacel and gel filtration on Sephadex G100. A typical procedure provided 20-fold purification with 11.9% yield. The apparent molecular mass was 30 kD and it was active on a broad pH range, however the maximal activity was detected at pH 7.5. The optimum temperature of the β-1,3-glucanase was 55C. Polymerase chain reaction (PCR) was used to amplify a fragment about 600 bp from β-1,3 gluanase gene using specific glu forward and reverse primers. The eluted DNA was ligated into pGEM-T-Easy vector and transformed into competent E. coli JM109. White transformed colony, named T1glu, containing recombinant plasmid was validated by PCR using both glu forward and reverse and M13 forward and reverse primers to confirm the presence of β 1,3 glucanase gene insert in right orientation whereas, the fragment amplified with glu forward and glu reverse primers was 600 bp. Partial sequence of the amplified DNA fragment showed 97% sequence homology with the other published sequences.

Purification and some properties of beta-transglycosylase of Trichoderma longibrachiatum.

Abstract: A beta-transglycosylase was purified to a homogeneous state from the extract of a wheat bran Koji culture of Trichoderma longibrachiatum by column chromatography. The purified enzyme showed a typical disproportionation reaction with cellopentaose as the substrate, producing a high molecular component (a water-insoluble glucan). The enzyme showed neither cellulase nor beta-glucosidase activity. The reaction was optimal at pH 6.0 and 37 degrees C. The molecular weight of the enzyme was estimated to be 11,000 by gel filtration using a TOYOPEARL HW-55F column. The amount of the glucan synthesized by the enzyme increased with prolonged incubation in a reaction with cellopentaose, and soluble cellooligosaccharides, such as cellobiose, cellotriose, cellotetraose, and cellohexaose, were also produced. No glucose was produced in the reaction even when it was carried out for a long time. The total number of molecules (cellooligosaccharides) in the reaction mixture remained at the initial substrate level during the entire reaction. The beta-transglycosylase proved to be a specific transferase showing transfer activity of glucosyl, cellobiosyl, and cellotriosyl moieties from one cellopentaose to an acceptor molecule from cellopentaose upwards with almost 100% efficiency.