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Trichoderma longibrachiatum

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


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Journal Article
TL;DR: Trichoderma longibrachiatum had strong parasitic and lethal effects on the cysts of H. avenae, and has the potential as a new biocontrol agent.
Abstract: Objective To evaluate the potential of Trichoderma longibrachiatum spore suspension against Heterodera avenae. Methods The parasitic and lethal effects of T. longibrachiatum spore suspension against the cysts of H. avenae were studied in vitro and observed under microscope. Results Microscopic observation showed that the spore suspension of T. longibrachiatum parasitized on the cyst surface, germinated a large number of hyphae, and grew on the surface of the cyst at the initial stage. Later, the cysts were completely surrounded by dense mycelium, and the contents of digestion in cysts was lysed, even some cysts produced vacuoles, and some were split up and finally the cyst was dissolved by the metabolite of T. longibrachiatum. In vitro studies showed that high concentrations of T. longibrachiatum spores had strong parasitic and lethal effects on the cysts of H. avenae, and the probable mechanism of parasitic and lethal effects of T. longibrachiatum against H. avenae were mainly by inducing and increasing chitinase, glucanase and caseinase activity. The cysts were parasitized by 93.3% at 18 days, the hatching of cysts were inhibited by 93.6% at 10 days when treated with the concentrations (1.5 x 10(8) CFU/mL) of T. longibrachiatum. Conclusion Trichoderma longibrachiatum had strong parasitic and lethal effects on the cysts of H. avenae, and has the potential as a new biocontrol agent.

9 citations

Journal ArticleDOI
TL;DR: In this article, the effects of pH, temperature, hydrolysis period, substrate and enzyme concentrations on the xylooligosaccharide yield and degree of polymerization were investigated.
Abstract: Xylooligosaccharide (XO) production was performed by enzymatic hydrolysis of xylans which were obtained by alkali extraction from tobacco stalk (TS), cotton stalk (CS) and wheat straw (WS). Xylan was hydrolyzed using Trichoderma longibrachiatum xylanase preparation, and the effects of pH, temperature, hydrolysis period, substrate and enzyme concentrations on the xylooligosaccharide yield and degree of polymerization were investigated. It was found that these three agricultural wastes contained different amounts of xylan, cellulose and lignin and the xylan obtained from these sources contained different amounts of sugar and uronic acid. The xylan from WS had the highest amount of arabinose while the other xylans mainly had xylose and small amount of glucose. Trichoderma longibrachiatum xylanase hydrolyzed highly branched wheat straw xylan (WSX) better than cotton stalk xylan (CSX) and tobacco stalk xylan (TSX) under favorable conditions ( reaction time of 8 h at pH 4.6 and 50oC). The TLC analysis of the hydrolysis products indicated that the hydrolysis product of T. longibrachiatum xylanase contained different amounts of oligosaccharides (X2, X3, X4, X5, X6, X7) with some monosaccharides. Regardless of the structural differences of the xylan types presented in this paper, all xylans generated XO with different degree of polymerization (DP).

9 citations

Journal ArticleDOI
TL;DR: These findings provide new insights into the plant interplay with Trichoderma, useful to further exploit rhizosphere fungi for the improvement of plant performance under limiting environments.

8 citations

Patent
10 May 1995
TL;DR: In this paper, the EG III cellulase enzyme from Trichoderma longibrachiatum and the amino acid sequence of the secreted (mature) and non-secreted (preprotein) forms of the enzyme were presented.
Abstract: The present invention is directed to purified EG III cellulase enzyme isolated from Trichoderma longibrachiatum and the amino acid sequence of the secreted (mature) and non-secreted (preprotein) forms. The present invention is further directed to the DNA fragment and sequence that encodes the EG III cellulase enzyme. Also disclosed are methods for isolating either purified or highly enriched EG III cellulase obtained from Trichoderma spp. or genetically modified strains of Trichoderma spp.

8 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
20221
202121
202026
201926
201819
201723