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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 ArticleDOI
TL;DR: In this article, a marine-related Trichoderma longibrachiatum strain isolated from mussels in a farming shellfish area was investigated for total lipid (TL) production, total lipid fatty acids (TLFA), and phospholipid fatty acid (PLFA).

21 citations

Journal ArticleDOI
TL;DR: Results suggest that the non-mutated strain T. longibrachiatum (GHL), isolated from soil near an Algerian hot spring, should be an attractive producer for cellulases production.
Abstract: The indigenous cellulolytic fungus Trichoderma longibrachiatum (GHL) isolated from soil near an Algerian hot spring was used for the production of cellulases by submerged fermentation on Mandels medium with cellulose Avicel (1%) as the sole carbon source. Endoglucanase and filter paper activities of the wild-type strain of Trichoderma were compared to the hypercellulolytic mutated Trichoderma reesei Rut C-30, in shake flask cultures at 35°C. After seven days of fermentation, T. longibrachiatum show equivalent activities than T. reesei (10.61 IU/ml of endoglucanase (CMCase) and 2.04 IU/ml of filter paper activity (FPA)). On the other hand, the s-glucosidase activity of Trichoderma GHL was twice more important than that of T. reseei . The influence of inoculum size on cellulase activities did not prove significant differences in enzymatic activities for spore concentrations between 105 and 108 spores/ml. The cellulases produced by the isolated strain were also characterized. The optimum temperatures were 55 and 60°C for endoglucanase and FPA, respectively. The endoglucanase was thermostable at 70°C after 5 h incubation, and it preserved 80% of the original activity. The half-life of the FPA appeared to be 3 h at 60°C. The endoglucanase was optimally active at pH 4.0, and the FPA was optimal at pH 4.0 and 5.0. These activities were stable at 50°C after 5 h incubation in a pH range of 3.0 to 6.0 and 4.0 to 6.0, respectively. These results suggest that the non-mutated strain T. longibrachiatum (GHL) should be an attractive producer for cellulases production. Keywords : Cellulase, Trichoderma reesei, Trichoderma longibrachiatum , submerged fermentation, characterization African Journal of Biotechnology Vol. 12(5), pp. 465-475

20 citations

Journal ArticleDOI
TL;DR: A mathematical model for enzymatic cellulose hydrolysis in a plug-flow column reactor has been developed and affords a reliable prediction of the kinetics of d -glucose and cellobiose formation from cellulose in a column reactor.

20 citations

Journal ArticleDOI
TL;DR: Extracts from 14 barley silages inhibited endo-1, 4-β-xylanase and α-amylase activities of a ruminant feed enzyme additive from Trichoderma longibrachiatum by 23 to 50% but had little effect on cellulase activity.
Abstract: Extracts from 14 barley silages inhibited endo-1, 4-β-xylanase and α-amylase activities of a ruminant feed enzyme additive from Trichoderma longibrachiatum by 23 to 50% but had little effect on cellulase activity. The inhibitory factor(s) were <10 kDa in size and were stable to autoclaving. These observations may explain why feed enzymes are generally less effective when applied to silages than when applied to dry feeds. Key words: Silage, fibrolytic enzymes, Trichoderma, xylanase, inhibitors

20 citations

Patent
11 Mar 1994
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 inventon 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 $i(Trichoderma spp.)

20 citations


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