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Showing papers on "Trichoderma longibrachiatum published in 1984"


Journal ArticleDOI
01 May 1984-Botany
TL;DR: Two new species are described in the section: Trichoderma citrinoviride Bissett has relatively large, ellipsoidal conidia and a very sparse branching system with curved or sinuous conidiophores, branches, and phialides.
Abstract: Variation in strains assignable to the Trichoderma longibrachiatum Rifai and T. pseudokoningii Rifai species aggregates was studied. Morphological similarities allow their assignment to one section...

223 citations


Journal ArticleDOI
TL;DR: 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 cellopentose upwards with almost 100% efficiency.
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.

1 citations


Journal ArticleDOI
TL;DR: A water-insoluble glucan was synthesized by the β-transglycosylase of Trichoderma longibrachiatum in a reasonable yield from 1% cellopentaose as the substrate after 48 hr incubation as discussed by the authors.
Abstract: A water-insoluble glucan was synthesized by the β-transglycosylase of Trichoderma longibrachiatum in a reasonable yield from 1% cellopentaose as the substrate after 48 hr incubation. The glucan could be completely solubilized by cellulase to give glucose, cellobiose and cellotriose, although the reaction time was about 9 times longer than that required for the complete solubilization of the higher cellodextrin (DP 14) synthesized by the β-transglucosylase of Sclerotinia libertiana. The glucan was separated into two main fractions according to the solubility in NaOH solution, the major soluble in 4 N-NaOH and the minor insoluble in it. The structure of the major fraction was investigated by methylation analysis, and it was clearly shown to be a linear β-l,4-glucan having an average degree of polymerization of 19. These results indicated that the β-transglycosylase of Trichoderma longibrachiatum had a strict specificity of forming β-1,4-glucosidic linkages and also had a capacity to elongate the linkage to ...