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- W1791736393 abstract "A β-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 β-glucosidase activity. The reaction was optimal at pH 6.0 and 37°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 β-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." @default.
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- W1791736393 date "1984-01-01" @default.
- W1791736393 modified "2023-09-23" @default.
- W1791736393 title "Purification and Some Properties of β-Transglycosylase of Trichoderma longibrachiatum" @default.
- W1791736393 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a134677" @default.
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