Purification and some properties of beta-transglycosylase of Trichoderma longibrachiatum.
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.
D055598:Chemical Phenomena; D002621:Chemistry; D002855:Chromatography, Thin Layer; D005964:Glucosyltransferases / Q000302:isolation & purification* / Q000378:metabolism; D003904:Mitosporic Fungi / Q000201:enzymology*; D008970:Molecular Weight; D013379:Substrate Specificity; D013696:Temperature; D014242:Trichoderma / Q000201:enzymology*
D005964:Glucosyltransferases