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Transglycosylation reactions catalyzed by cellobiohydrolase I from Trichoderma longibrachiatum in the hydrolysis of synthetic and natural substrates
A. V. Gusakov, O. V. Protas, V. M. Chernoglazov, A. P. Sinilsyn, G. V. Kovalysheva, O. V. Shpanchenko, O. V. Ermolova
Department of Chemistry, M. V. Lomonosov Moscow State University
Abstract: Using 4-methylumbelliferyl β-D-cellobioside as a substrate, the ability of cellobio-hydrolase I from Trichoderma longibrachiatum to catalyze transglycosylation has been demonstrated. At the substrate concentrations exceeding 2 mM, formation of a Muf-tetraoside was detected using HPLC. In the course of the enzymatic reaction, concentration of the transglycosylation product passed through a maximum, since at later stages the product was hydrolyzed. At Muf-β-D)-cellobioside concentrations of 2—10 mM, the maximum weight content of Muf-tetraoside was 1–4% of the total content of saccha-rides. In the reaction system containing 2.5 mM Muf- β-D-cellobioside and 10 mM Muf-β-D-glucoside, Muf-trioside was formed as the main transglycosylation product. In hydrolysis of natural substrates (cellulose and cellotriose) in the presense of Muf-β-D-glucoside, formation of a Muf-trioside was also observed.
Russian Journal of Bioorganic Chemistry 1990, 16 (7):898-903