[Detection of transglycosylation reactions under the influence of Trichoderma koningii and Trichoderma viride cellulase].
The transglycosylation reactions catalyzed by the low molecular weight endo-beta-1,4-glucanase from the cellulase complex of Trichoderma koningii as well as unseparated complexes from Tr. koningii and Tr. viride were investigated. The products obtained from the mixture of cellodextrine (donor, 0.5%) and p-nitrophenyl-beta-D-glucopyranoside (acceptor, 0.4%) with the aid of the above enzymes were analyzed. Transglycosylation products were separated by Sephadex G-15 gel-filtration. In all the three cases the highest molecular weight p-nitrophenyl glycosides of oligosaccharides (with a molecular weight of over 1500) were first synthesized and then hydrolyzed. At the beginning of the reaction the amount of p-nitrophenyl glycosides of oligosaccharides synthesized was greater than that of the reducing groups measured according to Nelson. Addition of p-nitrophenyl-beta-D-glucopyranoside to cellodextrine did not influence the rate with which the latter was hydrolyzed by endoglucanase.
D002480:Cellulase / Q000378:metabolism*; D007700:Kinetics; D003904:Mitosporic Fungi / Q000201:enzymology*; D013045:Species Specificity; D014242:Trichoderma / Q000201:enzymology*
D002480:Cellulase
Obnaruzhenie reaktsiĭ transglikozilirovaniia pri deĭstvii preparatov tselliulaz Trichoderma koningii i Trichoderma viride.