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Transglycosylation activity of cellobiohydrolase-i from trichoderma-longibrachiatum on synthetic and natural substratesстатья
Информация о цитировании статьи получена из
Scopus,
Web of Science
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
- Авторы: Gusakov A.V., Protas O.V., Chernoglazov V.M., Sinitsyn A.P., Kovalysheva G.V., Shpanchenko O.V., Ermolova O.V.
- Журнал: Biochimica et Biophysica Acta - Proteins and Proteomics
- Том: 1073
- Номер: 3
- Год издания: 1991
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 481
- Последняя страница: 485
- DOI: 10.1016/0304-4165(91)90219-7
- Аннотация: Using 4-methylumbelliferyl (MUF) beta-D-cellobioside as a substrate, the ability of cellobiohydrolase I from Trichoderma longibrachiatum to catalyze transglycosylation has been demonstrated. At substrate concentrations greater than 2 mM, the formation of MUF-tetrasaccharide was detected using HPLC. In the course of enzymatic reaction, a concentration of the transglycosylation product passed through a maximum, since at later stages of the reaction the product was further hydrolyzed. At MUF-beta-D-cellobioside concentrations of 2-10 mM, the maximum weight content of MUF-tetrasaccharide amounted to 1-4% of the total content of saccharides. In the reaction system, containing 2.5 mM MUF-beta-D-cellobioside and 10 mM MUF-beta-D-glucoside, MUF-trisaccharide was formed as the main transglycosylation product. In hydrolysis of natural substrates (cellulose and cellotriose) in the presence of MUF-beta-D-glucoside a formation of MUF-trisaccharide was also observed.
- Добавил в систему: Гусаков Александр Васильевич