Please use this identifier to cite or link to this item: https://open.uns.ac.rs/handle/123456789/13985
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dc.contributor.authorPekić B.en
dc.contributor.authorLepojević Z.en
dc.date.accessioned2020-03-03T14:54:27Z-
dc.date.available2020-03-03T14:54:27Z-
dc.date.issued1991-06-01en
dc.identifier.issn01415492en
dc.identifier.urihttps://open.uns.ac.rs/handle/123456789/13985-
dc.description.abstractThe enzymatic transformation of desacetyl-lanatoside A (DLA) to its secondary glycoside, digitoxin, in solutions of β-and γ-cyclodextrins is effected using of β-glucosidase from barley. Due to the interaction of cyclodextrins (CyDs) with desacetyl-lanatoside A, an increase in solubility of the latter of 24.5 and 230 times was observed for β-cyclodextrin and γ-cyclodextrin, respectively. Kinetic studies of the enzymatic transformation gave for β-glucosidase the values KM=3.3×10-4 mol. dm-3 and Vmax=0.557 μmol mg-1 min-1 when the substrate was the deacetyl-lanatoside A complex with β-cyclodextrin, while in the case of the complex with γ-cyclodextrin these values were KM=5.45×10-4 mol dm-3 and Vmax=0.896 μmol mg-1 min-1. © 1991 Science and Technology Letters.en
dc.relation.ispartofBiotechnology Lettersen
dc.titleEnzymatic transformation of desacetyl-lanatoside A into digitoxin by β-glucosidase action in cyclodextrin solutionsen
dc.typeJournal/Magazine Articleen
dc.identifier.doi10.1007/BF01030990en
dc.identifier.scopus2-s2.0-0025832250en
dc.identifier.urlhttps://api.elsevier.com/content/abstract/scopus_id/0025832250en
dc.relation.lastpage404en
dc.relation.firstpage399en
dc.relation.issue6en
dc.relation.volume13en
item.grantfulltextnone-
item.fulltextNo Fulltext-
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