Please use this identifier to cite or link to this item:
https://open.uns.ac.rs/handle/123456789/13985
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Pekić B. | en |
dc.contributor.author | Lepojević Z. | en |
dc.date.accessioned | 2020-03-03T14:54:27Z | - |
dc.date.available | 2020-03-03T14:54:27Z | - |
dc.date.issued | 1991-06-01 | en |
dc.identifier.issn | 01415492 | en |
dc.identifier.uri | https://open.uns.ac.rs/handle/123456789/13985 | - |
dc.description.abstract | The 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.ispartof | Biotechnology Letters | en |
dc.title | Enzymatic transformation of desacetyl-lanatoside A into digitoxin by β-glucosidase action in cyclodextrin solutions | en |
dc.type | Journal/Magazine Article | en |
dc.identifier.doi | 10.1007/BF01030990 | en |
dc.identifier.scopus | 2-s2.0-0025832250 | en |
dc.identifier.url | https://api.elsevier.com/content/abstract/scopus_id/0025832250 | en |
dc.relation.lastpage | 404 | en |
dc.relation.firstpage | 399 | en |
dc.relation.issue | 6 | en |
dc.relation.volume | 13 | en |
item.grantfulltext | none | - |
item.fulltext | No Fulltext | - |
Appears in Collections: | TF Publikacije/Publications |
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