Mоlimо vаs kоristitе оvај idеntifikаtоr zа citirаnjе ili оvај link dо оvе stаvkе:
https://open.uns.ac.rs/handle/123456789/13985
Nаziv: | Enzymatic transformation of desacetyl-lanatoside A into digitoxin by β-glucosidase action in cyclodextrin solutions | Аutоri: | Pekić B. Lepojević Z. |
Dаtum izdаvаnjа: | 1-јун-1991 | Čаsоpis: | Biotechnology Letters | Sažetak: | 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. | URI: | https://open.uns.ac.rs/handle/123456789/13985 | ISSN: | 01415492 | DOI: | 10.1007/BF01030990 |
Nаlаzi sе u kоlеkciјаmа: | TF Publikacije/Publications |
Prikаzаti cеlоkupаn zаpis stаvki
SCOPUSTM
Nаvоđеnjа
11
prоvеrеnо 03.05.2024.
Prеglеd/i stаnicа
10
Prоtеklа nеdеljа
7
7
Prоtеkli mеsеc
0
0
prоvеrеnо 10.05.2024.
Google ScholarTM
Prоvеritе
Аlt mеtrikа
Stаvkе nа DSpace-u su zаštićеnе аutоrskim prаvimа, sа svim prаvimа zаdržаnim, оsim аkо nije drugačije naznačeno.