Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników

Znaleziono wyników: 5

Liczba wyników na stronie
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników

Wyniki wyszukiwania

help Sortuj według:

help Ogranicz wyniki do:
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników
Cells of suspension culture Citrullus vulgaris cv. "Samara" were permeabilized by Tween 80 and immobilized by glutaraldehyde. The highest a-galactosidase activity was at pH 5.4 and 60°C. The hydrolysis of substrate was linear for 3.5 h reaching 65-70% conversion of the substrate. The cells characterized with high enzyme activity, and stability in long-term storage showed convenient physico-mechanical properties (physical protection from shear forces and easy separation of product from biocatalysts).
Extracellular plant β-galactosidase from opium poppy and celandine was detected on agar plates by the presence of dyed zones from 1-naphthyl-β-D-galactopyranoside used as a synthetic substrate. Evaluating the azo-dye zones assessed the degree β-galactosidase activity. No coloration of the agar medium was observed on non-inoculated parts, in medium inoculated with heat – inactivated cells (10 min. at 100oC) or in medium without substrate with all calli tested. On the agar plates with substrate and sterile opium poppy, celandine or gherkin seedlings (2–6 days old) changes in coloration were observed showing the release of β-galactosidase from the roots during germination.
Cell suspension of Papaver somniferum L. (opium poppy) was permeabilized by Tween 80 and immobilized by glutaraldehyde. The highest saccharase activity was at pH 4.6 and 50°C. The hydrolysis of the substrate was linear for 5 h reaching 69% of conversion, A very good storage stability was achieved when using dry catalyst, or a solution of 0.15 M NaCl with the addition of chloramphenicol, (l-methyldodecyl)-dimethylamin-4-oxide (ATDNO), Chlortetracycline hydrochloride (CLCTC) or by freezing the immobilized cells in 0.15 M NaCl. The cells characterized by high enzyme activity and stability in long-term storage showed convenient technological and physicomechanical properties.
A simple and rapid procedure for identification and determination of extracellular saccha- rase is described, using a culture medium of Chelidonium majus L. (celandine) cell suspen­sion cultures. Sucrose was used as a substrate for determination of the extracellular and intracellular activities of the studied enzyme. The culture medium (without cells) was used for identification and determination of extracellular enzyme activity. Intracellular activity was estimated using cell suspension.
Cell suspensions of gherkin (Cucumis sativus L.) were permeabilized by Tween-80, and immobilized by glutaraldehyde. β-Galactosidase showed pH optimum at 4.9 and temperature optimum at 58 °C. The enzyme catalysed hydrolysis was linear for 3 h with 60-68% conversion of the substrate. The cells characterized by high β-galactosidase activity and stability on long-term storage showed valuable technological properties.
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.