Zvýšení aktivity lipas účinkem superkritického oxidu uhličitého

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F08%3A00315362" target="_blank" >RIV/61388963:_____/08:00315362 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/67985858:_____/08:00315362 RIV/61389030:_____/08:00315362

Výsledek na webu

—

DOI - Digital Object Identifier

—

Jazyk výsledku

angličtina

Název v původním jazyce

Lipase Activity Enhancement by SC-CO2 Treatment

Popis výsledku v původním jazyce

The activity of lipases from porcine pancreas, Candida antartica recombinant from Aspergillus oryzae, Candida cylindracea (immobilized), Penicilium roqueforti, Aspergillus niger, Rhizopus arrhizus, Mucor miehei (two types of immobilization), and Pseudomonas cepacia (two types of immobilization) was studied after using them as biocatalysts of blackcurrant oil hydrolysis under SC-CO2 conditions. The reaction was performed at 40 degrees C and 15 MPa in a continuous-flow reactor. Increased relative activityof all used lipases after the hydrolytic reaction was observed. The most remarkable increase in the activity was noted for the lipase from Rhizopus arrhizus which was increased by more than 50 times. The highest activity was shown by Lipozyme (R), lipase from Mucor miehei immobilized on macroporous resin. Both treated and untreated Lipozyme(D were used as biocatalysts in hydrolytic resolution of the racemic cis- or trans-isomers of 2-(4-methoxybenzyl)cyclohexyl acetates. Satisfactory re

Název v anglickém jazyce

Lipase Activity Enhancement by SC-CO2 Treatment

Popis výsledku anglicky

The activity of lipases from porcine pancreas, Candida antartica recombinant from Aspergillus oryzae, Candida cylindracea (immobilized), Penicilium roqueforti, Aspergillus niger, Rhizopus arrhizus, Mucor miehei (two types of immobilization), and Pseudomonas cepacia (two types of immobilization) was studied after using them as biocatalysts of blackcurrant oil hydrolysis under SC-CO2 conditions. The reaction was performed at 40 degrees C and 15 MPa in a continuous-flow reactor. Increased relative activityof all used lipases after the hydrolytic reaction was observed. The most remarkable increase in the activity was noted for the lipase from Rhizopus arrhizus which was increased by more than 50 times. The highest activity was shown by Lipozyme (R), lipase from Mucor miehei immobilized on macroporous resin. Both treated and untreated Lipozyme(D were used as biocatalysts in hydrolytic resolution of the racemic cis- or trans-isomers of 2-(4-methoxybenzyl)cyclohexyl acetates. Satisfactory re

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CI - Průmyslová chemie a chemické inženýrství

OECD FORD obor

—

Projekt

<a href="/cs/project/OC%20D30.001" target="_blank" >OC D30.001: Enzymová katalýza v superkritickém oxidu uhličitém</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2008

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Zeitschrift fur Naturforschung. Section B: a Journal of Chemical Sciences

ISSN

0932-0776

e-ISSN

—

Svazek periodika

63b

Číslo periodika v rámci svazku

6

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

6

Strana od-do

—

Kód UT WoS článku

000256944000028

EID výsledku v databázi Scopus

—