Penicillin G splitting in a flow-through electro-membrane reactor with the membrane-bound enzyme

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F09%3A00021996" target="_blank" >RIV/60461373:22340/09:00021996 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Penicillin G splitting in a flow-through electro-membrane reactor with the membrane-bound enzyme

Popis výsledku v původním jazyce

Penicillin G (PenG) (0.05 mol dm(-3) in phosphate buffer, pH = 8) was hydrolyzed in a continuous flow-through electro-membrane reactor (EMR) with the penicillin G acylase (PGA) (EC 3.5.1.11) immobilized in 10% (w/v) polyacrylamide membrane with an area of 900 mm(2), thickness of 1 mm and enzyme activity of 100 U cm(-3) and 160 U cm(-3), respectively. The PenG was continuously fed to the substrate compartment adjacent to one membrane surface. Reaction products were washed from the membrane by a phosphatebuffer solution fed to the product compartment adjacent to the other membrane surface. The mean residence time of both streams was varied from 11.3 min to 45 min. An electric field perpendicular to the membrane surface was imposed on the reactor and theelectric current density was varied from 0 to 822 A m(-2). Substrate conversion was determined as a function of the mean residence time, of the applied electric current density and of the enzyme activity of the membrane. The conversion i

Název v anglickém jazyce

Penicillin G splitting in a flow-through electro-membrane reactor with the membrane-bound enzyme

Popis výsledku anglicky

Penicillin G (PenG) (0.05 mol dm(-3) in phosphate buffer, pH = 8) was hydrolyzed in a continuous flow-through electro-membrane reactor (EMR) with the penicillin G acylase (PGA) (EC 3.5.1.11) immobilized in 10% (w/v) polyacrylamide membrane with an area of 900 mm(2), thickness of 1 mm and enzyme activity of 100 U cm(-3) and 160 U cm(-3), respectively. The PenG was continuously fed to the substrate compartment adjacent to one membrane surface. Reaction products were washed from the membrane by a phosphatebuffer solution fed to the product compartment adjacent to the other membrane surface. The mean residence time of both streams was varied from 11.3 min to 45 min. An electric field perpendicular to the membrane surface was imposed on the reactor and theelectric current density was varied from 0 to 822 A m(-2). Substrate conversion was determined as a function of the mean residence time, of the applied electric current density and of the enzyme activity of the membrane. The conversion i

Druh

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

CEP obor

CI - Průmyslová chemie a chemické inženýrství

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2009

Kód důvěrnosti údajů

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

Název periodika

ASIA-PACIFIC JOURNAL OF CHEMICAL ENGINEERING

ISSN

1932-2143

e-ISSN

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Svazek periodika

4

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

9

Strana od-do

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Kód UT WoS článku

000267611600015

EID výsledku v databázi Scopus

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