Lipase enzymes on graphene oxide support for high-efficiency biocatalysis

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F16%3A00472483" target="_blank" >RIV/61388963:_____/16:00472483 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.apmt.2016.09.015" target="_blank" >http://dx.doi.org/10.1016/j.apmt.2016.09.015</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.apmt.2016.09.015" target="_blank" >10.1016/j.apmt.2016.09.015</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Lipase enzymes on graphene oxide support for high-efficiency biocatalysis

Popis výsledku v původním jazyce

Enzymatic biocatalysis is of huge importance on an industrial scale. The main problem of enzymes is that they undergo denaturation. Here, we demonstrate that stability and activity of the enzymes can be enhanced by their immobilization on graphene oxide. We show this by an example of biosynthesis of industrially highly important acylglycerols using lipase enzymes. The synthesis of mono-, di- and triacylglycerols is of huge technological importance in pharmaceutical as well as food and chemical industries. Since the mono- and diacylglycerols can be synthesized by chemical reactions only with several difficulties, the enzyme-catalyzed reactions are used. We demonstrate successful immobilization of lipases from Rhizopus oryzae, Candida rugosa and Penicillium camemberti on the surface of graphene oxide. The immobilized enzymes exhibit high stability as well as retain high activity in protic and aprotic polar solvents reaching up to 146% of immobilized lipase from P. camemberti activity in iso-propanol compared to non-incubated immobilized enzyme. The activity retention after the incubation in non-polar solvents like toluene and hexane was comparable to that of those not exposed to the organic solvent (100% relative activity). The immobilized lipases were shown to exhibit catalytic performance for esterification of glycerol and a series of fatty acids in hexane. Our results support suitability of immobilized lipases on graphene oxide as catalyst for monoacylglycerols and diacylglycerol syntheses. These products represent high value-added materials with application as biologically active pharmaceutical substances, synthetic building blocks, in the lipid modification of drugs and proteins, or in the effective synthesis of surfactants. The enhanced stability and activity of the enzymes may result in major application of graphene oxide on an industrial scale.

Název v anglickém jazyce

Lipase enzymes on graphene oxide support for high-efficiency biocatalysis

Popis výsledku anglicky

Enzymatic biocatalysis is of huge importance on an industrial scale. The main problem of enzymes is that they undergo denaturation. Here, we demonstrate that stability and activity of the enzymes can be enhanced by their immobilization on graphene oxide. We show this by an example of biosynthesis of industrially highly important acylglycerols using lipase enzymes. The synthesis of mono-, di- and triacylglycerols is of huge technological importance in pharmaceutical as well as food and chemical industries. Since the mono- and diacylglycerols can be synthesized by chemical reactions only with several difficulties, the enzyme-catalyzed reactions are used. We demonstrate successful immobilization of lipases from Rhizopus oryzae, Candida rugosa and Penicillium camemberti on the surface of graphene oxide. The immobilized enzymes exhibit high stability as well as retain high activity in protic and aprotic polar solvents reaching up to 146% of immobilized lipase from P. camemberti activity in iso-propanol compared to non-incubated immobilized enzyme. The activity retention after the incubation in non-polar solvents like toluene and hexane was comparable to that of those not exposed to the organic solvent (100% relative activity). The immobilized lipases were shown to exhibit catalytic performance for esterification of glycerol and a series of fatty acids in hexane. Our results support suitability of immobilized lipases on graphene oxide as catalyst for monoacylglycerols and diacylglycerol syntheses. These products represent high value-added materials with application as biologically active pharmaceutical substances, synthetic building blocks, in the lipid modification of drugs and proteins, or in the effective synthesis of surfactants. The enhanced stability and activity of the enzymes may result in major application of graphene oxide on an industrial scale.

Druh

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

CEP obor

CC - Organická chemie

OECD FORD obor

—

Projekt

<a href="/cs/project/GA15-09001S" target="_blank" >GA15-09001S: Chemické modifikace materiálů na bázi grafenu: Syntéza grafanu a halogengrafenu</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2016

Kód důvěrnosti údajů

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

Název periodika

Applied Materials Today

ISSN

2352-9407

e-ISSN

—

Svazek periodika

5

Číslo periodika v rámci svazku

Dec

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

9

Strana od-do

200-208

Kód UT WoS článku

000392950300019

EID výsledku v databázi Scopus

2-s2.0-84990050529