Graphene oxide immobilized enzymes show high thermal and solvent stability

0443878 - ÚOCHB 2016 RIV GB eng J - Článek v odborném periodiku
Hermanová, S. - Zarevúcka, Marie - Bouša, D. - Pumera, M. - Sofer, Z.
Graphene oxide immobilized enzymes show high thermal and solvent stability.
Nanoscale. Roč. 7, č. 13 (2015), s. 5852-5858. ISSN 2040-3364. E-ISSN 2040-3372
Grant CEP: GA ČR(CZ) GA15-09001S
Grant ostatní: GA AV ČR(CZ) M200551203
Institucionální podpora: RVO:61388963
Klíčová slova: graphene oxide * lipase * immobilization
Kód oboru RIV: CC - Organická chemie
Impakt faktor: 7.760, rok: 2015
http://pubs.rsc.org/en/content/articlepdf/2015/nr/c5nr00438a

The thermal and solvent tolerance of enzymes is highly important for their industrial use. We show here that the enzyme lipase from Rhizopus oryzae exhibits exceptionally high thermal stability and high solvent tolerance and even increased activity in acetone when immobilized onto a graphene oxide (GO) nanosupport prepared by Staudenmaier and Brodie methods. We studied various forms of immobilization of the enzyme: by physical adsorption, covalent attachment, and additional crosslinking. The activity recovery was shown to be dependent on the support type, enzyme loading and immobilization procedure. Covalently immobilized lipase showed significantly better resistance to heat inactivation (the activity recovery was 65% at 70 degrees C) in comparison with the soluble counterpart (the activity recovery was 65% at 40 degrees C). Physically adsorbed lipase achieved over 100% of the initial activity in a series of organic solvents. These findings, showing enhanced thermal stability and solvent tolerance of graphene oxide immobilized enzyme, will have a profound impact on practical industrial scale uses of enzymes for the conversion of lipids into fuels.
Trvalý link: http://hdl.handle.net/11104/0246565