fevereiro 2015 vol. 1 num. 2 - XX Congresso Brasileiro de Engenharia Química

Artigo - Open Access.

Idioma principal




Stabilization of multimeric enzymes is one of the major challenges in biocatalysis, because dissociation of subunits can inactivate the enzyme. Catalase (CAT; EC 1.11.16) is a homotetramer containing Fe-protoporphyrin IX in its active site. CAT breaks down hydrogen peroxide into water and molecular oxygen. In this study, cross-linked enzyme aggregates of bovine liver CAT (CAT-CLEAs) were prepared. The effects of precipitation and cross-linking on enzyme activity were studied. Thermal stability of free and immobilized enzyme were also evaluated at 40 ᵒC and pH 7 (200 h). CAT-CLEAs were successfully prepared using ammonium sulfate and glutaraldehyde (50 mM) as the precipitant and cross-linking agent, respectively. The best recovered activity obtained was 62 %. The derivative retained high activity along the stability test. The kinetic parameters values vmax and Km were estimated as 11,350 U/mg and 66.7±10 mM for the free CAT and 2,000 U/mg and 392±22 mM for the CAT-CLEAs,



DOI: 10.5151/chemeng-cobeq2014-1205-20483-160850

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Como citar:

MAFRA, A. C. O.; KOPP, W.; RAMOS, M. D.; BELTRAME, M. B.; RIBEIRO, M. P. A.; BADINO, A. C; TARDIOLI, P. W.; "CROSS-LINKED ENZYME AGGREGATES OF CATALASE FROM BOVINE LIVER", p. 1714-1721 . In: Anais do XX Congresso Brasileiro de Engenharia Química - COBEQ 2014 [= Blucher Chemical Engineering Proceedings, v.1, n.2]. São Paulo: Blucher, 2015.
ISSN 2359-1757, DOI 10.5151/chemeng-cobeq2014-1205-20483-160850

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