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    Effect of interfering agents for urease immobilized in Langmuir-Blodgett films of controlled molecular architecture

    Year: 2020

    Journal: Thin Solid Films, Volume 704, JUN 30

    Authors: Rodrigues, RT; Nordi, CFS; Siqueira, JR; Caseli, L

    Organizations: FAPESPFundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [2019/03239-0, 2016/01867-6, 2018/17697-0]; FAPEMIGFundacao de Amparo a Pesquisa do Estado de Minas Gerais (FAPEMIG) [APQ-00756-16]; CNPqConselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPQ) [400896/2016-8]

    Keywords: Dioctadecyldimethylammonium bromide; Carbon nanotubes; Extracellular polysaccharides; Langmuir-blodgett films; Urease; Biosensor; Enzyme activity

    Catalytic performance of enzymes confined in lipid Langmuir-Blodgett (LB) films can be tuned if the molecular architecture and environment are controlled. In this paper, nanohybrid LB films constituted of dioctadecyldimethylammonium bromide, algal polysaccharides, carbon nanotubes and urease had its catalytic activity investigated by adding possible interfering ions in the aqueous environment that contained urea in contact with the LB film. Catalytic activity of LB film towards urea hydrolysis was treated as obeying the Michaelis-Menten mechanism and the effect of ascorbate, oxalate, sulfate, phosphate and their respective counterions were measured. While oxalate and ascorbic acid inactivated totally the catalytic activity, sodium, potassium, sulfate and phosphate ions inhibited only partially. Therefore, these experiments gave us insight about the mechanism of enzymes confined in ultrathin films for biosensing.
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