Contact
    Start Publications Lipid-matrix effects on tyrosinase immobilization in Langmuir ...
    ←  Publication Finder
    KSV NIMA

    Lipid-matrix effects on tyrosinase immobilization in Langmuir and Langmuir-Blodgett films

    Year: 2021

    Journal: An. Acad. Bras. Cienc., Volume 93

    Authors: Pereira, Matheus S.; Maximino, Mateus D.; Martin, Cibely S.; Aoki, Pedro H. B.; Oliveira Jr, Osvaldo N.; Alessio, Priscila

    Organizations: Brazilian agency Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq); Brazilian agency Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [2013/14262-7, 2017/15019-0]; Brazilian agency Instituto Nacional de Eletronica Organica (INEO)

    Keywords: Lipid-matrix; tyrosinase; Langmuir-Blodgett; PM-IRRAS; cyclic voltammetry

    The immobilization of the enzyme tyrosinase (Tyr) in lipid matrices can be explored to produce biosensors for detecting polyphenols, which is relevant for the food industry. Herein, we shall demonstrate the importance of the lipid composition to immobilize the enzyme tyrosinase in Langmuir-Blodgett (LB) films. Tyr could be incorporated into Langmuir monolayers of arachidic acid (AA), 1,2-dipalmitoyl-sn-glycero3-phosphocholine (DPPC) and 1,2-dipalmitoyl-sn-glycero-3-phospho-(1'-rac-glycerol) (sodium salt) (DPPG), having as the main effect an expansion in the monolayers. Results from polarization-modulated infrared reflection-absorption spectroscopy (PM-IRRAS) pointed to electrostatic interactions between the charged residues of Try and the lipid headgroups, in addition to changes in the order of lipid chains. The interaction between Tyr and DPPC in Langmuir monolayers can be correlated with the superior performance of DPPC/Tyr LB films used as biosensors to detect catechol by cyclic voltammetry. The molecular-level interactions assessed via PM-IRRAS are therefore believed to drive an immobilization process for Tyr in the lipid LB matrix and may serve as a general criterion to identify matrices that preserve enzyme activity.
    View publication