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

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...

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Detalles Bibliográficos
Autores: Pereira, Matheus S. [UNESP], Maximino, Mateus D. [UNESP], Martin, Cibely S. [UNESP], Aoki, Pedro H. B. [UNESP], Oliveira, Osvaldo N., Alessio, Priscila [UNESP]
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2021
País:Brasil
Institución:Universidade Estadual Paulista (UNESP)
Repositorio:Repositório Institucional da UNESP
Idioma:inglés
OAI Identifier:oai:repositorio.unesp.br:11449/207496
Acceso en línea:http://dx.doi.org/10.1590/0001-3765202120200019
http://hdl.handle.net/11449/207496
Access Level:acceso abierto
Palabra clave:Cyclic voltammetry
Langmuir-Blodgett
Lipid-matrix
PM-IRRAS
Tyrosinase
Descripción
Sumario: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-glycero-3-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.