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(Reference retrieved automatically from SciELO through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
MATHEUS S. PEREIRA [1] ; MATEUS D. MAXIMINO [2] ; CIBELY S. MARTIN [3] ; PEDRO H.B. AOKI [4] ; OSVALDO N. OLIVEIRA JR [5] ; PRISCILA ALESSIO [6]
Total Authors: 6
Affiliation:
[1] Universidade Estadual Paulista/UNESP. Faculdade de Ciências e Tecnologia - Brasil
[2] Universidade Estadual Paulista/UNESP. Faculdade de Ciências e Tecnologia - Brasil
[3] Universidade Estadual Paulista/UNESP. Faculdade de Ciências e Tecnologia - Brasil
[4] Universidade Estadual Paulista/UNESP. Faculdade de Ciências e Letras - Brasil
[5] Universidade de São Paulo/USP. Instituto de Física de São Carlos - Brasil
[6] Universidade Estadual Paulista/UNESP. Faculdade de Ciências e Tecnologia - Brasil
Total Affiliations: 6
Document type: Journal article
Source: Anais da Academia Brasileira de Ciências; v. 93, n. 1 2021-03-26.
Abstract

Abstract 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. (AU)

FAPESP's process: 13/14262-7 - Nanostructured films from biologically-relevant materials
Grantee:Osvaldo Novais de Oliveira Junior
Support Opportunities: Research Projects - Thematic Grants
FAPESP's process: 17/15019-0 - Combination of confocal fluorescence microscopy and surface-enhanced Raman scattering techniques: interaction, detection, and quantification of molecules of interest in biomimetic system.
Grantee:Cibely da Silva Martin Sonvesso
Support Opportunities: Scholarships in Brazil - Post-Doctoral