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

Adsorption and enzyme activity of sucrose phosphorylase on lipid Langmuir and Langmuir-Blodgett films

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Author(s):
Rocha, Jefferson Muniz [1] ; Caseli, Luciano [1]
Total Authors: 2
Affiliation:
[1] Univ Fed Sao Paulo, Inst Environm Chem & Pharmaceut Sci, Diadema, SP - Brazil
Total Affiliations: 1
Document type: Journal article
Source: COLLOIDS AND SURFACES B-BIOINTERFACES; v. 116, p. 497-501, APR 1 2014.
Web of Science Citations: 8
Abstract

The production of bioelectronic devices, including biosensors, can be conducted using enzymes immobilized in ultrathin solid films, for which preserving the enzymatic catalytic activity is crucial for optimal performance. In this sense, nanostructured films that allow for control over molecular architectures are of interest. In this paper, we investigate the adsorption of sucrose phosphorylase onto Langmuir monolayers of the phospholipid dimyristoylphosphatidic acid, which caused the surface pressure isotherms to expand. With polarization-modulated infrared reflection absorption spectroscopy (PM-IRRAS), the amide bands from the enzyme could be identified, with the C-N and C=O dipole moments lying parallel to the air-water interface. Structuring of the enzyme into an alpha-helix was noted, and this structure was preserved when the mixed enzyme-phospholipid monolayer was transferred in the form of a Langmuir-Blodgett (LB) film. The latter was demonstrated with measurements of the catalytic activity of sucrose phosphorylase, which presented the highest enzyme activity for multilayer LB film. The approach presented in this study not only allows for optimized catalytic activity toward sucrose but also permits to explain why certain film architectures exhibit superior performance. (C) 2014 Elsevier B.V. All rights reserved. (AU)

FAPESP's process: 13/10213-1 - Interaction of bioactive materials in ultrathin films organized in models for biointerfaces models for investigation of molecular recognition processes and associated molecular mechanisms
Grantee:Luciano Caseli
Support Opportunities: Regular Research Grants