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Interfacial properties of pectinase forming ultrathin films from a saline solution

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Author(s):
Rodrigues, Raul Torres ; Caseli, Luciano
Total Authors: 2
Document type: Journal article
Source: Thin Solid Films; v. 753, p. 5-pg., 2022-07-01.
Abstract

Pectinase, an enzyme with poor surface activity, was adsorbed from a saline aqueous subphase at the water interface through the salting-out effect. Tensiometry measurements confirmed the formation of stable films at the interface, and surface potential-area isotherms confirmed the orientation of the enzyme dipoles at the interface. Polarization modulation reflection-absorption infrared spectroscopy provided information on the secondary structure of the enzyme, which showed negligible loss of its native conformation, with a majority presence of beta-sheets. We did not observe relevant formation of aggregates by means of cycles of compression-expansion as well as through Brewster Angle Microscopy. The floating enzyme monolayer could be transferred to solid supports as revealed with nanogravimmetry and fluorescence spectroscopy. (AU)

FAPESP's process: 18/22091-1 - Langmuir and Langmuir-Blodgett films of lipid containing pectinase for pectin sensors
Grantee:Raul Torres Rodrigues
Support Opportunities: Scholarships in Brazil - Master
FAPESP's process: 14/50869-6 - INCT 2014: on Organic Electronics
Grantee:Roberto Mendonça Faria
Support Opportunities: Research Projects - Thematic Grants
FAPESP's process: 19/03239-0 - Nanostructured interfaces for the investigation of bioactive substances in cell membrane models and for the construction of optoelectronic devices
Grantee:Luciano Caseli
Support Opportunities: Regular Research Grants
FAPESP's process: 18/22214-6 - Towards a convergence of technologies: from sensing and biosensing to information visualization and machine learning for data analysis in clinical diagnosis
Grantee:Osvaldo Novais de Oliveira Junior
Support Opportunities: Research Projects - Thematic Grants