Advanced search
Start date
Betweenand
Related content
(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Acylated Carrageenan Changes the Physicochemical Properties of Mixed Enzyme-Lipid Ultrathin Films and Enhances the Catalytic Properties of Sucrose Phosphorylase Nanostructured as Smart Surfaces

Full text
Author(s):
Rocha, Jefferson M. [1] ; Pavinatto, Adriana [2] ; Nobre, Thatyane M. [2] ; Caseli, Luciano [1]
Total Authors: 4
Affiliation:
[1] Univ Fed Sao Paulo, Inst Environm Chem & Pharmaceut Sci, BR-04021001 Diadema, SP - Brazil
[2] Univ Sao Paulo, Sao Carlos Phys Inst, Rua Sao Nicolau 210, BR-13566590 Sao Carlos, SP - Brazil
Total Affiliations: 2
Document type: Journal article
Source: Journal of Physical Chemistry B; v. 120, n. 24, p. 5359-5366, JUN 23 2016.
Web of Science Citations: 8
Abstract

Control over the catalytic activity of enzymes is important to construct biosensors with a wide range of detectability and higher stability. For this, immobilization of enzymes on solid supports as nanostructured films is a current approach that permits easy control of the molecular architecture as well as tuning of the properties. In this article, we employed acylated carrageenan (AC) mixed with phospholipids at the air water interface to facilitate the adsorption of the enzyme sucrose phosphorylase (SP). AC stabilized the adsorption of SP at the phospholipid monolayer, as detected by tensiornetry, by which thermodynamic parameters could be inferred from the surface pressure area isotherm. Also, infrared spectroscopy applied in situ over the monolayer showed that the AC-phospholipid system not only permitted the enzyme to be adsorbed but also helped conserve its secondary structure. The mixed monolayers were then transferred onto solid supports as Langmuir-Blodgett (LB) films and investigated with transfer ratio, quartz crystal microbalance, fluorescence spectroscopy, and atomic force microscopy. The enzyme activity of the LB film was then determined, revealing that although there was an expected reduction in activity in relation to the homogeneous environment the activity could be better preserved after 1 month, revealing enhanced stability. (AU)

FAPESP's process: 15/23446-0 - Smart surfaces: nanostructured and bioinspired systems for the investigation of molecular interactions in membrane models and for the production of devices for biosensors and environmental analysis
Grantee:Luciano Caseli
Support Opportunities: Regular Research Grants