Publication
Title
Hydration and confinement effects on horse heart myoglobin adsorption in mesoporous
Author
Abstract
Despite the intensive research on protein adsorption in mesoporous materials, the effect of (de)hydration and confinement on the adsorbed proteins stability and activity is poorly understood. In this paper, we study the effect of differences in structural features (pore size) and drying time on the adsorption and structural stability of horse heart myoglobin (hhMb) on mesoporous titanium dioxide. Infrared spectroscopy (DRIFT) and thermal analysis (TGA) coupled to a quadrupole mass spectrometer (TGAMS) were used to evaluate the impact of the confinement in different pores and hydration on the myoglobin secondary structure. Electron paramagnetic spectroscopy (EPR) was applied to identify the changes in the heme and its close surrounding. The peroxidase-like activity of myoglobin toward 2,2′-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) in the presence of hydrogen peroxide allowed us to detect changes in the protein activity after adsorption in pores with different sizes and drying for different periods of time. The results show a clear effect of the pore size and drying time on the secondary structure of hhMb, which is confirmed by differences induced in the catalytic activity of the adsorbed proteins. Therefore, we recommend evaluating the effect of both hydration and confinement in future applications involving biomolecule adsorption in porous matrices.
Language
English
Source (journal)
The journal of physical chemistry: C : nanomaterials and interfaces. - Washington, D.C., 2007, currens
The journal of physical chemistry: C : nanomaterials and interfaces. - Washington, D.C., 2007, currens
Publication
Washington, D.C. : 2018
ISSN
1932-7447 [print]
1932-7455 [online]
Volume/pages
122 :41 (2018) , p. 23393-23404
ISI
000448087900018
Full text (Publisher's DOI)
Full text (open access)
Full text (publisher's version - intranet only)
UAntwerpen
Faculty/Department
Research group
Project info
Targeted immobilization of globin proteins on porous materials for electrochemical applications.
Towards new approaches in bioelectrochemistry – Targeted immobilization of globins on porous materials.
Publication type
Subject
Affiliation
Publications with a UAntwerp address
External links
Web of Science
Record
Identification
Creation 08.10.2018
Last edited 24.10.2021
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