Authors:
A. K. Bordbar Laboratory of Biophysical Chemistry, Department of Chemistry, University of Isfahan, Isfahan, Iran, 81746-73441

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R. Hosseinzadeh Laboratory of Biophysical Chemistry, Department of Chemistry, University of Isfahan, Isfahan, Iran, 81746-73441
Food and Chemical Analysis Research Laboratory, Jahad-E-Daneshgahi, Urmia University, Urmia, Iran

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M. H. Norozi Laboratory of Biophysical Chemistry, Department of Chemistry, University of Isfahan, Isfahan, Iran, 81746-73441

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Abstract

The interaction of a series of n-alkyl trimethyl ammonium bromides (C12, C14 and C16) with egg white lysozyme have been studied using fluorescence and UV-Vis spectroscopies and isothermal titration calorimetry (ITC). The trend of variation of molar absorptivity at 281 nm, quantum yields (λex=281 nm) and heat of interaction with respect to surfactant concentration, were measured. The spectrophotometric results show that the hydrophobic interactions have a major role in denaturation mechanism and it would be increased with increasing in hydrocarbon tail length of surfactant. The ITC results indicated the two-step mechanism for unfolding of lysozyme due to its interaction with surfactants.

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Journal of Thermal Analysis and Calorimetry
Language English
Size A4
Year of
Foundation
1969
Volumes
per Year
1
Issues
per Year
24
Founder Akadémiai Kiadó
Founder's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
Publisher Akadémiai Kiadó
Springer Nature Switzerland AG
Publisher's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
CH-6330 Cham, Switzerland Gewerbestrasse 11.
Responsible
Publisher
Chief Executive Officer, Akadémiai Kiadó
ISSN 1388-6150 (Print)
ISSN 1588-2926 (Online)

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