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Technical Briefs

Structural Changes in Confined Lysozyme

[+] Author and Article Information
Eduardo Reátegui

Department of Mechanical Engineering, Biostabilization Laboratory, University of Minnesota, Minneapolis, MN

Alptekin Aksan

Department of Mechanical Engineering, Biostabilization Laboratory, University of Minnesota, Minneapolis, MNaaksan@me.umn.edu

J Biomech Eng 131(7), 074520 (Jul 27, 2009) (4 pages) doi:10.1115/1.3171565 History: Received November 04, 2008; Revised May 01, 2009; Published July 27, 2009

Proteins and enzymes can be encapsulated in nanoporous gels to develop novel technologies for biosensing, biocatalysis, and biosynthesis. When encapsulated, certain macromolecules retain high levels of activity and functionality and are more resistant to denaturation when exposed to extremes of pH and temperature. We have utilized intrinsic fluorescence and Fourier transform infrared spectroscopy to determine the structural transitions of encapsulated lysozyme in the range of 120°C<T<100°C. At cryogenic temperatures encapsulated lysozyme did not show cold denaturation, instead became more structured. However, at high temperatures, the onset of heat denaturation of confined lysozyme was reduced by 15°C when compared with lysozyme in solution. Altered dynamics of the solvent and pore size distribution of the nanopores in the matrix appear to be key factors influencing the decrease in the denaturation temperature.

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Copyright © 2009 by American Society of Mechanical Engineers
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Figures

Grahic Jump Location
Figure 1

Temperature-induced secondary structure changes in encapsulated LYS

Grahic Jump Location
Figure 2

Thermal denaturation behavior of LYS in solution and in silica gel (IF spectroscopy)

Grahic Jump Location
Figure 3

Changes in the intensity of surface silanol groups; (insert) changes in the silanol stretch band during heating

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