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 and temperature. We have utilized intrinsic fluorescence and Fourier transform infrared spectroscopy to determine the structural transitions of encapsulated lysozyme in the range of . 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 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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July 2009
Technical Briefs
Structural Changes in Confined Lysozyme
Eduardo Reátegui,
Eduardo Reátegui
Department of Mechanical Engineering, Biostabilization Laboratory,
University of Minnesota
, Minneapolis, MN
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Alptekin Aksan
Alptekin Aksan
Department of Mechanical Engineering, Biostabilization Laboratory,
e-mail: aaksan@me.umn.edu
University of Minnesota
, Minneapolis, MN
Search for other works by this author on:
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, MNe-mail: aaksan@me.umn.edu
J Biomech Eng. Jul 2009, 131(7): 074520 (4 pages)
Published Online: July 27, 2009
Article history
Received:
November 4, 2008
Revised:
May 1, 2009
Published:
July 27, 2009
Citation
Reátegui, E., and Aksan, A. (July 27, 2009). "Structural Changes in Confined Lysozyme." ASME. J Biomech Eng. July 2009; 131(7): 074520. https://doi.org/10.1115/1.3171565
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