The effects of biological buffers TRIS, TAPS, TES on the stability of lysozyme

  • Int J Biol Macromol. 2018 Jun;112:720-727. doi: 10.1016/j.ijbiomac.2018.01.203.
Pavani Pannuru  1 ,  Anjeeta Rani  2 ,  Pannuru Venkatesu  2 ,  Ming-Jer Lee  3
Affiliations
  • 1. Department of Chemical Engineering, National Taiwan University of Science and Technology, 43 Keelung Road, Section 4, Taipei 106-07, Taiwan.
  • 2. Department of Chemistry, University of Delhi, Delhi 110 007, India.
  • 3. Department of Chemical Engineering, National Taiwan University of Science and Technology, 43 Keelung Road, Section 4, Taipei 106-07, Taiwan. Electronic address: [email protected].
PMID: 29425867 DOI: 10.1016/j.ijbiomac.2018.01.203
Abstract

To explore the mechanism of lysozyme stabilization in buffer system, we have investigated the interactions between lysozyme and the biological buffers (TRIS, TAPS, and TES) using spectroscopic techniques, including ultraviolet-visible (UV-Vis), fluorescence, thermal fluorescence, dynamic light scattering (DLS), Fourier transform infrared spectroscopy (FTIR) and circular dichroism (CD) spectroscopy. From the series of spectroscopic studies, it is found that the native structure of the protein remains intact in the different concentrations (0.05, 0.1, 0.25, 0.5, and 1.0M) of the biological buffer aqueous solutions at pH7.0. Moreover, all these three investigated buffers are able to protect lysozyme against thermal denaturation, particularly in high concentration (1.0M) of the buffer aqueous solutions.

Keywords
Biological buffers; Enzyme stability; Lysozyme.
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