Related Experiment Video
Updated: Feb 14, 2026

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project
Published on: February 11, 2019
The effects of biological buffers TRIS, TAPS, TES on the stability of lysozyme
Pavani Pannuru1, Anjeeta Rani2, Pannuru Venkatesu2
1Department of Chemical Engineering, National Taiwan University of Science and Technology, 43 Keelung Road, Section 4, Taipei 106-07, Taiwan.
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.
Related Concept Videos
Buffer Effectiveness
The buffer capacity is the amount of acid or base that can be added to a given volume...
Biological Effects of Radiation
Buffers
Buffers: Buffer Capacity
In the graph, pH is plotted as a function of the number of moles of base (Cb) added to a weak...
Phosphate Buffer
Sodium dihydrogen phosphate does not fully dissociate in neutral or acidic solutions. When a strong base, such as sodium hydroxide (NaOH), is introduced into the solution, sodium dihydrogen phosphate...
Buffers: Overview

