FTIR‐ATR Study of pH Effects on Egg Albumin Secondary Structure

Abstract

The pH effects on the secondary structures of egg albumin were investigated using Fourier transform infrared–attenuated total reflection (FTIR‐ATR) technique with a single‐bounce diamond crystal. The albumin was first denatured in a series of solutions with pH ranging from 1 to 12. The albumin film was then cast on the ATR crystal from the albumin solution for the IR spectrum collection. Significant secondary structure spectral differences were observed for these films. The findings are presented in terms of the shape and position of the albumin amide I band between 1600 and 1700 cm⁻¹.

Keywords:

• Acid/base denaturation
• albumin secondary structure
• FTIR-ATR

Acknowledgments

We would like to thank Dr. Genesh Naik for helping with the SDS‐PAGE measurements. We would also like to thank our students, Richard Davis, Zach Reigart, Greg Aaron, and Alicia Stallard, for contributing to the project through their lab work.

Notes

The authors were invited to contribute this paper to a special issue of the journal entitled “Undergraduate Research and Education in Spectroscopy.” This special issue was organized by Associate Editor David J. Butcher, Professor of Chemistry at Western Carolina University, Cullowhee, North Carolina, USA.