Terahertz-time domain spectroscopy of hydrated casein and washed casein

Authors

  • Dustin Loren Velasco Almanza Institute of Mathematical Sciences and Physics, University of the Philippines Los Baños
  • Lou Serafin Lozada Institute of Mathematical Sciences and Physics, University of the Philippines Los Baños
  • Naoki Yamamoto Jichi Medica University, Japan
  • Keisuke Tominaga Graduate School of Science, Kobe University, Japan

Abstract

Dynamics of hydrated casein was studied at different temperature using terahertz-time domain spectroscopy (TDS). Specifically, the effect of hydration state on unwashed and washed casein was investigated. XRF data showed that washing removed calcium atom from the casein powder. For hydrated samples, the absorbance at 1 THz of the washed casein is lower than the unwashed casein, probably due to the strengthening of the negatively charged κ-casein, which is responsible for the disruption of hydrogen bond network. No significant change was observed in dehydrated samples for both the washed and unwashed casein. Both temperature dependence of the absorbance and the spectral intensity of the imaginary part of the complex permittivity for hydrated samples show protein "dynamical transition" like behavior.

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Published

2020-10-19

How to Cite

[1]
DLV Almanza, LS Lozada, N Yamamoto, and K Tominaga, Terahertz-time domain spectroscopy of hydrated casein and washed casein, Proceedings of the Samahang Pisika ng Pilipinas 38, SPP-2020-3A-02 (2020). URL: https://proceedings.spp-online.org/article/view/SPP-2020-3A-02.

Issue

Section

Condensed Matter and Materials Science (Short Presentations)