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A Method to Analyze the Protein Denaturation of Whole Quail Egg Based on in situ NMR and MRI

  • Chenyang Li , Xiu Zang , Bei-Wei Zhu and Mingqian Tan EMAIL logo
Published/Copyright: February 28, 2017

Abstract

The paper aims to study the change of protein denaturation in whole quail egg during heating using in situ nuclear magnetic resonance (NMR) and magnetic resonance imaging (MRI) techniques. The NMR relaxometry demonstrated that the protein denaturation occurred within 64–66 °C. The quail eggs after 8 min heating at 65 °C were successfully recognized by NMR combined with principal component analysis due to protein denaturation. The protein denaturation dynamics study revealed that the protein denaturation occurred at 8, 6, 4, 2 min for the quail eggs heated at 65, 70, 75, 100 °C, respectively. In addition, the protein denaturation of quail egg was also detected by the T1 weighted MRI imaging, confirming that the dramatic changes occurred at 8 min when the eggs were heated at 65 °C. All these results showed that the NMR with MRI provided an effective way to assess the protein denaturation of quail eggs.

Funding statement: This work was supported by the National Key Scientific Instrument and Equipment Development Project of China (2013YQ17046307), the National Nature Science Foundation of China(31401520, 31401519), and the National Key Technology Research and Development Program of China in 12th Five-Year Plan (2014BAD04B09).

Abbreviations and Nomenclature

LF-NMR

Low field nuclear magnetic resonance

MRI

Magnetic resonance imaging

3D

Three dimensional

DSC

Differential scanning calorimetry

KGM

Konjac glucomannan

PTFE

Polytetrafluoroethylene

CPMG

Carr-Purcell-Meiboom-Gill

TE

Echo time

TR

Repetition time

FOV

Field of view

PCA

Principal component analysis

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Published Online: 2017-2-28

© 2017 Walter de Gruyter GmbH, Berlin/Boston

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