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Analyses on the binding interaction between rice glutelin and conjugated linoleic acid by multi-spectroscopy and
Yujia Xu1, Taotao Dai1, Kechou Huang1
1State Key Laboratory of Food Science and Technology, Nanchang University, No. 235 Nanjing East Road, Nanchang, 330047 China.
Journal of Food Science and Technology
|March 4, 2020
Summary
Researchers explored how rice protein interacts with conjugated linoleic acid (CLA). Findings reveal spontaneous binding driven by hydrogen bonds, altering protein structure and providing insights into plant protein-fatty acid interactions.
Area of Science:
- Food science and nutrition
- Biochemistry
- Protein-lipid interactions
Background:
- Understanding plant protein and bioactive lipid interactions is crucial.
- Limited knowledge exists on rice protein and conjugated linoleic acid (CLA) interactions.
Purpose of the Study:
- To elucidate the interaction mechanism between rice glutelin (RG) and CLA.
- To characterize the binding forces and conformational changes involved.
Main Methods:
- Intrinsic fluorescence quenching spectroscopy
- Thermodynamic analysis
- Circular dichroism spectroscopy
- Synchronous fluorescence spectroscopy
- Computational docking
Main Results:
- Conjugated linoleic acid (CLA) quenched rice glutelin (RG) intrinsic fluorescence, indicating binding.
- Binding was spontaneous, driven by hydrogen bonds, with one binding site.
- Surface hydrophobicity decreased, and α-helical content increased, indicating conformational changes.
Conclusions:
- Rice glutelin (RG) and conjugated linoleic acid (CLA) interact spontaneously.
- Hydrogen bonds are the primary force, leading to conformational alterations in RG.
- This study enhances understanding of plant protein-fatty acid interactions.
