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Study on the Interaction Mechanism Between Linoleic Acid, Myristic Acid and Rice Protein by Spectroscopy
Ligen Wu1, Mouchang Fang1, Anna Wang1,2
1College of Food Science and Engineering, Henan University of Technology, Zhengzhou 450001, China.
Myristic acid (MA) and linoleic acid (LA) interact with rice protein (RP) primarily through electrostatic forces, affecting protein fluorescence. Linoleic acid shows a stronger binding affinity to rice protein.
Area of Science:
- Food Science
- Biochemistry
- Molecular Interactions
Background:
- Myristic acid (MA) and linoleic acid (LA) are common food additives with pharmacological effects.
- The molecular mechanisms of MA and LA interactions with rice protein (RP) are not well understood.
Purpose of the Study:
- To comprehensively characterize the molecular interactions between MA, LA, and RP.
- To determine fluorescence quenching pathways, binding affinities, and forces governing complex formation.
Main Methods:
- UV absorption spectroscopy
- Fluorescence emission spectroscopy (including synchronous and 3D fluorescence)
- Molecular docking simulations
Main Results:
- Both MA and LA induce static quenching of RP fluorescence, primarily via electrostatic forces.
- MA negligibly affects tyrosine fluorescence but reduces tryptophan fluorescence; LA reduces both tyrosine and tryptophan fluorescence.
- Molecular docking shows LA has a higher binding affinity to RP than MA.
Conclusions:
- This study elucidates the interaction mechanisms between RP and MA/LA.
- Findings provide a theoretical basis for developing RP-based products.
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