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Interaction study of aflatoxin M1 with milk proteins using ATR-FTIR
C G Harshitha1, Neelima Sharma1, Richa Singh1
1Dairy Chemistry Division, NDRI, Karnal, India.
Aflatoxin M1 (AFM1) binds to milk proteins, altering their structure. Attenuated Total Reflectance Fourier-Transform Infrared (ATR-FTIR) spectroscopy and chemometrics revealed specific spectral changes indicating this interaction and conformational shifts.
Area of Science:
- Food Chemistry
- Analytical Chemistry
- Biochemistry
Background:
- Aflatoxin M1 (AFM1), a milk-borne carcinogen, is a metabolite of aflatoxin B1 (AFB1).
- AFM1 is known to interact with milk proteins, but the precise mechanism remains unclear.
- Understanding this interaction is crucial for food safety and dairy product quality.
Purpose of the Study:
- To investigate the interaction mechanism between AFM1 and milk proteins.
- To identify spectral signatures indicative of AFM1-protein binding.
- To elucidate conformational changes in milk protein secondary structure induced by AFM1.
Main Methods:
- Attenuated Total Reflectance Fourier-Transform Infrared (ATR-FTIR) spectroscopy was employed.
- Chemometric analysis, including second-order derivative spectra and Principal Component Analysis (PCA), was utilized.
- Spectral data in the 1700-1600 cm⁻¹ region were analyzed.
Main Results:
- Second-order derivative spectra confirmed the affinity of AFM1 for milk proteins.
- PCA indicated the spectral window of 1700-1600 cm⁻¹ is highly informative for detecting AFM1.
- The study identified spectral changes corresponding to conformational alterations in milk protein secondary structures due to AFM1.
Conclusions:
- ATR-FTIR coupled with chemometrics effectively characterizes AFM1-milk protein interactions.
- AFM1 binding induces measurable changes in the secondary structure of milk proteins.
- This approach offers a sensitive method for detecting AFM1 contamination in milk products.
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