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Updated: Jan 28, 2026
Detection of Protein Aggregation using Fluorescence Correlation Spectroscopy
Published on: April 25, 2021
Thermal Effects on Biochemical Signatures of UHT, Pasteurized and Domestically Boiled Buffalo Milk Detected by
Hina Ali1, Muhammad Saleem2, Rahat Ullah2
1National Institute of Lasers and Optronics (NILOP), Lehtrar Road, Islamabad, Pakistan. hinali991@hotmail.com.
Abstract:
Thermal treatment of milk is performed to limit bacterial growth and make it safe for human consumption. To increase the shelf life of milk, either ultrahigh temperature (UHT) or pasteurization techniques are employed that destroy the microorganisms. In this study, the synchronous front face fluorescence spectroscopy was employed for comparative study of raw, UHT treated, pasteurized and conventionally boiled milk at 93 °C (domestic boiling). Principal Component analysis clearly showed distinct clustering of UHT milk due to formation of Maillard reaction products. Fluorescence emission peak at 410 nm showed irreversible change in peak intensity attributed to conformational changes in protein due to UHT treatment while pasteurization and domestic boiling showed reversible changes when milk was cooled down to 10 °C. Furthermore, fluorescence emission peaks at 410 nm previously assigned to vitamin A has also been discussed.
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