Abstract

The aim of the current study was to present the primary protein profile of cow, goat, camel, yak and buffalo milk, along with binary mixtures of these milks through two-dimensional gel electrophoresis coupled with mass spectrometry for detection of specific milks in mixtures. Distributions of α-lactalbumin and/or β-lactoglobulin spots on gel maps were used to detect goat, camel, yak and buffalo milk adulterated with cow milk. Appearance of α-lactalbumin and β-lactoglobulin protein spots were helpful for detection of camel, yak and buffalo milk adulteration with goat milk. αS1-Casein from cow and goat milk was also used to determine camel milk adulteration. In particular, β-lactoglobulin from cow, goat, yak and buffalo milk, and α-lactalbumin from camel milk were useful to detect adulteration of specific milk mixtures at levels as low as 0.5%. These results highlight applicability of this method for characterisation of milk proteome and detection of specific milk in mixtures.

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