Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2434221 | International Dairy Journal | 2014 | 6 Pages |
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.