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Proteomic profiling of camel and cow milk proteins under heat treatment
Imène Felfoul1, Julien Jardin2, Frédéric Gaucheron2
1Laboratoire Analyses, Valorisation et Sécurité des Aliments, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, Route Soukra, Sfax 3038, Tunisia.
Insights
Heat treatment of cow and camel milk affects specific whey proteins, with camel alpha-lactalbumin and peptidoglycan recognition protein disappearing, while casein fractions remain intact in both milk types.
Area of Science:
- Food Science
- Biochemistry
- Dairy Science
Background:
- Milk proteins are crucial for nutrition and functionality.
- Heat treatment is commonly used in dairy processing but can alter protein structure and function.
- Understanding the impact of heat on camel and cow milk proteins is important for optimizing processing and product quality.
Purpose of the Study:
- To identify and compare the effects of heat treatment on cow and camel milk proteins.
- To determine the stability of different protein fractions (whey vs. casein) under thermal stress.
Main Methods:
- Proteins in cow and camel milk were analyzed before and after heat treatment (80°C for 60 min).
- Techniques used included monodimensional electrophoresis, SDS-PAGE, LC/MS, and LC-MS/MS.
- Protein identification was performed using a UniProt database.
Main Results:
- Heat treatment significantly diminished camel serum albumin and eliminated camel alpha-lactalbumin and peptidoglycan recognition protein.
- Cow milk alpha-lactalbumin and beta-lactoglobulin were not significantly detected after heating.
- Casein fractions remained intact in both milk types after heat treatment.
- Camel and bovine whey proteins were affected by the heat treatment.
Conclusions:
- Heat treatment at 80°C for 60 min significantly alters specific whey proteins in both camel and cow milk.
- Casein proteins exhibit greater heat stability compared to whey proteins in both species.
- These findings provide insights into the differential heat sensitivity of milk proteins, aiding in dairy processing optimization.
Abstract:
Cow and camel milk proteins before and after heat treatment at 80°C for 60min were identified using LC/MS and LC-MS/MS following monodimensional electrophoresis. The database used for the identification of camel and cow proteins was set from http://www.uniprot.org/. The obtained results showed that, after heating, camel milk at 80°C for 60min, camel α-lactalbumin (α-la) and peptidoglycan recognition protein (PGRP) were not detected while camel serum albumin (CSA) was significantly diminished. When heating cow milk at 80°C for 60min, α-lactalbumin (α-la) and β-lactoglobulin (β-lg) were not significantly detected. Moreover, 19 protein bands from SDS-PAGE were analyzed and a total of 45 different proteins were identified by LC-MS/MS. Casein fractions were kept intact under a heat treatment of 80°C during 60min of both camel and cow milks. Camel and bovine whey proteins were affected by a heat treatment of 80°C for 60min.
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