| Literature DB >> 27596405 |
Imène Felfoul1, Julien Jardin2, Frédéric Gaucheron2, Hamadi Attia1, M A Ayadi3.
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.Entities:
Keywords: Camel milk; Cow milk; Electrophoresis; Heat treatment; LC/MS; LC–MS/MS
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Year: 2016 PMID: 27596405 DOI: 10.1016/j.foodchem.2016.08.007
Source DB: PubMed Journal: Food Chem ISSN: 0308-8146 Impact factor: 7.514