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Int. J. Mol. Sci. 2017, 18(4), 721; doi:10.3390/ijms18040721

Proteomic Profiling Comparing the Effects of Different Heat Treatments on Camel (Camelus dromedarius) Milk Whey Proteins

1
Proteomics Resource Unit, Obesity Research Center, College of Medicine, King Saud University, P.O. Box 2925(98), Riyadh 11461, Saudi Arabia
2
The National Center For Genomic Technology (NCGT), Life Science and Environment Research Institute, King Abdulaziz City for Science and Technology (KACST), P.O. Box 6086, Riyadh 11461, Saudi Arabia
3
National Center for Biotechnology, Life Science and Environment Research Institute, King Abdulaziz City for Science and Technology (KACST), P.O. Box 6086, Riyadh 11461, Saudi Arabia
4
Department of Medicine, College of Medicine, King Saud University, P.O. Box 2925(38), Riyadh 11461, Saudi Arabia
*
Author to whom correspondence should be addressed.
Academic Editors: Miguel Herrero, Carolina Simó and and Virginia Garcia-Cañas
Received: 16 January 2017 / Revised: 16 March 2017 / Accepted: 22 March 2017 / Published: 28 March 2017
(This article belongs to the Special Issue New Foodomics Approaches in Food Science)
View Full-Text   |   Download PDF [1002 KB, uploaded 30 March 2017]   |  

Abstract

Camel milk is consumed in the Middle East because of its high nutritional value. Traditional heating methods and the duration of heating affect the protein content and nutritional quality of the milk. We examined the denaturation of whey proteins in camel milk by assessing the effects of temperature on the whey protein profile at room temperature (RT), moderate heating at 63 °C, and at 98 °C, for 1 h. The qualitative and quantitative variations in the whey proteins before and after heat treatments were determined using quantitative 2D-difference in gel electrophoresis (DIGE)-mass spectrometry. Qualitative gel image analysis revealed a similar spot distribution between samples at RT and those heated at 63 °C, while the spot distribution between RT and samples heated at 98 °C differed. One hundred sixteen protein spots were determined to be significantly different (p < 0.05 and a fold change of ≥1.2) between the non-heated and heated milk samples. Eighty protein spots were decreased in common in both the heat-treated samples and an additional 25 spots were further decreased in the 98 °C sample. The proteins with decreased abundance included serum albumin, lactadherin, fibrinogen β and γ chain, lactotransferrin, active receptor type-2A, arginase-1, glutathione peroxidase-1 and, thiopurine S, etc. Eight protein spots were increased in common to both the samples when compared to RT and included α-lactalbumin, a glycosylation-dependent cell adhesion molecule. Whey proteins present in camel milk were less affected by heating at 63 °C than at 98 °C. This experimental study showed that denaturation increased significantly as the temperature increased from 63 to 98 °C. View Full-Text
Keywords: camel milk; whey protein; heat treatment; 2D-DIGE; proteomics; matrix-assisted laser desorption/ionization-Time of Flight (MALDI-TOF) camel milk; whey protein; heat treatment; 2D-DIGE; proteomics; matrix-assisted laser desorption/ionization-Time of Flight (MALDI-TOF)
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Benabdelkamel, H.; Masood, A.; Alanazi, I.O.; Alzahrani, D.A.; Alrabiah, D.K.; AlYahya, S.A.; Alfadda, A.A. Proteomic Profiling Comparing the Effects of Different Heat Treatments on Camel (Camelus dromedarius) Milk Whey Proteins. Int. J. Mol. Sci. 2017, 18, 721.

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