Combining proteomic tools to characterize the protein fraction of llama ([i]Lama glama[/i]) milk
| Autor: | Saadaoui, Besma, BIANCHI, Leonardo, Henry, Celine, Miranda, Guy, Martin, Patrice, Cebo, Christelle |
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| Přispěvatelé: | Faculté des Sciences de Gabès, Université de Gabès, Génétique Animale et Biologie Intégrative (GABI), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, MICrobiologie de l'ALImentation au Service de la Santé (MICALIS), AgroParisTech-Institut National de la Recherche Agronomique (INRA) |
| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Proteomics
Spectrometry Mass Electrospray Ionization Mass spectrometry [SDV]Life Sciences [q-bio] Liquid chromatography food and beverages Milk proteins Milk fluids and secretions Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Camelids Animals Electrophoresis Polyacrylamide Gel Camelids New World Chromatography High Pressure Liquid |
| Zdroj: | Electrophoresis Electrophoresis, Wiley-VCH Verlag, 2014, 35 (10), pp.1406-1418. ⟨10.1002/elps.201300383⟩ |
| ISSN: | 0173-0835 1522-2683 |
| DOI: | 10.1002/elps.201300383⟩ |
| Popis: | Llamas belong to the Camelidae family along with camels. While dromedary camel milk has been broadly characterized, data on llama milk proteins are scarce. The objective of this study was thus to investigate the protein composition of llama milk. Skimmed llama milk proteins were first characterized by a 2D separation technique coupling RP-HPLC in the first dimension with SDS-PAGE in the second dimension (RP-HPLC/SDS-PAGE). Llama milk proteins, namely caseins (αs1 -, αs2 -, β-, and κ-caseins), α-lactalbumin, lactoferrin, and serum albumin, were identified using PMF. Llama milk proteins were also characterized by online LC-ESI-MS analysis. This approach allowed attributing precise molecular masses for most of the previously MS-identified llama milk proteins. Interestingly, α-lactalbumin exhibits distinct chromatographic behaviors between llama and dromedary camel milk. De novo sequencing of the llama α-lactalbumin protein by LC coupled with MS/MS (LC-MS/MS) showed the occurrence of two amino acid substitutions (R62L/I and K89L/I) that partly explained the higher hydrophobicity of llama α-lactalbumin compared with its dromedary counterpart. Taken together, these results provide for the first time a thorough description of the protein fraction of Lama glama milk. |
| Databáze: | OpenAIRE |
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