The goat whey proteome has been explored in depth via capture with combinatorialpeptide ligand libraries (CPLL) at three different pH values. A total of 452 uniquespecies has been tabulated, a proteome discovery so far unmatched in any single otherinvestigation of milk from any mammalian species. This massive discovery is probablyrelated to: i) the extraordinary load of proteins onto the CPLL beads (i.e. two grams foreach different pH capture) vs. barely 100 μL of beads; ii) the high resolution/high massaccuracy of mass spectral data; and iii) the use of two complementary tools, Mascotand PEAKS, each one contributing to a set of unique protein IDs. Due to the relativepaucity of available protein annotations for goat, only 10% of the identified proteinsbelong to the capra, whereas 52% are specific of sheep and 37% are homologous tothat of bovine milk. This work reports the largest description so far of the goat milkproteome, which has been compared with cow’s milk proteome and would thus help tounderstand the importance of low-abundance proteins with respect to the uniquebiological properties of this nutrient.

Zeus, Aesculapius, Amalthea and the proteome of goat milk

CUNSOLO, VINCENZO;SALETTI, Rosaria;MUCCILLI, VERA;FOTI, Salvatore
2015

Abstract

The goat whey proteome has been explored in depth via capture with combinatorialpeptide ligand libraries (CPLL) at three different pH values. A total of 452 uniquespecies has been tabulated, a proteome discovery so far unmatched in any single otherinvestigation of milk from any mammalian species. This massive discovery is probablyrelated to: i) the extraordinary load of proteins onto the CPLL beads (i.e. two grams foreach different pH capture) vs. barely 100 μL of beads; ii) the high resolution/high massaccuracy of mass spectral data; and iii) the use of two complementary tools, Mascotand PEAKS, each one contributing to a set of unique protein IDs. Due to the relativepaucity of available protein annotations for goat, only 10% of the identified proteinsbelong to the capra, whereas 52% are specific of sheep and 37% are homologous tothat of bovine milk. This work reports the largest description so far of the goat milkproteome, which has been compared with cow’s milk proteome and would thus help tounderstand the importance of low-abundance proteins with respect to the uniquebiological properties of this nutrient.
goat milk proteome; low-abundance proteins; combinatorial peptide ligand; milk allergy; orbitrap tribrid mass spectrometer
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/20.500.11769/17936
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