Differences in physicochemical properties and proteomics analysis of spray- and freeze-dried milk powders from bovine, goat, and horse source
Description
Table S1. Identified milk proteins from bovine, goat, and horse milk powders between spray- and freeze-dried methods.
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The tryptic peptide mixtures were reconstituted using buffer A solution (0.1% formic acid in water) and subjected to EASY-nLC 1000 liquid phase chromatography and Orbitrap Fusion Lumos system (Thermo Fisher Scientific, CA, USA). The peptide mixtures were loaded onto a C18 trapped column (100 µm ×2 cm, 5 µm; Thermo Fisher Scientific), and separated on a C18 analytical column (100 mm×75 µm, 3 µm; Thermo Fisher Scientific) with buffer A and buffer B solution (80% acetonitrile solution of 0.1% (v/v) FA) with flow rate at 300 nL/min. The gradient elution procedure was buffer B from 0% to 10% within 3 min, from 10% to 35% within 45 min, from 35% to 80% within 26 min, and to 100% within 1 min, and final holding at 100% for 15 min. For DDA analysis, the Orbitrap Fusion Lumos MS was run in positive ion mode with parent ions range of 350 to 1,800 m/z. Automatic switching between MS and MS/MS was set. The parameters for MS were set as follows: resolution, 60,000; AGC target, 400,000; Maximum injection time: 50ms; Exclusion duration, 40s. The top 20 most abundant precursor ions with charge ≥2 was screened from the mass spectral scans and fragmented by high-energy collision dissociation. The parameters of secondary mass spectrometry were as follows: normalized collision energy, 27ev; Resolution, 15,000; AGC target of 50,000; Maximum injection time, 50 ms.