Xevo g2 xs qtof quadrupole time of flight mass spectrometer

Phenolic compound tentative identification was made according to Fonseca-Hernández et al. [27 (link)]. A chromatographic method was performed on a Waters Acquity UPLC H-Class system (Milford, MA, USA). Chromatographic separation was done at 40 °C with a flow rate of 0.3 mL/min on an Acquity UPLC BEH C18 column (2.1 × 50 mm, 1.7 µm). The mobile phase consisted of two eluent solvents: (A) acetonitrile with 0.3% formic acid and (B) Mili-Q water 0.3%. The gradient elution was as follows: 90% A at 0–1 min, 90–30% A at 1–11 min, 30–90% A at 11–12 min, 90% at 12–15 min. The injection volume was set at 8 µL.
Mass spectrometry (MS) analysis was performed on a Water Xevo G2-XS QToF quadrupole time-of-flight mass spectrometer, with an electrospray ionization (ESI) interface (Milford, MA, USA). The MS acquisition was operated in negative ion mode, with a mass range of m/z 50 to 800. The parameters were: capillary voltage: 2.5 kV, cone voltage: 40 kV, source temperature: 100 °C, desolvation temperature: 250 °C, collision energy: 6.0 eV. MassLynx 4.1 MS software (Milford, MA, USA) was used to process data.

High resolution electrospray ionization
mass spectrometry was performed in the School of Chemistry at the
University of Birmingham on a Waters Xevo G2-XS QTof Quadrupole Time-of-Flight
mass spectrometer.

LC/MS experiments were performed on a Waters ACQUITY UPLC coupled with a Waters Xevo G2-XS Q-TOF (Quadrupole Time-of-Flight) mass spectrometer (Waters Corporation). The MilliporeSigma BIOshell IgG C4 column (1,000 Å, 2.1 × 100 mm, 2.7 μm) was also used for LC/MS peak separation. LC/MS was run in a similar fashion as RP-UPLC (Table 1) with modified mobile phases to be more compatible with mass spectrometry detector. In LC/MS, mobile phase A consists of 0.1% formic acid and 0.025% TFA in LC/MS grade water, whereas mobile phase B consists of 0.1% formic acid and 0.025% TFA in acetonitrile.
Mass spectra were obtained in positive mode by spraying the eluent into the mass spectrometer using an electrospray ionization source. The capillary, source cone, and extraction cone voltages were set at 3 kV, 50 V, and 80 V, respectively. Nitrogen was used as a desolvation gas at a flow rate of 600 L/h. The source and desolvation temperatures were set at 120°C and 400°C, respectively. The instrument was operated in Sensitivity mode and spectra were acquired in an m/z range of 400–3,000. Data acquisition and analysis (deconvolution) were performed with Waters (MassLynx 4.1 software). Protein spectra were deconvoluted to obtain the observed intact protein masses. A uniform Gaussian model was used with width at half height of either 1 or 0.8.