Data on the peptide mapping and MS identification for phosphorylated peptide.

Area of Science:

• Food Science
• Biochemistry
• Analytical Chemistry

Background:

• Ovalbumin, a major protein in egg white, undergoes modifications like phosphorylation.
• Understanding phosphorylation is crucial for food processing and allergenicity studies.
• Dry-heating treatment can alter protein structures and functionalities.

Purpose of the Study:

• To identify and quantify specific phosphorylation sites on ovalbumin.
• To determine the degree of phosphorylation (DSP) after dry-heating treatment.
• To demonstrate a method for DSP calculation using mass spectrometry data.

Main Methods:

• Utilized Fourier transform ion cyclotron mass spectrometry (FTICR MS) for high-resolution analysis.
• Employed peptides mapping to identify modified peptide sequences.
• Monitored mass shifts in FTICR MS spectra to detect phosphorylated peptides.
• Quantified DSP based on the relative abundance of phosphorylated and non-phosphorylated peptides.

Main Results:

• Successfully identified and quantified phosphorylated ovalbumin peptides.
• Determined specific phosphorylation sites on the ovalbumin protein.
• Established a method for calculating the degree of phosphorylation (DSP) using FTICR MS data.
• Demonstrated the impact of dry-heating treatment on ovalbumin phosphorylation.

Conclusions:

• High-resolution mass spectrometry is effective for identifying and quantifying protein phosphorylation.
• The developed method allows for precise DSP determination in ovalbumin.
• Findings provide insights into the structural changes of ovalbumin during food processing.
• This research contributes to a better understanding of protein modification in food systems.