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Peptide Identification Using Tandem Mass Spectrometry

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...

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Peptide-Based Quantitative Analysis of Rapeseed Storage Proteins and Their Isoforms by Targeted LC-MS/MS.

Kasper Engholm-Keller¹, Peter Fog Lihme¹, Poul-Erik Jensen¹

¹Department of Food Science, Faculty of Science, University of Copenhagen, Rolighedsvej 26, 1958Frederiksberg, Denmark.

Journal of Agricultural and Food Chemistry

|April 15, 2026

Summary

This summary is machine-generated.

We developed a targeted LC-MS/MS method to quantify rapeseed (Brassica napus) proteins, napin and cruciferin. This method reveals distinct protein profiles in various rapeseed ingredients, aiding in optimizing their food applications.

Keywords:

cruciferin isoforms napin quantitation selected reaction monitoring

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Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Published on: August 17, 2015

Area of Science:

Food Science
Analytical Chemistry
Biochemistry

Background:

Rapeseed (Brassica napus) is a significant protein source, with napin and cruciferin as major storage proteins.
Accurate quantification of these proteins and their isoforms is crucial for food ingredient development and application optimization.
Understanding protein heterogeneity in rapeseed is key to unlocking its full potential in the food industry.

Purpose of the Study:

To develop and validate a targeted LC-MS/MS method for quantifying napin and cruciferin isoforms in rapeseed.
To apply the method for analyzing protein composition in various rapeseed-derived samples.
To demonstrate the method's capability in resolving protein heterogeneity for quality control and product development.

Main Methods:

Development of a selected reaction monitoring (SRM) LC-MS/MS method.
Utilized surrogate matrix-matched calibration for peptide-based quantitative analysis.
Analyzed seven napin and six cruciferin isoforms across different rapeseed protein matrices.

Main Results:

The method achieved a lower limit of quantification (LLOQ) ranging from 0.60–29 nM.
Observed variations in accuracy for cruciferin quantification due to trypsin hydrolysis efficiency.
Successfully quantified napin and cruciferin isoforms in isolates, extracts, and commercial rapeseed protein isolates.
Revealed distinct protein compositions and isoform distributions among the analyzed samples.

Conclusions:

The developed targeted LC-MS/MS method is effective for quantifying rapeseed napin and cruciferin isoforms.
The method can resolve protein heterogeneity, providing insights into sample composition.
This approach serves as a valuable tool for characterizing rapeseed protein ingredients and optimizing their functional properties in food applications.