Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

7.0K
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...
7.0K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Impact of phosphatidylcholine and galactolipids on the oxidative stability of commercial microalgal oil containing tocopherols.

Food chemistry·2026
Same author

Characterization of the reactions of β-lactoglobulin and potato proteins with chlorogenic acid using a UHPLC-ESI-MS approach.

Food research international (Ottawa, Ont.)·2026
Same author

Bacterial lipoxygenases for fatty acid oxyfunctionalization: advances and future directions.

Applied microbiology and biotechnology·2026
Same author

Generation of Koku-Related Peptides Using Gamma-Glutamyl Transpeptidase Post-Treatment in Porcine Liver Hydrolyzates.

International journal of molecular sciences·2026
Same author

Identification of Glycosylated and Prenylated (Iso)flavonoids Using cIMS-MS.

Analytical chemistry·2026
Same author

Natural Strategies to Preserve Alcohol-Free Beer: Phenolamide Dimers with Anti-Yeast Potential.

Journal of agricultural and food chemistry·2026

Related Experiment Video

Updated: Sep 30, 2025

Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry
06:09

Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry

Published on: July 31, 2011

23.1K

A method to identify and quantify the complete peptide composition in protein hydrolysates.

Gijs J C Vreeke1, Wouter Lubbers1, Jean-Paul Vincken1

  • 1Laboratory of Food Chemistry, Wageningen University & Research, P.O. 17, 6708 AA, Wageningen, the Netherlands.

Analytica Chimica Acta
|March 18, 2022
PubMed
Summary

This study presents a structured method for reproducible peptide annotation in food proteomics. The approach ensures high consistency in identifying and quantifying peptides, even in complex mixtures.

Keywords:
DigestionFood peptidesPeptide release kineticsPeptidomicsQuantitative proteomicsUNIFI

More Related Videos

Quantitative Proteomics Using Reductive Dimethylation for Stable Isotope Labeling
11:53

Quantitative Proteomics Using Reductive Dimethylation for Stable Isotope Labeling

Published on: July 1, 2014

16.4K
Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders
11:14

Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders

Published on: April 14, 2015

16.2K

Related Experiment Videos

Last Updated: Sep 30, 2025

Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry
06:09

Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry

Published on: July 31, 2011

23.1K
Quantitative Proteomics Using Reductive Dimethylation for Stable Isotope Labeling
11:53

Quantitative Proteomics Using Reductive Dimethylation for Stable Isotope Labeling

Published on: July 1, 2014

16.4K
Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders
11:14

Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders

Published on: April 14, 2015

16.2K

Area of Science:

  • Proteomics and Mass Spectrometry
  • Food Science and Analysis
  • Analytical Chemistry

Background:

  • Automated proteomics methods are crucial for characterizing peptides in food applications and protein digests.
  • Peptide annotation confidence relies on fragment spectra, but low reproducibility in repeat analyses is a known issue, even for high-confidence annotations.
  • Accurate and reproducible peptide annotation is essential for analyzing food protein hydrolysates.

Purpose of the Study:

  • To establish criteria for highly reproducible peptide annotations in the analysis of protein hydrolysates.
  • To develop and validate a structured approach for optimizing peptide identification and quantification in food applications.
  • To assess the impact of sample complexity (individual vs. mixed hydrolysates) on annotation reproducibility.

Main Methods:

  • Analysis of tryptic hydrolysates from α-lactalbumin, β-lactoglobulin, and β-casein using ultra-performance liquid chromatography-photodiode array-mass spectrometry (UPLC-PDA-MS).
  • Implementation of a two-component lock mass strategy for high mass accuracy (average error of 1 ppm).
  • Application of processing filters to ensure reliable MS/MS fragmentation-based annotations while maximizing information content.

Main Results:

  • Peptides above the limit of annotation (LOA) represented 99% of total MS intensity and achieved 100% consistent annotation across four replicates for individual hydrolysates.
  • High amino acid (99-100%) and peptide sequence (89-95%) coverage was achieved for individual protein hydrolysates.
  • Mixing hydrolysates led to an 11% loss in peptide annotations above the LOA, reduced reproducibility to 97%, and increased co-elution, with concentration variations up to 37% ± 21% for co-eluting peptides.

Conclusions:

  • The proposed structured approach enables complete description of peptide composition with highly repeatable annotations and quantification.
  • The method demonstrates robust performance even when analyzing complex mixtures of protein hydrolysates.
  • This methodology addresses the need for reproducible peptide analysis in food science and proteomics.