Related Experiment Video
Updated: Jan 13, 2026
Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry
Published on: July 31, 2011
Development of a targeted mass spectrometry method for porcine pancreas marker peptides detection in protein
Jiaoyi Luo1, Gang Chen2, Jin Cao3
1College of Food Science and Engineering, Northwest A&F University, Yangling, Shaanxi 712100, China; Key Laboratory of Food Quality and Safety for State Market Regulation, National Institute of Food and Drug Control, Beijing 100050, China.
Abstract:
Protein hydrolysates are widely used in health foods, but undisclosed enzymatic sources, particularly porcine pancreas, raising concerns regarding food safety, allergenicity, and dietary restrictions. To address this issue, this study comprehensively characterized the porcine pancreas proteome, identifying 418 proteins and establishing 50 °C autolysis to ensure consistent peptide profiles. Three homologous highly specific α-amylase-derived marker peptides, VTNPSRPW, VVTNPSRPW, and IVVTNPSRPW, were selected and validated, and a targeted LC-MS/MS assay was established with porcine pancreas detection limits of 0.5 %, 1 %, and 5 % (w/w), respectively. Application of this method to commercial products revealed the presence of porcine peptides in samples labeled as "animal-free" which was further proved by on-site investigation. This study provides a robust and practical approach for verifying the species origin of enzymatic preparations in protein hydrolysates, enhancing traceability, food safety, and regulatory compliance. To our knowledge, it represents the first systematic investigation into enzyme source authenticity in such products.
