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Updated: May 8, 2026

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry
Published on: March 23, 2020
Identification of bitter peptides in whey protein hydrolysate
Xiaowei Liu1, Deshou Jiang, Devin G Peterson
1Department of Food Science and Nutrition, 145 FScN Building, University of Minnesota , 1334 Eckles Avenue, St. Paul, Minnesota 55108, United States.
Abstract:
Bitterness of whey protein hydrolysates (WPH) can negatively affect product quality and limit utilization in food and pharmaceutical applications. Four main bitter peptides were identified in a commercial WPH by means of sensory-guided fractionation techniques that included ultrafiltration and offline two-dimensional reverse phase chromatography. LC-TOF-MS/MS analysis revealed the amino acid sequences of the bitter peptides were YGLF, IPAVF, LLF, and YPFPGPIPN that originated from α-lactalbumin, β-lactoglobulin, serum albumin, and β-casein, respectively. Quantitative LC-MS/MS analysis reported the concentrations of YGLF, IPAVF, LLF, and YPFPGPIPN to be 0.66, 0.58, 1.33, and 2.64 g/kg powder, respectively. Taste recombination analysis of an aqueous model consisting of all four peptides was reported to explain 88% of the bitterness intensity of the 10% WPH solution.

