Inhibition and Promotion of Heat-Induced Protein Modifications in Whey by Vitamins: Quantitative Profiling of 14 Modifications at 29 β-Lactoglobulin Binding Sites

Schichtl TM, Biwo V, Dittrich D, Belli C, Pischetsrieder M (2025)


Publication Type: Journal article

Publication year: 2025

Journal

Book Volume: 73

Pages Range: 32209-32220

Journal Issue: 50

DOI: 10.1021/acs.jafc.5c12551

Abstract

Nonenzymatic post-translational modifications (nePTMs) induced by thermal processing of whey-based foods impair the protein quality and digestibility. This study evaluates the impact of 14 water- or fat-soluble vitamins on the formation of heat-induced nePTMs in whey proteins. Whey samples were fortified with vitamins and subjected to heat treatment. After Glu-C hydrolysis, 14 nePTMs at 29 binding sites in β-lactoglobulin were quantified by microflow-liquid chromatography-electrospray ionization tandem mass spectrometry in scheduled multiple reaction monitoring mode. The analysis included primary and advanced Maillard products, oxidation products, deamidation and deamination products. This comprehensive structure- and site-specific approach revealed that vitamin B2, folic acid, vitamin A, and vitamin B12 were the most effective inhibitors against nePTM formation. Vitamin K2, vitamin D3, retinoic acid, vitamin K1, and β-carotene demonstrated moderate inhibitory effects. In contrast, vitamin B1 and biotin tended to promote modifications, while vitamin C affected different reaction mechanisms in varying ways.

Authors with CRIS profile

How to cite

APA:

Schichtl, T.M., Biwo, V., Dittrich, D., Belli, C., & Pischetsrieder, M. (2025). Inhibition and Promotion of Heat-Induced Protein Modifications in Whey by Vitamins: Quantitative Profiling of 14 Modifications at 29 β-Lactoglobulin Binding Sites. Journal of Agricultural and Food Chemistry, 73(50), 32209-32220. https://doi.org/10.1021/acs.jafc.5c12551

MLA:

Schichtl, Theresa Maria, et al. "Inhibition and Promotion of Heat-Induced Protein Modifications in Whey by Vitamins: Quantitative Profiling of 14 Modifications at 29 β-Lactoglobulin Binding Sites." Journal of Agricultural and Food Chemistry 73.50 (2025): 32209-32220.

BibTeX: Download