Effects of sodium dihydrogen phosphate (MSP) and disodium hydrogen phosphate (DSP) on the glycation of casein (CN)
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Updated: Oct 24, 2026

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
Published on: March 9, 2010
Shaohong Xu1, Xiaodong Hu1, Yushuo Sun2
1School of Pharmacy, Bengbu Medical University, Bengbu 233000, China.
Abstract:
This study investigated the effects of phosphate addition on the Maillard reaction in glycated casein. Results showed that phosphate (especially at 100 mM) promoted the accumulation of Maillard intermediates and final products, while suppressing protein aggregation and increasing free amino group content. Structural analysis indicated a shift toward a more disordered conformation, enhancing reaction activity. Notably, specific phosphate treatments differentially modulated glycation sites and volatile compound formation; MSP significantly reduced aldehyde, ketone, and alcohol generation, contributing to flavor stability, whereas DSP showed limited effects. Phosphate thus plays a dual role by promoting early reaction stages and selectively modulating final product profiles, offering insights for controlling Maillard reaction and flavor in protein processing.
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