This study evaluated the effects of sodium acid pyrophosphate (SAPP) and sodium tripolyphosphate (STPP) on the glycation of myofibrillar proteins (MPs), soy protein isolate (SPI), and casein (CN). The addition of phosphate generally increased the reduction in free amino acids and the formation of UV signals in Maillard reaction products (MRPs) in MP and CN during glycation. It also decreased the protein structural order and particle size, which could help increase glycation. The number of glycation sites decreased in SPI and MP but increased in CN during the initial heating. The addition of phosphates markedly enhanced the formation of alkanes and sulfides in SPI and MP. In model systems in which lysine and arginine were used, STPP and SAPP directly catalyzed the Maillard reaction. This study elucidated the acceleration role of STPP and SAPP by changing the structure of the tested proteins and directly catalyzing the Maillard reaction.
Sun et al. (Sat,) studied this question.
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