Plastein reaction augments the metal chelating capabilities of silver carp (Hypophthalmichthys molitrix) hydrolysates: Unlocking the chemical modification mechanism

Plastein reaction mechanisms and the alteration of its product properties have been studied for decades. This study investigated the plastein-mediated modifications in silver carp protein hydrolysate (SCPH) from both mechanistic and functional perspectives. Unlike prior research, this investigation uncovered that hydrogen bonding supplemented the dominant hydrophobic interactions in plastein's mechanism for the first time, as supported by peptide concentrations, molecular weight, amino acids, chemical forces, and peptide sequence by LC-MS/MS. This innovative reaction mechanism cascaded into the enhancement of SCPH functional attributes. Plastein induced increased COOH in SCPH’s side-chain groups significantly enhanced Fe2+ (from 4.49 to 14.12 %) and Zn2+ (from 53.53 to 64.47 %) chelation. Moreover, the elevated DPPH (17.56 %–23.97 %) and hydroxyl radical (68.49 %–79.32 %) scavenging power indicated a broader improvement in SCPH with plastein. In SCPH, plastein elucidated reaction intricacies and enhanced its utility, propelling SCPH into a realm of extended potential.