The enhancement and mechanism of the perception of saltiness by umami peptide from Ruditapes philippinarum and ham. (30th March 2023)

• Record Type: Journal Article
• Authors: Xie, Xiangning; Dang, Yali; Pan, Daodong; Sun, Yangying; Zhou, Changyu; He, Jun; Gao, Xinchang
• Is Part Of: Food chemistry. Volume 405:Part A(2023)
• Publication Date: 2023-03-30
• Subjects: Umami peptides -- Saltiness enhancement -- Electronic tongue -- TMC4 -- Molecular docking; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2022.134886
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Low isoelectric of umami peptide led to TMC4 to enhance salty taste. Ten umami peptides were found to be the salt - reducing peptides. Lys568, Trp145, Tyr565, Arg151, and Gln155 were found in umami peptide and TMC4. Abstract: To explore the saltiness enhancement effect and mechanism of umami peptides, umami peptides from Ruditapes philippinarum and ham were mixed with NaCl and determined using electronic tongue, sensory evaluation, and the aroma chicken model (ACM), then transmembrane channel-like protein 4 (TMC4) receptor was constructed for molecular docking. The results showed that KEMQKN, NGKET, RGEPNND, AHSVRFY, LSERYP, NRTF, TYLPVH, EV, AGAGPTP, and GPAGPAGPR had saltiness enhancement effect, which could be increased to 0.4–0.6 % NaCl salty taste in 0.3 % NaCl. Under neutral conditions (pH6.5), most umami peptides were in negative ion state which may be the main reason that umami peptides could bind to the TMC4 receptor and enhance saltiness. The lowest docking energy was −113.325 kcal/mol among 10 peptides and the active sites Lys568, Trp145, Tyr565, Arg151, and Gln155 in TMC4 may play a key role. Thus, this study provides basic theory and data for salt-reduction strategies.