Characteristics of umami peptides identified from porcine bone soup and molecular docking to the taste receptor T1R1/T1R3. (1st September 2022)

• Record Type: Journal Article
• Authors: Liang, Li; Zhou, Chenchen; Zhang, Jingcheng; Huang, Yan; Zhao, Jing; Sun, Baoguo; Zhang, Yuyu
• Is Part Of: Food chemistry. Volume 387(2022)
• Publication Date: 2022-09-01
• Subjects: Umami peptide -- Taste characteristics -- Molecular docking -- Porcine bone; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2022.132870
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Three umami peptides were identified from porcine bone soup with welsh onion or not. FSGLDGSK had the highest umami intensity and umami-enhancing effect. The binding of the four peptides with T1R1/T1R3 were studied by docking simulation. Abstract: To study the umami peptides derived from porcine bone soup, ultrafiltration fractions with molecular weight less than 1 kDa were screened by sensory analysis which showed higher umami intensity. Four potential umami peptides were identified from the screened fractions by Nano-LC-Q-TOF-MS/MS, among which FSGLDGAK, FAGDDAPR and FSGLDGSK were proved to have dominant umami taste by sensory evaluation and electronic tongue. The threshold of the three peptides ranged from 0.1 mM to 0.89 mM. In addition, FSGLDGSK had the highest umami intensity and exhibited a significant umami-enhancing effect in a 0.35% monosodium glutamate solution. The results of molecular docking simulation showed that the key binding sites of taste receptor type 1 member 1 (His71, Asp108 and Glu301) and taste receptor type 1 member 3 (Glu48, Ser104 and His145) were crucial to the interaction with the umami peptides. Besides, electrostatic interaction and hydrogen bond mainly contributed to the mechanism of umami taste.