Taste peptides derived from Stropharia rugosoannulata fermentation mycelium and molecular docking to the taste receptor T1R1/T1R3

Abstract

This study identified the peptides in the fermentation mycelia of Stropharia rugosoannulata. The molecular weight of the peptides was below 3,000 Da. Heptapeptides to decapeptides were the main peptides in the fermentation mycelia of S. rugosoannulata. More than 50% of the peptides had salty and umami taste characteristics, and the long-chain peptides (decapeptides to 24 peptides) also played an essential role in the pleasant taste characteristics of mycelium. In the salty and umami peptide of S. rugosoannulata, the distribution of non-polar hydrophobic amino acids and polar-uncharged amino acids accounted for a relatively high proportion, and the proportion of polar-uncharged amino acids further increased, with the extension of the peptide chain. P, F, I, l, V, G, S, T, and D were the amino acids with a high proportion in the peptides. The taste peptides can bind to more than 60% of the active amino acid residues in the cavity-binding domain of the T1R1/T1R3 receptors. Hydrogen bond interaction was the primary mode of interaction between the peptides and the receptor. The first and second amino acid residues (such as S, V, E, K, G, and A) at the C-terminal and N-terminal of the peptides were easy to bind to T1R1/T1R3 receptors. Asp108, Asn150, Asp147, Glu301, Asp219, Asp243, Glu70, Asp218 in T1R1, and Glu45, Glu148, Glu301, Glu48, and Ala46 in TIR3 were the key active amino acid sites of taste peptides binding to T1R1/T1R3 receptors.

Study on the relationship between structure and taste activity of the umami peptide of Stropharia rugosoannulata prepared by ultrasound

“…The T1R1/T1R3 receptor model constructed by our team was used [13] . The receptor binding cavity and binding site are the same as those in the report [35] . The molecular docking technique simulated the binding state between the umami peptides of S.rugosoannulata and the receptor protein.…”

“…Stropharia rugosoannulata , also known as the red pine mushroom, is rich in umami peptides and is a high-quality raw material for developing a base material of natural flavors [13] , [35] . Our previous research found that the base material of S.rugosoannulata prepared by traditional enzymatic hydrolysis had a high proportion of peptide (461.31 mg/g dry weight) and the flavor characteristics of the base material were close to those of the umami reference (MSG) with the same concentration.…”

Nutritional, Bioactive, and Flavor Components of Giant Stropharia (Stropharia rugoso-annulata): A Review

“…S. rugoso-annulata mushrooms are a premium source of umami peptides. Free peptides in the fruiting body of S. rugoso-annulata reach a content of 11.28–12.56% [ 73 ]. As shown in Table 5 , the taste peptides of S. rugoso-annulata exhibit a strong umami taste, accompanied by saltiness, bitterness, richness, or aftertaste [ 5 , 74 , 75 ].…”

“…Free peptides in the fruiting body of S. rugoso-annulata reach a content of 11.28–12.56% [ 73 ]. As shown in Table 5 , the taste peptides of S. rugoso-annulata exhibit a strong umami taste, accompanied by saltiness, bitterness, richness, or aftertaste [ 5 , 74 , 75 ]. The taste peptides in the mature fruiting body are pentapeptides to undecapeptides and the taste threshold is relatively low (0.117–0.640 mmol·L −1 ) [ 5 , 74 ], while the peptide variety in the mycelium is particularly rich and the taste peptides are mostly heptapeptides to decapeptides [ 74 ].…”

Revealing the ACE receptor binding properties and interaction mechanisms of salty oligopeptides from Stropharia rugosoannulata mushroom by molecular simulation and antihypertensive evaluation

“…At a mass concentration of 1 mg mL −1 , the peptide matrix had a salty evaluation value of 23.33 ± 0.11, an umami evaluation value of 13.17 ± 0.16, and a 50% ACE inhibitory concentration (IC 50 ) of 0.122 mg mL −1 , ABTS-free radical scavenging rate (%) was 72.24 ± 1.52, and a 50% DPP-IV inhibitory concentration of 6.62 mg mL −1 . [4][5][6] The ACE inhibitory activity of the S. rugosoannulata peptide matrix is more prominent than its antioxidant and DPP-IV inhibitory activity. Many ACE inhibitors have been identified from plant and animal protein hydrolysates and showed better ACE inhibitory effects in cellular models and blood pressure-lowering activity in animal models.…”