Identification of umami peptides from Wuding chicken by Nano-HPLC-MS/MS and insights into the umami taste mechanisms.

Identification of umami peptides from Wuding chicken by Nano-HPLC-MS/MS and insights into the umami taste mechanisms.
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DOI:
10.1016/j.foodres.2023.113208
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发表时间:
2023-10
影响因子:
8.1
通讯作者:
Rong Jia;Ying He;G. Liao;Zijiang Yang;Dahai Gu;Yuehong Pu;Ming Huang;Guiying Wang
Rong Jia;Ying He;G. Liao;Zijiang Yang;Dahai Gu;Yuehong Pu;Ming Huang;Guiying Wang
中科院分区:
农林科学1区
文献类型:
--
作者:
Rong Jia;Ying He;G. Liao;Zijiang Yang;Dahai Gu;Yuehong Pu;Ming Huang;Guiying Wang

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武定鸡因其鲜味而深受中国消费者的喜爱。本研究旨在鉴定武定鸡中的新型鲜味肽,并探讨鲜味肽的呈味机制。采用纳米级液相色谱-串联质谱法(Nano-HPLC-MS/MS)对武定鸡中肽的分子量和氨基酸组成进行鉴定。通过感官评价结合电子舌技术对固相法合成的肽的味道特征进行评价。通过圆二色性(CD)进一步分析肽的二级结构,并通过分子对接阐明肽的结构与味道之间的关系。结果显示,鉴定出8种潜在的鲜味肽,其中FVT(FT-3)、LDF(LF-3)和DLAGRDLTDYLMKIL(DL-15)具有明显的鲜味,其中FT-3的鲜味强度最高,其次是LF-3和DL-15。三种鲜味肽中β-折叠相对含量分别为55.20%、57.30%和47.70%,是武定鸡肉鲜味肽的关键成分。除了嵌入 TIR1 空腔结合域的 LF-3 之外,FT-3 和 DL-15 都嵌入 T1R3 的捕蝇草域 (VFTD),以结合鲜味受体 T1R1/T1R3。鲜味肽与鲜味受体T1R1/T1R3之间的结合力主要依靠氢键和疏水相互作用,鲜味肽与鲜味受体T1R1/T1R3结合的关键氨基酸残基为Glu292、Asn235和Tyr262。
Wuding chicken is popular with consumers in China because of its umami taste. This study aimed to identify novel umami peptides from Wuding chicken and explore the taste mechanism of umami peptides. The molecular masses and amino acid compositions of peptides in Wuding chicken were identified by nano-scale liquid chromatography-tandem mass spectrometry (Nano-HPLC-MS/MS). The taste characteristics of the peptides synthesized by the solid-phase method were evaluated by sensory evaluation combined with electronic tongue technology. The secondary structure of the peptides was further analyzed by circular dichroism (CD), and the relationship between the structure and taste of the peptides was elucidated by molecular docking. The results showed that eight potential umami peptides were identified, among which FVT (FT-3), LDF (LF-3), and DLAGRDLTDYLMKIL (DL-15) had distinct umami tastes, and FT-3 had the highest umami intensity, followed by LF-3 and DL-15. The relative contents of β-sheets in the three umami peptides were 55.20%, 57.30%, and 47.70%, respectively, which were the key components of Wuding chicken umami peptides. In addition to LF-3 embedded in the cavity-binding domain of the TIR1, both FT-3 and DL-15 were embedded in the venus flytrap domain (VFTD) of the T1R3 to bind the umami receptor T1R1/T1R3. The main binding forces between the umami peptides and the umami receptor T1R1/T1R3 relied on hydrogen bonds and hydrophobic interactions, and the key amino acid residues of the combination of umami peptides and the umami receptor T1R1/T1R3 were Glu292, Asn235, and Tyr262.