Identification of Novel Umami Peptides in Chicken Breast Soup through a Sensory-Guided Approach and Molecular Docking to the T1R1/T1R3 Taste Receptor.
Identification of Novel Umami Peptides in Chicken Breast Soup through a Sensory-Guided Approach and Molecular Docking to the T1R1/T1R3 Taste Receptor.
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DOI：
10.1021/acs.jafc.3c01251
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发表时间：
2023-05
影响因子：
6.1
通讯作者：
Li-li Zhang;Dandan Pu;Jingcheng Zhang;Zhilin Hao;Xixuan Zhao;B. Sun;Yuyu Zhang
中科院分区：
文献类型：
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作者：
Li-li Zhang;Dandan Pu;Jingcheng Zhang;Zhilin Hao;Xixuan Zhao;B. Sun;Yuyu Zhang
采用超滤技术结合纳米液相色谱-四极杆飞行时间质谱（nano-LC-QTOF-MS）和感官评价对鸡胸汤中的鲜味肽进行分离鉴定。采用nano-LC-QTOF-MS从分子量≤1 kDa的组分中鉴定出15种鲜味倾向评分>588的肽，其在鸡胸汤中的浓度范围为0.02 ± 0.01至6.94 ± 0.41 μg/L。根据感官分析结果（检测阈值：0.18-0.91 mmol/L），认为AEEHVEAVN、PKESEKPN、VGNEFVTKG、GIQKELQF、FTERVQ和AEINKILGN是鲜味肽。主观相等点的测量表明，这六种鲜味肽（2.00 g/L）在鲜味强度方面相当于0.53-0.66 g/L的谷氨酸盐（MSG）。值得注意的是，感官评价结果显示，AEEHVEAVN肽显著增强了味精溶液和鸡汤模型的鲜味强度。分子对接结果显示丝氨酸残基是T1 R1/T1 R3中最常见的结合位点。结合位点Ser 276特别有助于鲜味肽-T1 R1复合物的形成。在鲜味肽中观察到的酸性谷氨酸残基也参与了它们与T1 R1和T1 R3亚基的结合。
Ultrafiltration combined with nanoliquid chromatography quadrupole time-of-flight mass spectrometry (nano-LC-QTOF-MS) and sensory evaluation was used to separate and identify umami peptides in chicken breast soup. Fifteen peptides with umami propensity scores of >588 were identified from the fraction (molecular weight ≤1 kDa) using nano-LC-QTOF-MS, and their concentrations ranged from 0.02 ± 0.01 to 6.94 ± 0.41 μg/L in chicken breast soup. AEEHVEAVN, PKESEKPN, VGNEFVTKG, GIQKELQF, FTERVQ, and AEINKILGN were considered as umami peptides according to sensory analysis results (detection threshold: 0.18-0.91 mmol/L). The measurement of point of subjective equality showed that these six umami peptides (2.00 g/L) were equivalent to 0.53-0.66 g/L of monosodium glutamate (MSG) in terms of umami intensity. Notably, the sensory evaluation results showed that the peptide of AEEHVEAVN significantly enhanced the umami intensity of the MSG solution and chicken soup models. The molecular docking results showed that the serine residues were the most frequently observed binding sites in T1R1/T1R3. The binding site Ser276 particularly contributed to the formation of the umami peptide-T1R1 complexes. The acidic glutamate residues observed in the umami peptides were also involved in their binding to the T1R1 and T1R3 subunits.