基于分子模拟的鸡肉增鲜肽增鲜机制
TS202.3; 为了研究增鲜肽的增鲜机制,通过分子模拟技术结合感官评价分析3 条鸡肉源肽LPLQD、DGGRYY和DEAGPSIVH的增鲜作用、增鲜肽-谷氨酸-味觉受体互作分子机制及其动态结合过程.增鲜肽的特性分析结果表明,3 条增鲜肽水溶性较好且无毒性.感官分析结果显示,3 条增鲜肽均对质量分数0.35%谷氨酸钠溶液具有鲜味感知加成作用.分子对接结果表明,增鲜肽的存在显著增加了配体体系与味觉受体亚型1(taste receptor type 1,T1R1)间的相互作用,包括静电相互作用、疏水相互作用和氢键相互作用,从而增强了配体体系与T1R1之间的结合稳定性.在分子动力学模拟过程中,鲜味受...
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| Published in | 食品科学 Vol. 45; no. 24; pp. 1 - 8 |
|---|---|
| Main Authors | , , , |
| Format | Magazine Article |
| Language | Chinese |
| Published |
北京工商大学 中国商业联合会味科学重点实验室,北京 100048
25.12.2024
北京工商大学 老年营养与健康教育部重点实验室,北京 100048 北京工商大学 中原食品实验室,北京 100048 |
| Subjects | |
| Online Access | Get full text |
| ISSN | 1002-6630 |
| DOI | 10.7506/spkx1002-6630-20231222-193 |
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| Abstract | TS202.3; 为了研究增鲜肽的增鲜机制,通过分子模拟技术结合感官评价分析3 条鸡肉源肽LPLQD、DGGRYY和DEAGPSIVH的增鲜作用、增鲜肽-谷氨酸-味觉受体互作分子机制及其动态结合过程.增鲜肽的特性分析结果表明,3 条增鲜肽水溶性较好且无毒性.感官分析结果显示,3 条增鲜肽均对质量分数0.35%谷氨酸钠溶液具有鲜味感知加成作用.分子对接结果表明,增鲜肽的存在显著增加了配体体系与味觉受体亚型1(taste receptor type 1,T1R1)间的相互作用,包括静电相互作用、疏水相互作用和氢键相互作用,从而增强了配体体系与T1R1之间的结合稳定性.在分子动力学模拟过程中,鲜味受体T1R1胞外捕蝇草结构域相对稳定,而富半胱氨酸结构域存在较大的空间波动.氢键数量统计结果显示,增鲜肽加入配体体系能够增加配体与受体间氢键相互作用,从而增强配体与受体的结合强度.通过前沿分子轨道计算确定了Ser、Tyr、Gln、Arg和His等氨基酸残基为增鲜肽与T1R1结合的主要活性位点.以上研究结果可为理解增鲜肽的增鲜机制以及新型增鲜剂的开发提供理论支持. |
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| AbstractList | TS202.3; 为了研究增鲜肽的增鲜机制,通过分子模拟技术结合感官评价分析3 条鸡肉源肽LPLQD、DGGRYY和DEAGPSIVH的增鲜作用、增鲜肽-谷氨酸-味觉受体互作分子机制及其动态结合过程.增鲜肽的特性分析结果表明,3 条增鲜肽水溶性较好且无毒性.感官分析结果显示,3 条增鲜肽均对质量分数0.35%谷氨酸钠溶液具有鲜味感知加成作用.分子对接结果表明,增鲜肽的存在显著增加了配体体系与味觉受体亚型1(taste receptor type 1,T1R1)间的相互作用,包括静电相互作用、疏水相互作用和氢键相互作用,从而增强了配体体系与T1R1之间的结合稳定性.在分子动力学模拟过程中,鲜味受体T1R1胞外捕蝇草结构域相对稳定,而富半胱氨酸结构域存在较大的空间波动.氢键数量统计结果显示,增鲜肽加入配体体系能够增加配体与受体间氢键相互作用,从而增强配体与受体的结合强度.通过前沿分子轨道计算确定了Ser、Tyr、Gln、Arg和His等氨基酸残基为增鲜肽与T1R1结合的主要活性位点.以上研究结果可为理解增鲜肽的增鲜机制以及新型增鲜剂的开发提供理论支持. |
| Abstract_FL | To investigate the mechanism of action of umami-enhancing peptides,molecular simulation and sensory evaluation were employed to analyze the umami-enhancing effects of three peptides derived from chicken:LPLQD,DGGRYY,and DEAGPSIVH,the molecular mechanism of umami-enhancing peptide-glutamic acid-taste receptor interaction and the dynamic binding process.The results indicated that all three umami-enhancing peptides exhibited good water solubility and non-toxicity and had an additive effect on the umami taste of 0.35%glutamic acid solution.Molecular docking results revealed that the presence of umami-enhancing peptides greatly enhanced the interactions between the ligand system and the taste receptor type 1(T1R1)including electrostatic interaction,hydrophobic interaction,and hydrogen bonding interaction,thereby leading to enhanced binding stability.Furthermore,molecular dynamic simulations disclosed that the venus flytrap(VFT)domain in the T1R1 receptors was relatively stable,while the cysteine-rich domain exhibited significant spatial fluctuations.Statistics of hydrogen bonds indicated that the addition of umami-enhancing peptides to the ligand system enhanced the hydrogen bonding interaction and consequently binding intensity between ligands and receptors.By analyzing the frontier molecular orbitals,serine,tyrosine,glutamine,arginine,and histidine residues were identified as active sites in the peptides that contributed to the binding with T1R1.The above results provide theoretical support for understanding the umami-enhancing mechanism of peptides and for the development of new umami enhancers. |
| Author | 何玮 张玉玉 张敬铖 梁莉 |
| AuthorAffiliation | 北京工商大学 老年营养与健康教育部重点实验室,北京 100048;北京工商大学 中国商业联合会味科学重点实验室,北京 100048;北京工商大学 中原食品实验室,北京 100048 |
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| Author_FL | ZHANG Jingcheng HE Wei ZHANG Yuyu LIANG Li |
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| DocumentTitle_FL | Elucidating the Mechanism of Action of Umami-Enhancing Peptides Derived from Chicken Based on Molecular Simulation |
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| Keywords | 前沿分子轨道 molecular docking frontier molecular orbital 分子动力学 umami-enhancing peptide molecular dynamics 分子对接 增鲜肽 |
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| Publisher | 北京工商大学 中国商业联合会味科学重点实验室,北京 100048 北京工商大学 老年营养与健康教育部重点实验室,北京 100048 北京工商大学 中原食品实验室,北京 100048 |
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| Title | 基于分子模拟的鸡肉增鲜肽增鲜机制 |
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