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Structural Feature of Salty/Saltiness-Enhancing Peptides Derived from Coprinus comatus and Their Stability during Subsequent Thermal Treatment and Maillard Reaction

文献类型： 外文期刊

作者： Song, Mingzhou 1 ; Zhou, Tong 1 ; Liao, Qiuhong 2 ; Zhang, Foxin 3 ; Hussain, Shahzad 4 ; Hayat, Khizar 5 ; Zhang, Xiaoming 1 ; Ho, Chi-Tang 6 ;

作者机构： 1.Jiangnan Univ, Sch Food Sci & Technol, State Key Lab Food Sci & Resources, Wuxi 214122, Jiangsu, Peoples R China

2.Chinese Acad Agr Sci, Inst Urban Agr, Chengdu 610299, Peoples R China

3.Anhui Qiang Wang Flavouring Food Co Ltd, Anhui Prov Key Lab Funct Cpd Seasoning, Jieshou 236500, Anhui, Peoples R China

4.King Saud Univ, Coll Food & Agr Sci, Dept Food Sci & Nutr, Riyadh 11451, Saudi Arabia

5.Alabama A&M Univ, Dept Food & Anim Sci, Normal, AL 35762 USA

6.Rutgers State Univ, Dept Food Sci, New Brunswick, NJ 08901 USA

关键词： Coprinus comatus; saltinessenhancement peptides; molecular docking; secondarystructure; thermal stability

期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：6.2； 五年影响因子：6.4 ）

ISSN： 0021-8561

年卷期： 2025 年 73 卷 1 期

页码：

收录情况： SCI

摘要： Through a quantitative analysis of saltiness perception, favorable enzymatic hydrolysis parameters were confirmed for the preparation of saltiness-enhancing peptide mixtures from Coprinus comatus. The enzymatic hydrolysate was fractionated into four fractions (F1-F4) by gel chromatography, with F3 exhibiting the strongest saltiness-enhancing effect (22% increase). LC-MS/MS analysis of F3 identified 36 peptides, and their secondary structures and interactions with the TMC4 receptor were examined through circular dichroism spectroscopy and molecular docking. Molecular docking analysis revealed Asn588, Ser165, Asp5, and Arg168 as key amino acid residues, with the peptide GDNVGF showing the lowest binding energy. Synthetic GDNVGF (0.01%) in 70 mmol/L NaCl enhanced saltiness by 17%. When 0.7% GDNVGF was added to the aqueous solution, its saltiness was equivalent to that of 36.89 mmol/L NaCl, which suggested that GDNVGF functions both as a saltiness-enhancing peptide and a salty peptide. The taste changes of peptides during thermal reactions were further investigated. The thermal stability of Coprinus comatus peptides was good, but their saltiness-enhancing effect slightly reduced due to thermal degradation. The Maillard reaction further diminished this effect, though the umami level remained satisfactory, offering new insights into using Coprinus comatus peptides as low-sodium salt substitutes.

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