Discovery of peptides with saltiness-enhancing effects in enzymatic hydrolyzed Agaricus bisporus protein and evaluation of their salt-reduction property

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作者
Wang, Zhangjingyi [1 ]
Cheng, Yunpeng [1 ]
Muhoza, Bertrand [2 ]
Sun, Min [1 ]
Feng, Tao [1 ]
Yao, Linyun [1 ]
Liu, Qian [1 ]
Song, Shiqing [1 ]
机构
[1] School of Perfume and Aroma Technology, Shanghai Institute of Technology, 100 Haiquan Road, Shanghai,201418, China
[2] College of Food Science, Northeast Agricultural University, 600 Changjiang Road, Harbin,Heilongjiang,150030, China
基金
中国国家自然科学基金; 上海市自然科学基金;
关键词
This study aimed to screen peptides with saltiness-enhancing effects from enzymatic hydrolyzed Agaricus bisporus protein and quantify their salt-reduction. The saltiness evaluation standard curve was first established to evaluate salinity. The peptide fractions (U-1; U-2; and U-3) were obtained from enzymatic hydrolyzed Agaricus bisporus protein by ultrafiltration. Quantitative calculations showed that the U-2 fraction (200–2000 Da) had the strongest saltiness-enhancing effect; and its perceived saltiness in 50 mmol NaCl solution was 60.24 ± 0.10 mmol/L. The peptide sequences were identified by liquid chromatography/mass spectrometry (LC-MS/MS). Results suggested that the potential peptides with saltiness-enhancing effects were umami peptides. Molecular docking with the umami receptor T1R1/T1R3 revealed that the key amino acid residues were Asp82; Glu392; Glu270; and Asp269. Furthermore; peptide YDPNDPEK (976.4138 Da); DDWDEDAPR; (1117.4312; Da); and DVPDGPPPE (1058.4668 Da) were synthesized for salt-reduction quantification. 0.4 % peptide YDPNDPEK in NaCl solution was found to have a salt-reduction of 30 %; which provided the basic theory and data for the salt-reduction of peptide in enzymatic hydrolyzed Agaricus bisporus protein. © 2024 Elsevier Ltd;
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    [J]. FOOD RESEARCH INTERNATIONAL, 2024, 177
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