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Discovery of peptides with saltiness-enhancing effects in enzymatic hydrolyzed Agaricus bisporus protein and evaluation of their salt-reduction property
被引:0
|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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