In this study, umami peptides were screened and characterized from bovine bone soups manufactured via atmospheric and high-pressure boiling. Peptide fractions with molecular weights less than 3 kDa were selected for peptide sequencing using LC-MS/MS, the toxicity prediction of the umami peptides was carried out by using an website, and the peptides were screened according to the binding energy, i.e., three peptides including YDAELS, TDVAHR, and ELELQ were selected. The three umami peptides were further synthesized, and their umami thresholds were determined through sensory evaluation and electronic tongue analysis, ranging from 0.375 to 0.75 mg/mL. All three peptides exhibited a significant synergistic taste enhancement effect when combined with MSG (monosodium glutamate) solution. The molecular docking of the umami peptides with the T1R1/T1R3 receptor revealed the mechanism of umami presentation, and the main interaction forces between the three umami peptides and the receptor were hydrogen bonding, electrostatic interactions, and hydrophobic interactions.
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http://dx.doi.org/10.3390/foods13182870 | DOI Listing |
Food Chem
January 2025
Key Laboratory of Tea Biology and Resource Utilization of Ministry of Agriculture, Tea Research Institute, Chinese Academy of Agricultural Sciences, Hangzhou 310008, China. Electronic address:
Food Res Int
January 2025
State Key Laboratory of Food Science and Resources, National Engineering Research Center of Cereal Fermentation and Food Biomanufacturing, School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; Guangdong Engineering Research Center of High-Value Utilization and Equipment Development of Marine Biological Resources, Southern Marine Science and Engineering Guangdong Laboratory, Guangzhou, Guangdong 511458, China; Jiangnan University (Shaoxing) Industrial Technology Research Institute, Shaoxing, Zhejiang 31200, China; National Engineering Research Center of Huangjiu, Zhejiang Guyuelongshan Shaoxing Wine CO., LTD, Shaoxing 646000, Zhejiang, China. Electronic address:
To explore the mechanism of Virgibacillus proteases on hydrolysis of shrimp myofibrillar protein (SMP) and formation of volatile compounds, the fermented broth of Virgibacillus halodenitrificans was purified and the protease was identified as peptidase S8. The enzyme had optimum activity at pH 7.0-8.
View Article and Find Full Text PDFFood Chem
December 2024
Department of Food Science & Technology, School of Agriculture & Biology, Shanghai Jiao Tong University, Shanghai 200240, PR China; School of Food Science and Engineering, Ningxia University, Yinchuan 750021, China. Electronic address:
To prepare dual-functional seasoning ingredients with a salty-umami taste, five proteases were applied to hydrolyze proteins, preparing enzymatic hydrolysates. Their taste compounds along with the salty-umami taste, were investigated. The results revealed that enzymatic hydrolysis facilitated the release of taste compounds from .
View Article and Find Full Text PDFJ Agric Food Chem
January 2025
Department of Food Science, Rutgers University, 65 Dudley Road, New Brunswick, New Jersey 08901, United States.
Through a quantitative analysis of saltiness perception, favorable enzymatic hydrolysis parameters were confirmed for the preparation of saltiness-enhancing peptide mixtures from . 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.
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