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Updated: Sep 23, 2025

Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders
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Characterization of Peanut Protein Hydrolysate and Structural Identification of Umami-Enhancing Peptides
Lixia Zhang1, Xiaojing Sun1, Xin Lu1
1Research Center for Agricultural and Sideline Products Processing, Henan Academy of Agricultural Sciences, Zhengzhou 450002, China.
Abstract:
Umami peptides are naturally found in various foods and have been proven to be essential components contributing to food taste. Defatted peanut powder hydrolysate produced by a multiprotease (Flavorzyme, Alcalase, and Protamex) was found to elicit an umami taste and umami-enhancing effect. The taste profiles, hydrolysis efficiency, amino acids, molecular weight distribution, Fourier transform infrared spectroscopy (FT-IR), and separation fractions obtained by ultrafiltration were evaluated. The results showed that peanut protein was extensively hydrolyzed to give mainly (up to 96.84%) free amino acids and peptides with low molecular weights (<1000 Da). Furthermore, β-sheets were the major secondary structure. Fractions of 1−3000 Da and <1000 Da prominently contributed to the umami taste and umami enhancement. To obtain umami-enhancing peptides, these two fractions were further purified by gel filtration chromatography, followed by sensory evaluation. These peptides were identified as ADSYRLP, DPLKY, EAFRVL, EFHNR, and SDLYVR by ultra-performance liquid chromatography (UPLC), and had estimated thresholds of 0.107, 0.164, 0.134, 0.148, and 0.132 mmol/L, respectively. According to the results of this work, defatted peanut powder hydrolysate had an umami taste and umami-enhancing effect, and is a potential excellent umami peptide precursor material for the food industry.
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