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. 2022 Apr 30;27(9):2853.
doi: 10.3390/molecules27092853.

Characterization of Peanut Protein Hydrolysate and Structural Identification of Umami-Enhancing Peptides

Lixia Zhang  1 , Xiaojing Sun  1 , Xin Lu  1 , Songli Wei  1 , Qiang Sun  1 , Lu Jin  1 , Guohui Song  1 , Jing You  1 , Fei Li  2
Affiliations

Characterization of Peanut Protein Hydrolysate and Structural Identification of Umami-Enhancing Peptides

Lixia Zhang et al. Molecules. .

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.

Keywords: amino acid sequence; characterization; isolation and purification; peanut protein hydrolysate; umami-enhancing peptide.

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Conflict of interest statement

The authors declare that they have no conflict of interest.

Figures

Figure 1
Figure 1
Taste characteristics of DPH. Different letters denote significant differences (p < 0.05).
Figure 2
Figure 2
Enzymatic hydrolysis characteristics of DPF.
Figure 3
Figure 3
Molecular weight distribution of peptides.
Figure 4
Figure 4
Fourier transform infrared (FT-IR) spectra of DPF and DPH.
Figure 5
Figure 5
Gel filtration chromatography of the mixture of fractions GFC-I, GFC-II, and GFC-III.
See this image and copyright information in PMC

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