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. 2022 Jun 26;11(13):1889.
doi: 10.3390/foods11131889.

Purification and Identification of a Novel Angiotensin Converting Enzyme Inhibitory Peptide from the Enzymatic Hydrolysate of Lepidotrigla microptera

Xuejia Hu  1 , Zhiyuan Dai  1 , Renyao Jin  1
Affiliations

Purification and Identification of a Novel Angiotensin Converting Enzyme Inhibitory Peptide from the Enzymatic Hydrolysate of Lepidotrigla microptera

Xuejia Hu et al. Foods. .

Abstract

In this study, Lepidotrigla microptera were hydrolyzed with four different proteolytic enzymes (Papain, neutrase, flavourzyme, and alcalase), and their distribution of molecular weights and ACE-inhibitory activity were tested. The alcalase hydrolysates showed the maximum ACE-inhibitory activity. A novel ACE-inhibitory peptide was isolated and purified from Lepidotrigla microptera protein hydrolysate (LMPH) using ultrafiltration, gel filtration chromatography, and preparative high performance liquid chromatography (prep-HPLC). The amino acid sequence of the purified peptide was identified as Phe-Leu-Thr-Ala-Gly-Leu-Leu-Asp (DLTAGLLE), and the IC50 value was 0.13 mg/mL. The ACE-inhibitory activity of DLTAGLLE was stable across a range of temperatures (<100 °C) and pH values (3.0−11.0) and retained after gastrointestinal digestion. DLTAGLLE was further identified as a noncompetitive inhibitor by Lineweaver−Burk plot. The molecular docking simulation showed that DLTAGLLE showed a high binding affinity with ACE sites by seven short hydrogen bonds. As the first reported antihypertensive peptide extracted from alcalase hydrolysate of Lepidotrigla microptera, DLTAGLLE has the potential to develop functional food or novel ACE-inhibitor drugs.

Keywords: ACE inhibitory peptide; Lepidotrigla microptera; identification; molecular docking; stability.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Molecular mass distribution of standards (a), and molecular mass distribution of LMPH obtained by papain, neutrase, flavourzyme, and alcalase (b).
Figure 2
Figure 2
Gel filtration chromatography of LMPH I on a Sephadex G-15 column (a), and ACE-inhibitory activities of fractions F1–F5 (b). The column values of a–d with the different superscript indicated a significant difference (p < 0.05).
Figure 3
Figure 3
Chromatograph obtained by prep-HPLC of fraction F4 (a) and ACE inhibitory activities of fractions F4-1–F4-19 (b). The column values of a–n with the different superscript indicated a significant difference (p < 0.05).
Figure 4
Figure 4
Molecular masses and amino acid sequences of ACE-inhibitory peptides from the purified F4-12 fraction. MS/MS spectra of NSSRFGKF (a), DLTAGLLE (b), and REVALGIN (c).
Figure 5
Figure 5
Lineweaver−Burk plots of ACE inhibition by the DLTAGLLE peptide.
Figure 6
Figure 6
Stability of the DLTAGLLE. Effect of temperature (a), pH (b), and gastrointestinal digestion (c) on the ACE inhibitory activity of DLTAGLLE. The column values of A–D, a–d and a*–d* with the different superscript indicated a significant difference (p < 0.05).
Figure 7
Figure 7
Molecular docking simulation of DLTAGLLE binding to ACE. (a) Structure of the peptide. (b) Docking diagram of DLTAGLLE (green) binding to ACE (shown as cartoon). (c) Interaction between DLTAGLLE (green) and residues of ACE (shown as sticks).
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