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. 2022 Dec 9;11(24):3991.
doi: 10.3390/foods11243991.

Novel Peptide Sequences with ACE-Inhibitory and Antioxidant Activities Derived from the Heads and Bones of Hybrid Groupers (Epinephelus lanceolatus × Epinephelus fuscoguttatus)

Pei-Teng Chan  1 , Patricia Matanjun  1 , Cahyo Budiman  2 , Rossita Shapawi  3 , Jau-Shya Lee  1
Affiliations

Novel Peptide Sequences with ACE-Inhibitory and Antioxidant Activities Derived from the Heads and Bones of Hybrid Groupers (Epinephelus lanceolatus × Epinephelus fuscoguttatus)

Pei-Teng Chan et al. Foods. .

Abstract

The heads and bones of hybrid groupers are potential precursors for angiotensin-converting enzyme (ACE)-inhibitory and antioxidant peptides. The aim of this study was to isolate the dual-action peptides from the Alcalase-treated head and bone hydrolysate of hybrid groupers followed by identification of the novel peptides. The stability of these peptides against stimulated in vitro gastrointestinal digestion (SGID) was also determined. Fraction HB-IV (less than 1 kDa) obtained from ultrafiltration showed the strongest ACE-inhibition ability (IC50: 0.28 mg/mL), which was comparable to the potency of the commercial supplement, PeptACE (IC50: 0.22 mg/mL). This fraction also demonstrated the highest hydroxyl radical scavenging and metal-chelating activities. However, further fractionation of HB-IV by a series of chromatography resulted in peptide fractions of reduced ACE-inhibitory and antioxidant activities. The hydroxyl radical scavenging and reduction potential of HB-IV were enhanced, whereas ACE-inhibitory and metal-chelating activities were reduced following SGID. A total of 145 peptide sequences were identified from HB-IV, of which 137 peptides were novel to the BIOPEP database. The results suggested that the bioactive peptides isolated from the heads and bones of hybrid groupers could be used as functional foods/ingredients with potential ACE-inhibitory and antioxidant effects.

Keywords: ACE-inhibition kinetic; Alcalase; gastrointestinal digestion; hydroxyl radical scavenging activity; metal-chelating activity; reducing power.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Process flow diagram for the separation of ACE-inhibitory and antioxidant peptides from the Alcalase-treated bone hydrolysate.
Figure 2
Figure 2
(A) The molecular weight distribution of HB-control and Al-HB after passage through a Superdex Peptide 10/300 GL column. (B) The ACE-inhibitory and antioxidant activities of the HB-control and Al-HB. The values represent the mean ± SD. Means without a common letter (a, b) on the bars indicate significant difference at p < 0.05.
Figure 3
Figure 3
(A) The elution profile of HB-IV fraction separated by anion exchange chromatography on a QFF column. (B) The protein content and bioactivities of each collected fractions (F1–F3). The values represent the mean ± SD. Mean without a common letter (a–c) on the bars indicate significant difference at p < 0.05.
Figure 4
Figure 4
(A) The elution profile of F1 fraction on a Superdex Peptide 10/300 GL gel filtration column. (B) The protein content and bioactivities of the collected fractions (F1-A and F1-B). The values represent the mean ± SD. Means without a common letter (a, b) on the bars indicate significant difference at p < 0.05.
Figure 5
Figure 5
The effect of in vitro stimulated gastrointestinal digestion on HB-IV and PeptACE. (A) The bioactivities of HB-IV and PeptACE during SGID. (B) The molecular weight distribution of HB-IV and PeptACE before and after SGID. The values represent the mean ± SD. Means without a common letter (a–c) on the bars indicate significant difference at p < 0.05.
Figure 6
Figure 6
The Lineweaver–Burk plots for the inhibition of ACE by different concentrations of (a) PeptACE and (b) HB-IV.
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