Rapid purification and characterization of angiotensin converting enzyme inhibitory peptides from lizard fish protein hydrolysates with magnetic affinity separation

Lan, Xin; Liao, Dankui; Wu, Shanguang; Wang, Feng; Sun, Jianhua; Tong, Zhangfa

doi:10.1016/j.foodchem.2015.02.004

Cited by 61 publications

(32 citation statements)

References 18 publications

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“…Two of the main factors that influence a peptide's biological activity are the sequence and position of its amino acids . Former studies on the structure–activity relationship concluded that 2–12 amino acid residues make up the ACEIPs, according to the BIOPEP database . Valine and proline may contribute to the inhibitory activity of antihypertensive peptides, and hydrophobic (valine) and aliphatic amino acids (especially isoleucine and leucine) also compose the N‐terminus of the ACEIPs sequence .…”

Section: Discussionmentioning

confidence: 99%

Comparison of an angiotensin‐I‐converting enzyme inhibitory peptide from tilapia (Oreochromis niloticus) with captopril: inhibition kinetics, in vivo effect, simulated gastrointestinal digestion and a molecular docking study

et al. 2019

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BACKGROUND: In order to utilize tilapia skin gelatin hydrolysate protein, which is normally discarded as industrial waste in the process of fish manufacture, we study the in vivo and in vitro angiotensin-I-converting enzyme (ACE) inhibitory activity of the peptide Leu-Ser-Gly-Tyr-Gly-Pro (LSGYGP). The aim was to provide a pharmacological basis of the development of minimal side effects of ACE inhibitors by comparative analysis with captopril in molecular docking. RESULTS:This peptide from protein-rich wastes showed excellent ACE inhibitory activity (IC 50 = 2.577 mol L −1 ) and exhibited a mixed noncompetitive inhibitory pattern with Lineweaver-Burk plots. Furthermore, LSGYGP and captopril groups both showed significant decreases in blood pressure after 6 h and maintained good digestive stability over 4 h. Molecular bond interactions differentiate competitive captopril upon hydrogen bond interactions and Zn(II) interaction. The C-terminal Pro generates three interactions (hydrogen bonds, hydrophilic interactions and Van der Waals interactions) in the peptide and effectively interactswith the S1 and S2 pockets of ACE. CONCLUSION: LSGYGP, with an IC 50 value of 2.577 mol L −1 , has an antihypertensive effect in spontaneously hypertensive rats. Through comparison with captopril, this study revealed that LSGYGP may be a potential food-derived ACE inhibitory peptide and could act as a functional food ingredient to prevent hypertension.

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Section: Discussionmentioning

confidence: 99%

Comparison of an angiotensin‐I‐converting enzyme inhibitory peptide from tilapia (Oreochromis niloticus) with captopril: inhibition kinetics, in vivo effect, simulated gastrointestinal digestion and a molecular docking study

et al. 2019

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“…Furthermore, among the N-terminal amino acids of the highly active short-chain peptides, the branched-chain aliphatic amino acids I and V are predominant. Interestingly, the most potent ACE inhibitory peptide derived from shrimp waste protein contain aliphatic amino acids such as A, L, I, G and P. Glycine, aspartic acid, proline and alanine were all shown in other ACE inhibitory peptides from food proteins, such as ACE inhibitory peptides from jellyfish [36] from chum salmon [9] and from lizard fish [37].…”

Section: Identification Of the Ace Inhibitory Peptidesmentioning

confidence: 99%

Identification and molecular docking of novel ACE inhibitory peptides from protein hydrolysates of shrimp waste

Krichen

Sila

Caron

et al. 2018

Engineering in Life Sciences

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The effect of enzymatic hydrolysis by Savinase on the interfacial properties and antihypertensive activity of shrimp waste proteins was evaluated. The physicochemical characterization, interfacial tension, and surface characteristics of shrimp waste protein hydrolysates (SWPH) using different enzyme/substrate (E/S) (SWPH5 (SWPH using E/S = 5), SWPH15 (SWPH using E/S = 15), and SWPH40 (SWPH using E/S = 40)) were also studied. SWPH5, SWPH15, and SWPH40 had an isoelectric pH around 2.07, 2.17, and 2.54 respectively. SWPH5 exhibited the lowest interfacial tension (68.96 mN/m) followed by SWPH15 (69.36 mN/m) and SWPH40 (70.29 mN/m). The in vitro ACE inhibitory activity of shrimp waste protein hydrolysates showed that the most active hydrolysate was obtained using an enzyme/substrate of 15 U/mg (SWPH15). SWPH15 had a lower IC50 value (2.17 mg/mL) than that of SWPH5 and SWPH40 (3.65 and 5.7 mg/mL, respectively). This hydrolysate was then purified and characterized. Fraction F1 separated by Sephadex G25 column which presents the best ACE inhibition activity was then separated by reversed‐phase high performance liquid chromatography. Four ACE inhibitory peptides were identified and their molecular masses and amino acid sequences were determined using ESI–MS and ESI–MS/MS, respectively. The structures of the most potent peptides were SSSKAKKMP, HGEGGRSTHE, WLGHGGRPDHE, and WRMDIDGDIMISEQEAHQR. The structural modeling of anti‐ACE peptides from shrimp waste through docking simulations results showed that these peptides bound to ACE with high affinity.

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“…In recent years, many peptides with ACEinhibitory activity have been prepared from the proteins of various organisms, e.g. Enteromorpha clathrata [11], Pacific cod (Gadus macrocephalus) skin gelatin [13], Grass carp protein [14], Agaricus bisporus [15], fermented shrimp pastes [16], silkworm pupa (Bombyx mori) protein [17], lizard fish protein hydrolysates [18], flounder fish (Paralichthys olivaceus) muscle [19], sweet sorghum grain protein [20] and cauliflower by-products protein hydrolysate [21]. The amino-acid sequences of these ACE-inhibitory peptides are summarized in Table 1.…”

Section: Amino-acid Sequence Of the Purified Peptidementioning

confidence: 99%

Preparation of an ACE-inhibitory peptide from Perinereis aibuhitensis protein

Chen

Wang

2017

Biotechnology & Biotechnological Equipment

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The peptides with angiotensin-I converting enzyme (ACE)-inhibition activity were prepared from Perinereis aibuhitensis protein (PAP) by hydrolysis with neutral protease, in which the ACE-inhibition rate of peptides derived from PAP was monitored. The hydrolysis conditions were optimised as follows: reaction time 5 h, temperature 50 C, pH 7 and enzyme amount 0.5%. Under the optimum hydrolysis conditions, the ACE-inhibition rate of peptides of PAP reached up to 83.61%. The hydrolysates were fractionated into two molecular-weight ranges (below and above 10 kDa) by ultrafiltration. The below-10-kDa fraction with higher ACE-inhibitory was subsequently purified by Sephadex G-15 gel filtration chromatography. The structure of the active peptide was identified as Gly-Ala-Phe by high performance liquid chromatography (HPLC) coupled with quadrupole (Q) time-of-flight (TOF) mass spectrometry (HPLC-Q-TOF-MS). Thus, the peptide prepared from PAP by hydrolysis with neutral protease could be a beneficial ingredient of nutraceuticals and pharmaceuticals against hypertension.

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Rapid purification and characterization of angiotensin converting enzyme inhibitory peptides from lizard fish protein hydrolysates with magnetic affinity separation

Cited by 61 publications

References 18 publications

Comparison of an angiotensin‐I‐converting enzyme inhibitory peptide from tilapia (Oreochromis niloticus) with captopril: inhibition kinetics, in vivo effect, simulated gastrointestinal digestion and a molecular docking study

Comparison of an angiotensin‐I‐converting enzyme inhibitory peptide from tilapia (Oreochromis niloticus) with captopril: inhibition kinetics, in vivo effect, simulated gastrointestinal digestion and a molecular docking study

Identification and molecular docking of novel ACE inhibitory peptides from protein hydrolysates of shrimp waste

Preparation of an ACE-inhibitory peptide from Perinereis aibuhitensis protein

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