Isolation and characterization of nutraceutically potential ACE-Inhibitory peptides from leatherjacket (Meuchenia sp.) protein hydrolysates

Salampessy, Junus; Reddy, N. Venkata; Phillips, Mike; Kailasapathy, Kasipathy

doi:10.1016/j.lwt.2017.03.004

Cited by 64 publications

(30 citation statements)

References 25 publications

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“…A number of sequences could be identified, with molecular weights ranging from 866.47 to 2,857.27 Da (Table ). Peptides with molecular weight under 3 kDa have been portrayed as those with strongest ACE‐inhibitory and antioxidant activities, (Ren et al, ; Salampessy, Reddy, Phillips, & Kailasapathy, ; Wang, Chen, Fu, Li, & Wei, ) in tune with our findings. In addition, sequences in Table are rich (above 50%) in hydrophobic and aromatic amino acids, reported to increase antioxidant and ACE‐inhibitory activities (Shazly et al, ; Zhuang, Tang, & Yuan, ).…”

Section: Resultssupporting

confidence: 90%

Identification and synthesis of multifunctional peptides from wheat germ hydrolysate fractions obtained by proteinase K digestion

et al. 2019

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Wheat germ protein hydrolysate (WGPH) was obtained by proteinase K digestion, in order to produce bioactive antioxidant and antihypertensive peptides. Response surface methodology (RSM) was used to optimize hydrolysis conditions (enzyme‐to‐substrate ratio, time, and temperature) for antioxidant activity of hydrolysates. The crude WGPH produced in this way significantly inhibited angiotensin‐I converting enzyme (ACE) in a concentration‐dependent manner. It was next fractionated by reversed‐phase semi‐preparative High Performance Liquid Chromatography (HPLC) into 12 fractions that were examined for antioxidant and antihypertensive activities. Fractions with antioxidant and ACE‐inhibitory activities were then submitted to further analysis by nano‐LC‐ESI‐MS‐MS. Among the various peptides identified, MDATALHYENQK (IC50: 293.3 ± 6.5 µg/ml) and SGGSYADELVSTAK (IC50: 265.5 ± 8.3 µg/ml) displayed antioxidant activity and VALTGDNGHSDHVVHF (IC50: 189.3 ± 4.05 µg/ml), VDSLLTAAK (IC50: 159.7 ± 0.33 µg/ml), MDATALHYENQK (IC50: 303.6 ± 2.47 µg/ml), IGGIGTVPVGR (IC50: 125.7 ± 2.3 µg/ml) and SGGSYADELVSTAK (IC50: 128.2 ± 1.17 µg/ml) showed good ACE‐inhibitory activity. Practical applications Wheat milling industries produce massive amounts of wheat germ as by‐product that can be converted into valuable compounds. The present research indicates that proteinase K is useful to hydrolyze wheat germ proteins in a search for bioactive peptides with antioxidant and ACE‐inhibitory properties. The identified peptides can be regarded as functional food additives, or nutraceuticals to improve human health.

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Section: Resultssupporting

confidence: 90%

Identification and synthesis of multifunctional peptides from wheat germ hydrolysate fractions obtained by proteinase K digestion

et al. 2019

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“…It is known that the ACE inhibition is strongly influenced by the type of amino acid composition of peptides. A series of studies have figured out that binding to ACE is influenced by hydrophobic amino acid residues (aromatic or branched chain) at three positions from the C-terminus of the peptide [30,31]. Some branched chain aliphatic amino acids, such as Ile and Val, are predominant in potent peptide inhibitors [32].…”

Section: Characterization Of Ace Inhibitory Peptide By Nano Uhplc-esimentioning

confidence: 99%

Novel ACE Inhibitory Peptides Derived from Simulated Gastrointestinal Digestion in Vitro of Sesame (Sesamum indicum L.) Protein and Molecular Docking Study

Wang

Lü

Sun

et al. 2020

IJMS

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The aim of this study was to isolate and identify angiotensin I-converting enzyme (ACE) inhibitory peptides from sesame protein through simulated gastrointestinal digestion in vitro, and to explore the underlying mechanisms by molecular docking. The sesame protein was enzymatically hydrolyzed by pepsin, trypsin, and α-chymotrypsin. The degree of hydrolysis (DH) and peptide yield increased with the increase of digest time. Moreover, ACE inhibitory activity was enhanced after digestion. The sesame protein digestive solution (SPDS) was purified by ultrafiltration through different molecular weight cut-off (MWCO) membranes and SPDS-VII (< 3 kDa) had the strongest ACE inhibition. SPDS-VII was further purified by NGC Quest™ 10 Plus Chromatography System and finally 11 peptides were identified by Nano UHPLC-ESI-MS/MS (nano ultra-high performance liquid chromatography-electrospray ionization mass spectrometry/mass spectrometry) from peak 4. The peptide GHIITVAR from 11S globulin displayed the strongest ACE inhibitory activity (IC50 = 3.60 ± 0.10 μM). Furthermore, the docking analysis revealed that the ACE inhibition of GHIITVAR was mainly attributed to forming very strong hydrogen bonds with the active sites of ACE. These results identify sesame protein as a rich source of ACE inhibitory peptides and further indicate that GHIITVAR has the potential for development of new functional foods.

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“…In vitro, fish-scale collagen peptides reduced the expression of pro-inflammatory cytokines [16]. Several peptides with ACE inhibitory activity have been identified from bluefin tuna [17], leatherjacket [18], Atlantic salmon [19,20], boarfish [21], rockfish [22], skate [23], and Pangasius catfish [24].…”

Section: Introductionmentioning

confidence: 99%

Valorization of Fish by-Products: Purification of Bioactive Peptides from Codfish Blood and Sardine Cooking Wastewaters by Membrane Processing

et al. 2020

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Codfish blood and sardine cooking wastewaters were processed using membrane ultrafiltration that allowed for the preparation of bioactive peptides enriched fractions. The raw materials and corresponding permeates were characterized chemically and in terms of biological properties. The fractionation process was evaluated by analyzing the selective permeation of small peptides (<1 kDa) from larger compounds when using membranes with different molecular weight cut-offs (MWCOs) combined with different materials (MW, PW, and UP010 for codfish blood) and when operated at different transmembrane pressures (with GH for sardine cooking wastewaters). A rejection of the protein/peptides >10 kDa was achieved for both raw materials with the studied membranes. Also, low values of rejection of peptides <1 kDa were accomplished, namely 2% with UP010 from codfish blood and 23% when operated at minimum pressure (1.0 bar) with GH from sardine wastewaters. The peptide fractions from codfish blood with MW and UP010 exhibited the highest ABTS+ and ORAC values. Peptide fractions from sardine wastewaters with GH demonstrated no improvement in antioxidant activity compared to sardine wastewaters. The antimicrobial results showed that the peptide fractions from codfish blood with UP010 and from sardine with GH at 1.0 bar were capable of inhibiting Escherichia coli growth.

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Isolation and characterization of nutraceutically potential ACE-Inhibitory peptides from leatherjacket (Meuchenia sp.) protein hydrolysates

Cited by 64 publications

References 25 publications

Identification and synthesis of multifunctional peptides from wheat germ hydrolysate fractions obtained by proteinase K digestion

Identification and synthesis of multifunctional peptides from wheat germ hydrolysate fractions obtained by proteinase K digestion

Novel ACE Inhibitory Peptides Derived from Simulated Gastrointestinal Digestion in Vitro of Sesame (Sesamum indicum L.) Protein and Molecular Docking Study

Valorization of Fish by-Products: Purification of Bioactive Peptides from Codfish Blood and Sardine Cooking Wastewaters by Membrane Processing

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