• Food Science of Animal Resources
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• v.44 no.3
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• pp.551-569
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• 2024

This study was conducted to compare and analyze the changes in the biochemical characteristics and biological activity of peptide extracts derived from Chickso, Hanwoo, and Wagyu beef during digestion. The results of the in vitro digestion analysis revealed that the digestion rate, total free amino acid content, and antioxidant and antihypertensive activities of Chickso loin and shank myofibrillar proteins were significantly higher (p<0.05) than those of Hanwoo and Wagyu loin and shank myofibrillar proteins. Particularly, the peptide extracts of Chickso loin and shank had a high angiotensin-converting enzyme inhibitory activity. In mice in vivo digestion experiment, the blood serum of mice fed with Chickso loin peptide extract (<10 kDa) showed the highest antioxidant enzyme activity. Thus, Chickso peptide extracts were deemed to be similar or more bioactive than Hanwoo and Wagyu peptide extracts, and can be used as bioactive materials.

• Journal of Microbiology and Biotechnology
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• v.22 no.3
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• pp.339-342
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• 2012

This study describes the characterization of a new angiotensin I-converting enzyme (ACE) inhibitory peptide from a Korean traditional rice wine. After purification of the ACE inhibitor peptides with ultrafiltration, Sephadex G-25 column chromatography, and successively $C_{18}$ and SCX solid-phase extraction, reverse-phase HPLC, and size exculsion chromatography, two types of the purified ACE inhibitors with $IC_{50}$ values of 0.34 mg/ml and 1.23 mg/ml were finally obtained. The two purified ACE inhibitors (F-1 and F-2) were found to have two kinds of novel oligopeptides, showing very little similarity to other ACE inhibitory peptide sequences. The amino acid sequences of the two purified oligopeptides were found to be Gln-Phe-Tyr-Ala-Val (F-1) and Ala-Gly-Pro-Val-Leu-Leu (F-2), and their molecular masses were estimated to be 468.7 Da (F-1) and 357.7 Da (F-2), respectively. They all showed a clear antihypertensive effect on spontaneously hypertensive rats at a dosage of 500 mg/kg.

• Food Science of Animal Resources
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• v.44 no.3
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• pp.533-550
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• 2024

Peptides with bioactive effects are being researched for various purposes. However, there is a lack of overall research on pork-derived peptides. In this study, we reviewed the process of obtaining bioactive peptides, available analytical methods, and the study of bioactive peptides derived from pork. Pepsin and trypsin, two representative protein digestive enzymes in the body, are hydrolyzed by other cofactors to produce peptides. Bicinchoninic acid assay, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, chromatography, and in vitro digestion simulation systems are utilized to analyze bioactive peptides for protein digestibility and molecular weight distribution. Pork-derived peptides mainly exhibit antioxidant and antihypertensive activities. The antioxidant activity of bioactive peptides increases the accessibility of amino acid residues by disrupting the three-dimensional structure of proteins, affecting free radical scavenging, reactive oxygen species inactivation, and metal ion chelating. In addition, the antihypertensive activity decreases angiotensin II production by inhibiting angiotensin converting enzyme and suppresses blood pressure by blocking the AT1 receptor. Pork-derived bioactive peptides, primarily obtained using papain and pepsin, exhibit significant antioxidant and antihypertensive activities, with most having low molecular weights below 1 kDa. This study may aid in the future development of bioactive peptides and serve as a valuable reference for pork-derived peptides.

• Journal of Life Science
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• v.13 no.5
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• pp.668-674
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• 2003

This study was carried out to investigate the ACE inhibitory materials of Raja kenojei. Raja kenojei was sperated to fillet and viscera, and these were extracted with hot water. Antihypertensive activity was examined by mesearing angiotensin converting enzyme ACE inhibitory activity. ACE inhibitory activity of viscera at the concentration of 2% for Day 0 showed the highest value by 71.0%. But ACE inhibitory activity of fillet at 2% showed by 29%, which was lower antihypertensive activity than viscera. The protein content of viscerial hot water extracts in proximate composition showed the highest. And also, there was a large amount of aromatic and branched aliphatic amino acids in viscera than those in fillet. For the purification of antihypertensive material in visceral hot water extracts, it was separated and collected by Sephadex G-25 gel chromatography. The fraction (B) of 111 to 160 showed the highest ACE inhibitory activity by 65.1% at the concentration of 0.05%. But the other fractions (A and C) showed lower activity than B. These results demonstrate that crude hot water extracts of viscera from Raj kenojei may be useful as functional food ingredient with antihypertensive property.

• The Journal of Natural Sciences
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• v.16 no.1
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• pp.1-13
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• 2005

The angiotensin I-converting enzyme (ACE) inhibitor has anti-hypertensive effects and has long been used as prevention or remedy of hypertension. This study were carried out to produce and purify a new ACE inhibitor from recombinant E. coli and further elucidate its structure-function relationship. Recombinant pGEX-4T-3 containing ACE inhibitory peptide gene of Saccharomyces cerevisiae was transformed into E. coli BL21(DE3). Glutathione-S transferase (GST) fusion protein from E. Coli BL21(DE3) harboring the recombination pGEX-4T-3 was obtained and the ACE inhibitory peptide was purified with Sephadex G-25 column chromatography. The purified ACE inhibitory peptide was a novel decapeptide with sequence Tyr-Asp-Gly-Gly-Val-Phe -Arg-Val-Tyr-Thr which shows very low similarity to the other ACE inhibitory peptide sequence. The purified ACE inhibitor competitively inhibited ACE.

• Food Science of Animal Resources
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• v.42 no.1
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• pp.46-60
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• 2022

In this study, angiotensin-I-converting enzyme inhibitory (ACEI) activity was evaluated in fermented goat milk fermented by lactic acid bacteria (LAB) from fermented foods and breast milk. Furthermore, the potential for ACEI peptides was identified in fermented goat milk with the highest ACEI activity. The proteolytic specificity of LAB was also evaluated. The 2% isolate was inoculated into reconstituted goat milk (11%, w/v), then incubated at 37℃ until pH 4.6 was reached. The supernatant produced by centrifugation was analyzed for ACEI activity and total peptide. Viable cell counts of LAB and titratable acidity were also evaluated after fermentation. Peptide identification was carried out using nano liquid chromatography mass spectrometry (LC-MS/MS), and potential as an ACEI peptide was carried out based on a literature review. The result revealed that ACEI activity was produced in all samples (20.44%-60.33%). Fermented goat milk of Lc. lactis ssp. lactis BD17 produced the highest ACEI activity (60.33%; IC₅₀ 0.297±0.10 mg/mL) after 48 h incubation, viable cell counts >8 Log CFU/mL, and peptide content of 4.037±0.27/mL. A total of 261 peptides were released, predominantly derived from casein (93%). The proteolytic specificity of Lc. lactis ssp. lactis BD17 through cleavage on the amino acid tyrosine, leucine, glutamic acid, and proline. A total of 21 peptides were identified as ACEI peptides. This study showed that one of the isolates from fermented food, namely Lc. lactis ssp. lactis BD17, has the potential as a starter culture for the production of fermented goat milk which has functional properties as a source of antihypertensive peptides.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.44 no.2
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• pp.118-125
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• 2011

In this study, an angiotensin I-converting enzyme (ACE) inhibitor from squid skin was purified and characterized. Squid (Todarodes pacificus) skin protein isolates were hydrolyzed using six commercial proteases: alcalase, ${\alpha}$-chymotrypsin, neutrase, papain, pepsin, and trypsin. The peptic hydrolysate had the highest ACE inhibitory activity. The ACE inhibitory peptide was purified using Sephadex G-25 column chromatography and reverse phase high-performance liquid chromatography (HPLC) with a $C_{18}$ column. The purified ACE inhibitory peptide was identified and sequenced, and found to consist of seven amino acid residues: Ser-Ala-Gly-Ser-Leu-Val-Pro (657Da). The $IC_{50}$ value of the purified ACE inhibitory peptide was 766.2 ${\mu}M$, and Lineweaver-Burk plots suggested that the purified peptide acts as a noncompetitive ACE inhibitor. These results suggest that the ACE inhibitory peptide purified from the peptic hydrolysate of squid skin may be of benefit in developing antihypertensive drugs and functional foods.

• YAKHAK HOEJI
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• v.56 no.3
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• pp.191-197
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• 2012

We previously reported that the novel isoflavone-free peptide mixture (black soybean peptide, BSP) had several beneficial effects like antiobesity and hypotriglyceridemic effect. However, there are no reports for BSP on anti-hypertensive activity. BSP induced heme oxygenase-1 (HO-1) in HUVECs, thus investigated the HO-1-induced activity in HUVECs and the anti-hypertensive effects in SHR animal model. BSP significantly induced HO-1 expression both at transcriptional and protein levels in a time- and dose-dependent manner as measured by RT-PCR and Western blot analysis, respectively. These inductions were abolished by pretreatment of N-acetyl-cystein (NAC, 1~10 mM), but not by employing Tempol, a superoxide dismutase (SOD) mimetic (1~5 mM). As expected, enzymatic activity (~2 fold) determined by bilirubin formation assay and cGMP concentration (~6 fold) were significantly increased in BSP-treated cells. Based on the numerous evidences on the beneficial effects of HO-1 and our results, we investigated in vivo effects of BSP on the antihypertensive activity. The administration of BSP (1% in drinking water) significantly decreased mean blood pressure (BP) (from $218.6{\pm}6.99$ to $190.0{\pm}3.42$ mm Hg, p<0.01). This result indicates that BSP is strong inducer of HO-1 expression, which may be triggered by oxidative stress, and has anti-hypertensive activity.

• KSBB Journal
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• v.14 no.5
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• pp.600-605
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• 1999

For the production of angiotensin I converting enzyme inhibitory peptides as a material for antihypertensive functional foods from animal blood produced in slaughterhouse, the optimum condition for enzymatic hydrolysis to yield a peptide fraction of the highest activity were investigated with a respect of industrial production. Among several industrially-usable enzymes tested, $Alcalase^？$ produced hydrolysates of the highest activity from total plasma and purified albumin. $IC_50$ values of albumin hydrolysate and its third fraction separated by gel chromatography were 0.5 and 0.02 mg/mL, respectively. The fraction was found to be obtained by a simple ultrafiltration using a membrane of MW cutoff 1,000. The possibility for the industrial production of antihypertensive peptides from animal blood plasma protein was suggested.

• Food Science and Biotechnology
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• v.14 no.6
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• pp.772-777
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• 2005

The goal of this study was to screen and characterize the physiological functions of Korean traditional wines (TW) and liquors (TL). Forty-two TW and TL were collected and evaluated for quality and cardiovascular activities. Ethanol content ranged from $9.0%{\sim}41%$, and pH ranged from $3.0{\sim}7.8$, and they also contained 0.01% to 0.67% of total acid. Samples contained a maximum of 2.0% of crude protein and $0.1%{\sim}14.0%$ of reducing sugar. Commercial CM-wine showed the highest antihypertensive angiotensin I-converting enzyme (ACE) inhibitory activity, 85.9%. The greatest fibrinolytic activity and platelet aggregation inhibitory activity were also found in commercial CM-wine (31.8U) and commercial SS2-wine (38.6 %), respectively. Commercial SHBI-liquor showed the highest HMG-CoA reductase inhibitory activity, 78%. The ACE inhibitor from commercial CM-wine was a peptide compound and also showed an antihypertensive effect in spontaneous hypertensive rats at a dosage of 1.5 mg/kg.