• 약학회지
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• 제56권5호
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• pp.309-313
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• 2012

Antiobesity, hypotriglyceridemic and antihypertensive activities of isoflavone-free peptide mixture (black soybean peptide, BSP) were reported in our previous experiments. In the present study, angiotensin converting enzyme inhibitory (ACEi) activity was decreased in the aorta tissues of spontaneously hypertensive rats (SHRs) treated with BSP (1% in drink water) for 4 weeks, but not in serum. BSP administration significantly decreased ACE activity by 17.5% (from $33.2{\pm}4.5$ to $27.4{\pm}1.96$ mUnit/mg, p=0.0013) in aorta tissue hydrolysate. BSP treatment also decreased significantly mean blood pressure (BP) (from $213.0{\pm}16.96$ to $184.0{\pm}6.53$ mmHg, p<0.0001) as expected. These results indicate that BSP has antihypertensive activity as well as ACEi activity.

• Journal of Microbiology and Biotechnology
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• 제14권6호
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• pp.1318-1323
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• 2004

This study describes the purification and characterization of a novel antihypertensive angiotensin 1­converting enzyme (ACE) inhibitory peptide from Saccharomyces cerevisiae. Maximal production of the ACE inhibitor from Saccharomyces cerevisiae was obtained from 24 h of cultivation at $30^{\circ}C$ and its ACE inhibitory activity was increased by about 1.5 times after treatment of the cell-free extract with pepsin. After the purification of ACE inhibitory peptides with ultrafiltration, Sephadex G-25 column chromatography, and reverse-phase HPLC, an active fraction with an $IC_{50}$ of 0.07 mg and $3.5\%$ yield was obtained. The purified peptide was a novel decapeptide, showing very low similarity to other ACE inhibitory peptide sequences, and its amino acid sequence was Tyr-Asp-Gly-Gly-Val-Phe-Arg-Val-Tyr-Thr. The purified inhibitor competitively inhibited ACE and also showed a clear antihypertensive effect in spontaneously hypertensive rats (SHR) at a dosage of 1 mg/kg body weight.

• Journal of Microbiology and Biotechnology
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• 제22권3호
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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.

• 한국식품영양과학회지
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• 제29권4호
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• pp.737-742
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• 2000

대두발효식품의 기능성 탐색 연구의 일환으로 Bacillus natto 를 접종한 납두의 발효과정 중 고혈압을 유발하는 angiotension converting enzyme의 저해 peptide를 분리하고 저해효과를 검토함으로서 대두발효식품의 우수성을 입증하기 위한 과학 적 접근을 시도하고자 하였다. 납두는 Bacillus natto균을 이용하여 제조하였고, 2$0^{\circ}C$, 3$0^{\circ}C$, 4$0^{\circ}C$, 5$0^{\circ}C$, 6$0^{\circ}C$에서 0~72시간 동안 배양하면서 protein량, protease activity, ACE 저해율 을 측정하고 저해활성을 가지는 peptide를 정제 후 아미노산 조상을 분석하였다. Bacillus natto에 의한 납두의 발효시간이 경과함에 따라 protein 함량이 증가하여 4$0^{\circ}C$, 60시간에서 최대를 나타낸 후 감소하였다. 발효시간에 따른 protease activity는 4$0^{\circ}C$, 60 시간 배양이 최적의 조건이었으며, 최적 발효조건에 따라 납두를 제조한 후 20 mM sodium phosphate buffer(pH 7.0)를 가해 추출한 추출물을 Amicon membrane YM-3 filtration 과 Sephadex G-10, G-25를 이용한 gel filtration으로 부분정제하였다. 또한 정제한 peptide는 첨가함량이 높아질수록 저해활성은 높게 나타났으며, 1 mg 정도의 peptide 함량으로 74.74%의 저해율 을 나타내었다. 정제한 peptide의 아미노산 조성은 alanine(30.84%), phenylalanine(30.03%), histidine(20.24%) 순서로 그 함량이 높게 나타났다.

• Journal of Animal Science and Technology
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• 제47권1호
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• pp.83-90
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• 2005

ACE-inhibitory peptides derived from goat's whey hydrolyzed by various proteolytic enzymes were separated and purified for antihypertension materials. The highest ACE-inhibitory activity of goat's whey hydrolysates was 85.5 % by pepsin for 72 hrs. Also the highest ACE-inhibitory activity of goat's whey hydrolysates was F-4 by pepsin for 72 hrs by Sephadex G-25 gel chromatograms. F-4e and F-4ed from F-4 by RP-HPLC to first and second purification were the highest in ACE-inhibitory activity, respectively. The most abundant amino acid was leucine(I 8.54 %) in F-4ed of ACE-inhibitory peptides after second purification. Amino acid sequence of F-4ed of ACE-inhibitory peptides showed Leu-Lys-Asp-Tyr-Gly-GlyVal- Ser-Leu and Leu-Gly-Asp-Gly-Ala-Gly- Asp-Val-Ala-Phe. $IC_{50}$ calibrated in peptic hydrolysates(72 hrs), F-4, F-4e and F-4ed from goat's whey hydrolysates by pepsin for 72 hrs were 33.93, 28.75, 11.74 and 1.09 mg/ml, respectively. From the results of this experiment, goat's whey hydrolysate by pepsin was shown to have ACE-inhibitory activity.

• Journal of Dairy Science and Biotechnology
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• 제16권2호
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• pp.98-105
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• 1998

Various peptides derived from food are among the most potent physiologically active agents known, and include anticancer peptides, angiotensin converting enzyme(ACE) inhibitor exhibiting antihypertension action, opioid peptides, antithrombotic peptides, hypocholesterolemic peptides, immunomodulators, calcium absorption enhancers, and other peptides. Hydrophobic peptides extracted from a Cheddar-type cheese slurry were fractionated by gel chromatography and repeated HPLC. A peptide fraction from HPLC showed high cytotoxicity on the tumor cell lines such as a human colon carcinoma, and comprised of Tyr, Ser, Leu, Gly, and others. Hypocholesterolemic peptides were isolated from peptic hydrolyzates of casein and soy proteins. Macropeptides of 1,000${\sim}$5,000 dalton were effective on reducing the cholesterol level of mouse serum. Peptides showing high Krigbaum hydrophobicity and ANS surface hydrophobicity resulted in high hypocholesterolemic effect and fecal steroid concentrations. Caseinomacropeptides(CMP) were isolated from whey powder and treated with soluble and immobilized trypsin to obtain antithrombotic peptides. One fraction from the CMP hydrolyzed with immobilized trypsin for 24h exhibited high antithrombotic activity with 52.5% inhibition of platelet aggregation. These result suggested that peptides from various milk products could be utilized as a good bioactive agents for developing health functional foods.

• 한국유가공학회:학술대회논문집
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• 한국유가공기술과학회 1998년도 제46회 춘계 유가공 심포지움 - 우유 및 유제품의 기능성
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• pp.22-29
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• 1998

Various peptides derived from food are among the most potent physiologically active agents known, and include anticancer peptides, angiotensin converting enzyme(ACE) inhibitor exhibiting antihypertension action, opioid peptides, antithrombotic peptides, hypocholesterolemic peptides, immunomodulators, calcium absorption enhancers, and other peptides. Hydrophobic peptides extracted from a Cheddar-type cheese slurry were fractionated by gel chromatography and repeated HPLC. A peptide fraction from HPLC showed high cytotoxicity on the tumor cell lines such as a human colon carcinoma, and comprised of Tyr, Ser, Leu, Gly, and others. Hypocholesterolemic peptides were isolated from peptic hydrolyzates of casein and soy proteins. Macropeptides of 1,000${\sim}$5,000 dalton were effective on reducing the cholesterol level of mouse serum. Peptides showing high Krigbaum hydrophobicity and ANS surface hydrophobicity resulted in high hypocholesterolemic effect and fecal steroid concentrations. Caseinomacropeptides (CMP) were isolated from whey powder and treated with soluble and immobilized trypsin to obtain antithrombotic peptides. One fraction from the CMP hydrolyzed with immobilized trypsin for 24h exhibited high antithrombotic activity with 52.5% inhibition of platelet aggregation. These results suggested that peptides from various milk products could be utilized as a good bioactive agents for developing health functional foods.

• Asian-Australasian Journal of Animal Sciences
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• 제18권5호
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• pp.741-746
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• 2005

To investigate the basic information and the possibility of ACE-inhibitory peptides for antihypertension materials, goat's caisin (CN) was hydrolyzed by various proteolytic enzymes and ACE-inhibitory peptides were separated and purified. ACE-inhibition ratios of enzymatic hydrolysates of goat's CN and various characteristics of ACE-inhibitory peptides were determined. ACE-inhibition ratios of goat's CN hydrolysates were shown the highest with 87.84% by pepsin for 48 h. By Sephadex G-25 gel chromatograms, Fraction 3 from goat's CN hydrolysates by pepsin for 48 h was confirmed the highest ACE-inhibition activity. Fraction 3 g and Fraction 3 gh from peptic hydrolysates by RP-HPLC to first and second purification were the highest in ACE-inhibition activity, respectively. The most abundant amino acid was leucine (18.83%) in Fraction 3 gh of ACE-inhibitory peptides after second purification. Amino acid sequence analysis of Fraction 3 gh of ACE-inhibitory peptides was shown that the Ala-Tyr-Phe-Tyr, Pro-Tyr-Tyr and Tyr-Leu. IC$_{50}$ calibrated in peptic hydrolysates at 48 h, Fraction 3, Fraction 3 g and Fraction 3 gh from goat's CN hydrolysates by pepsin for 48 h were 29.89, 3.07, 1.85 and 0.87 g/ml, respectively. Based on the results of this experiment, goat's CN hydrolysates by pepsin were shown to have ACE-inhibitory activity.

• Mycobiology
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• 제48권5호
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• pp.399-409
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• 2020

Many of the 𝛽-glucans are known to have antihypertensive activities, but, except for angiotensin-converting enzyme II inhibition, the underlying mechanisms remain unclear. Corin is an atrial natriuretic peptide (ANP)-converting enzyme. Activated corin cleaves pro-ANP to ANP, which regulates water-sodium balance and lowers blood pressure. Here, we reported a novel antihypertensive mechanism of 𝛽-glucans, involved with corin and ANP in mice. We showed that multiple oral administrations of 𝛽-glucan induced the expression of corin and ANP, and also increased natriuresis in mice. Microarray analysis showed that corin gene expression was only upregulated in mice liver by multiple, not single, oral administrations of the 𝛽-glucan fraction of Phellinus baumii (BGF). Corin was induced in liver and kidney tissues by the 𝛽-glucans from zymosan and barley, as well as by BGF. In addition to P. baumii, 𝛽-glucans from two other mushrooms, Phellinus linteus and Ganoderma lucidum, also induced corin mRNA expression in mouse liver. ELISA immunoassays showed that ANP production was increased in liver tissue by all the 𝛽-glucans tested, but not in the heart and kidney. Urinary sodium excretion was significantly increased by treatment with 𝛽-glucans in the order of BGF, zymosan, and barley, both in 1% normal and 10% high-sodium diets. In conclusion, we found that the oral administration of 𝛽-glucans could induce corin expression, ANP production, and sodium excretion in mice. Our findings will be helpful for investigations of 𝛽-glucans in corin and ANP-related fields, including blood pressure, salt-water balance, and circulation.

• 한국해양바이오학회지
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• 제14권1호
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• pp.9-24
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• 2022

Low-molecular weight peptides derived from fish collagen exhibit several bioactivities, including antioxidant, antiwrinkle, antimicrobial, antidiabetic, and antihypertension effects. These peptides are also involved in triglyceride suppression and memory improvement. This study aimed to investigate the optimal processing condition for preparing low-molecular weight peptides from flounder skin, and the properties of the hydrolysate. The optimal processing conditions for peptic hydrolysis were as follows: a ratio of pepsin to dried skin powder of 2% (w/w), pH of 2.0, and a temperature of 50℃. Peptic hydrolysate contains several low-molecular weight peptides below 300 Da. Gly-Pro-Hyp(GPHyp) peptide, a process control index, was detected only in peptic hydrolysate on matrix-assisted laser desorption/ionization-time-of-flight(MALDI-TOF) spectrum. 2,2'-azinobis-(3-3-ethylbenzothiazolline-6- sulfonic acid(ABTS) radical scavenging activity of the peptic hydrolysate was comparable to that of 1 mM ascorbic acid, which was used as a positive control at pH 5.5, whereas collagenase inhibition was five times higher with the peptic hydrolysate than with 1 mM ascorbic acid at pH 7.5. However, the tyrosinase inhibition ability of the peptic hydrolysate was lower than that of arbutin, which was used as a positive control. The antibacterial effect of the peptic hydrolysate against Propionibacterium acne was not observed. These results suggest that the peptic hydrolysate derived from a flounder skin is a promising antiwrinkle agent that can be used in various food and cosmetic products to prevent wrinkles caused by ultraviolet radiations.