• Journal of Animal Science and Technology
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• 제49권1호
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• pp.129-136
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• 2007

본 실험은 한우 육단백질의 가수분해물로부터 항고혈압 활성을 측정하기 위하여 실시한 것으로서 한우 등심과 우둔으로부터 추출한 myosin B를 pepsin으로 가수분해하여 가수분해물들의 전기영동 결과, 가열처리와 가수분해 시간의 증가에 따라 단백질의 소실이 증가하였다. 항 고혈압 활성을 측정한 결과 10 ug/ml의 희석된 가수분해물의 ACE 억제효과는 1시간 이상 가수분해 시키면 약 40%의 억제율을 가졌다. 가수분해물 원액으로 ACE 억제효과를 살펴본 결과에서는 등심이 우둔보다 높았으며 (p<0.05), 비가열 가수분해물이 가열한 가수분해물 보다 억제율이 높게 나타났다 (p<0.05). 또한, 가수분해 시간별 처리구에서는 1시간 이상 가수분해 시키면 약 70% 이상의 억제율을 갖는 것으로 나타나 한우의 myosin B를 1시간 이상 가수분해하면 ACE 억제율이 증진되는 것으로 사료된다.

• 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.

• Fisheries and Aquatic Sciences
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• 제15권3호
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• pp.183-190
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• 2012

The purpose of this study was the purification and characterization of an angiotensin I converting enzyme (ACE) inhibitory peptide purified from enzymatic hydrolysates of rainbow trout Oncorhynchus mykiss muscle. After removal of lipid, the approximate composition analysis of the rainbow trout revealed 24.4%, 1.7%, and 68.3% for protein, lipid, and moisture, respectively. Among six hydrolysates, the peptic hydrolysate exhibited the highest ACE inhibitory activity. We attempted to purify ACE inhibitory peptides from peptic hydrolysate using high performance liquid chromatography on an ODS column. The $IC_{50}$ value of purified ACE inhibitory peptide was $63.9{\mu}M$. The amino acid sequence of the peptide was identified as Lys-Val-Asn-Gly-Pro-Ala-Met-Ser-Pro-Asn-Ala-Asn, with a molecular weight of 1,220 Da, and the Lineweaver-Burk plots suggested that they act as a competitive inhibitor against ACE. Our study suggested that novel ACE inhibitory peptides purified from rainbow trout muscle protein may be beneficial as anti-hypertension compounds in functional foods.

• 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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• 제40권3호
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• pp.93-102
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• 2022

본 연구는 L. plantarum K79를 이용하여 ACE 억제활성 향상을 위한 최적의 발효조건을 RSM을 이용하여 예측하고자 하였다. 4개의 독립변수[탈지유(포도당 1% 첨가) 농도(6%-14%), 배양 온도(32℃-42℃), 배양 시간(8-24시간), 스타터 첨가량(0.02%-0.2%)] 5단계 중심 합성 설계 및 반응 표면 분석법을 사용하여 최적의 발효 조건을 결정하는 데 사용하였다. 종속변수는 ACE 억제 활성과 pH였다(이때 ACE 억제율은 조건별 발효원액에서 100배 희석하여 나타낸 값이다). 결정 계수(R²)는 ACE 억제 활성, pH에 대해 각각 0.791, 0.905이었다. 최대 ACE 억제 활성은 10% 탈지유(포도당 1% 첨가) 농도, 37℃ 배양 온도, 17.8 h 배양 시간 및 0.2% 스타터 첨가량 조건에서 90%이었다. RSM에 기초하여 예측된 최적 발효 ACE 조건은 탈지유(포도당 1% 첨가) 농도 13.49%, 스타터 0.0578%, 배양온도 33.4℃에서 21.5시간 동안 배양할 때 ACE 억제 활성 및 pH의 예측 값은 86.69% 및 pH 4.6이었으며 실제 값은 각각 85.5%와 pH 4.58이었다.

• 한국수산과학회지
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• 제44권2호
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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.

• 생명과학회지
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• 제13권5호
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• pp.668-674
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• 2003

홍어를 발효하여 발효기간에 따른 항고혈압 효과를 조사하고 그에 따른 항고혈압성 물질을 분리하기 위해 GPC system을 사용하여 항고혈압 물질을 조 분리하였다. 항고혈압성 물질을 농축하기 위해 홍어 내장 및 가식부 열수 추출물을 대량 포집 하였다. 그리고 그에 따른 ACE 억제효과를 검색하였다. 즉, 홍어 가식 부의 ACE 저해 작용은 2% 첨가시 29%로, 다소 낮으나 상시 섭취될 수 있는 식품이란 측면에서 볼 때 그 유용성이 기대된다고 할 수 있으며 홍어 내장 열수 추출물의 ACE 저해 효과는 시료 2% 첨가의 경우 발효 0일째에 71.0%로 가장 높게 나타났다. 발효가 진행되면서 ACE 저해 효과는 감소하는 것으로 나타났다. 이러한 ACE 억제효과를 나타내는 성분을 추정하기 위하여 홍어 내장 열수 추출물의 일반성분과 원소분석을 실시한 결과 일반성분 중 순단백질이 58.7%로 가장 높게 나타났으며, 원소분석 결과 C, H, O, N의 성분비가 당류라기 보다는 peptide계인 것으로 나타났다. 또한, 질소화합물의 분석결과 ACE를 억제하는 기능성 peptide의 성분인 Tyr, Phe, Val, His 등이 가식부 보다 많아서 ACE를 억제하는 peptide를 함유하리라 예상되었다. ACE억제 물질을 조 분리하기 위하여 Sephadex G-25 column chromatography에 의해 분자량별로 분획한 결과, 분획물 들의 ACE 저해 효과는 분획물 B(111-160)의 농도 0.2%에서 67.8%로 가장 높은 ACE저해 효과를 나타내었다. 이상의 결과로 미루어 보아 홍어 내장 열수 추출물의 ACE 저해인자는 가열에 대하여 안정한 비교적 저분자의 peptide와 같은 물질이라고 추정할 수 있었다.

• Biotechnology and Bioprocess Engineering:BBE
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• 제9권5호
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• pp.400-404
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• 2004

This Study was tarried out to investigate the relationship ACE inhibitory activity and degradations of sulfur containing materials in Dolsan leaf mustard juice (DLMJ). The changes of sulfur containing materials which were treated with autolysis, myrosinase, ascorbate and papain were studied, as well as the changes of ACE inhibitory activity in DLMJ. At $37^{\circ}C$, sulfur contain-ing materials by autolysis decreased most rapidly from $0.43\%$ to $0.13\%$ in the second day. Conversely. ACE inhibitory activity increased most from $66\%$ to $87\%$. in the second day at $37^{\circ}C$. As myrosinase concentrations increased more, sulfur containing materials in DLMJ decreased more. The ACE inhibitory activities at 0, 0.5, 1, 2, and 4 Units of myrosinase for 240 min later were 70, 74, 75, 82, and $85\%$, respectively. At 1 mM ascorbate. concentrations of Sulfur containing materials in DLMJ decreased more significantly on the second day than on the other days. At 1 mM ascorbate for 6 days, ACE Inhibitory activity reached a maximum of about $92\%$. And, an increase of papain concentration was noted in accordance with a decreased sulfur containing materials. The maximum rate of AEC inhibitory activity at control, 3, 6, and 12 Units of papains treatments was shown as 70, 70, 75, and $78\%$ at 60 min, respectively. These results suggested that the degradation of sulfur containing materials led to the increase of ACE inhibitory activity. Consequently, it was suggested that ACE inhibiting was significantly related to the degradatives of sulfur containing materials.

• Fisheries and Aquatic Sciences
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• 제5권1호
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• pp.21-27
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• 2002

Angiotensin I converting enzyme inhibitory activities of shelled krill (Euphausia superba) hydrolysates by autolysis and by hydrolysis with commercial proteases were analyzed. Among the proteases, Alcalase was the most effective protease for the hydrolysis of krill considering the degree of hydrolysis $(87.5\%)$ and the ACE inhibitory activity $(60\%)$. Four hour hydrolysis suggested as the most suitable and economic. In order to establish the optimum hydrolysis condition of krill, degree of hydrolysis and ACE inhibitory activity as affected by Alcalase concentration and water amount added were statistically analyzed by response surface methodology (RSM). The optimum hydrolysis condition was $2.0\%$ Alcalase hydrolysis in 2 volumes (v/w) of water at $55\% for 4 hr. The hydrolysate prepared from the optimum hydrolysis condition was fractionated by molecular weight. The lower molecular weight fraction showed the higher ACE inhibitory activity. $IC_{50}$ of the fraction under 500 Da was 0.57mg protein/mL.

• 한국식품영양학회지
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• 제18권1호
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• pp.11-18
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• 2005

Angiotensin Ⅰ converting enzyme(ACE) inhibitory activities of laver(Porphyra tenera) protein hydrolysates were investigated by enzymes used for hydrolysis, molecular fractions and drying methods. For the enzymatic hydrolysis, crude laver protein, separated by filtration of water extract of dried laver extracted with 20 times(w/v) water for 3 hours at boiling temperature, were hydrolyzed with three commercial protease, Pepsin, alcalase and maxazyme NNP at optimal conditions. The yield of hydrolysis and ACE inhibitory activities of which were high in order of pepsin, alcalase and maxazyme NNP. ACE inhibitory activities of laver hydrolysates by molecular levels were high in order of 3 kDa > 10 kDa > 3∼10 kDa, and the IC/sub 50/ ACE inhibitory activities by molecular lebels were 4 mg/mL(3 kDa), 5 mg/mL(total hydrolysate), and 20 mg/mL(10 kDa), respectively. The storage stability of dried laver hydrolysates at 20℃ were strongly affected by drying methods, hot air dried of which were much stabler than freeze-dried one.