• 한국식품영양과학회지
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• 제22권2호
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• pp.226-233
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• 1993

효소에 의한 가수분해로 식품단백질로부터 생리활성 peptide의 생성을 밝히기 위한 연구의 일환으로 효소에 의한 단백질 가수분해물의 ACE 저해작용을 검토한 결과는 다음과 같다. 1. 가수분해에 따른 ACE 저해능은 가수분해 8시간까지는 급격히 증가하다가 그 후로는 완만하게 증가하였으며, 특히 복합효소, bromelain 및 pepsin등에 의해 우수하게 나타났다. 그러나 trypsin 및 $\alpha$-chymotrypsin에 의한 egg albumin 및 casein 가수분해시에는 가수분해 8시간 이후에는 오히려 감소하는 경향을 나타내었다. 2. 단백질 가수분해물의 ACE 저해능은 첨가량의 증가와 함께 우수한 것으로 나타났으며, 가열에 대하여 비교적 안정한 것으로 나타났다. 3. 단백질 가수분해물의 아미노산 조성은 거의 유사한 것으로 나타났으며, 특히 glutamic acid의 함량이 월등히 많은 것으로 나타났다. 그러나 egg albumin 가수분해물의 경우는 glutamic acid의 함량이 적은 반면 alanine 및 cysteine의 함량이 다소 많은 것으로 나타났다 4. Gel 여과에 의한 단백질 가수분해물의 획분별 ACE 저해작용은 서로 비슷한 획 분에서 나타났으며 이 때의 분자량은 1,400부근으로 나타났다. 5. Gel 여과에 의한 ACE 저해작용 획분의 아미노산 조성은 서로 다른 것으로 나타났다.

• 한국자원식물학회지
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• 제21권1호
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• pp.12-18
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• 2008

제주도에 자생하는 양치식물 25종을 대상으로 항산화활성, ACE 저해활성, APN 저해활성 및 $\alpha$-amylase 저해활성을 검색하였다. 항산화활성은 쇠고비와 일색고사리에서 비교적 높아서 항산화 음료로 애용되고 있는 차나무 잎보다도 더 높았다. ACE 저해활성과 APN 저해활성은 전체적으로 낮았으나, 쇠고비에서 각각 26.7%와 28.2%으로 비교적 높은 저해활성을 나타내었다. $\alpha$-Amylase 저해활성은 10종이 50% 이상의 높은 활성으로 보였으며, 그 중에서 쇠고비와 홍지네고사리의 저해활성이 특히 높았다. 이상의 결과로부터 쇠고비는 항산화활성뿐만 아니라 ACE 저해활성, APN 저해활성과 $\alpha$-amylase 저해활성 모두 다른 식물에 비해 높아 생리활성 물질의 분리 및 동정 등 식품소재 및 식물생약으로 이용하기 위한 후속 연구가 기대된다.

• 한국축산식품학회:학술대회논문집
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• 한국축산식품학회 2005년도 제36차 추계 학술발표대회
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• pp.329-333
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• 2005

ACE inhibition activity of peptides was measured after 2 months of storage at $4^{\circ}C$ under condition of pH 6.0, 6.5, 7.0, 7.5, 8.0. and the ACE inhibitory activity were changed only slightly. After 2 months of chilled storage ($4^{\circ}C$), no dramatic change and significance was found. This indicates that acidic, neutral, weak alkali conditions did not affect ACE inhibitory activity of those peptides. Among peptide 1134, 1152, and 1155, peptides from thermolysin + protease A hydrolysates, inhibition activity of peptide 1134 and 1152 was decreased significantly at $60^{\circ}C$, however, they showed stable inhibition activity from $70^{\circ}C$ to $100^{\circ}C$ (P<0.001). Also, chromatogram of peptide 1134, 1152, and 1155 was shown that retention time of peptide of $60^{\circ}C$ was not correspond to the retention time of the rest of peptides. This indicated that temperature may change the inhibitory activity and profile of peptides.

• Nutrition Research and Practice
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• 제5권2호
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• pp.93-100
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• 2011

Inhibition of angiotensin I-converting enzyme (ACE) activity is the most common mechanism underlying the lowering of blood pressure. In the present study, five organic extracts of a marine brown seaweed Ecklonia cava were prepared by using ethanol, ethyl acetate, chloroform, hexane, and diethyl ether as solvents, which were then tested for their potential ACE inhibitory activities. Ethanol extract showed the strongest ACE inhibitory activity with an $IC_{50}$ value of 0.96 mg/ml. Five kinds of phlorotannins, phloroglucinol, triphlorethol-A, eckol, dieckol, and eckstolonol, were isolated from ethanol extract of E. cava, which exhibited potential ACE inhibition. Dieckol was the most potent ACE inhibitor and was found to be a non-competitive inhibitor against ACE according to Lineweaver-Burk plots. Dieckol had an inducible effect on the production of NO in EAhy926 cells without having cytotoxic effect. The results of this study indicate that E. cava could be a potential source of phlorotalnnins with ACE inhibitory activity for utilization in production of functional foods.

• Preventive Nutrition and Food Science
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• 제10권3호
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• pp.239-243
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• 2005

Angiotensin I-converting enzyme (ACE) inhibitory activities of elk antler hydrolysates prepared with three kinds of proteases, pepsin, trypsin and $\alpha-chymotrypsin$, were investigated. The ACE inhibitory activity of the pepsinolytic hydrolysate was the highest with an $IC_{50}$ value of $9.3\mu g/mL.$ In addition, three kinds of pepsinolytic hydrolysates with relatively high molecular weights (over 10,000 Da), medium molecular weights (5,000 to 10,000 Da), and low molecular weights (below 5,000 Da) were fractionated using an ultrafiltration membrane system. The below 5,000 Da hydrolysate exhibited the highest ACE inhibitory activity. These results indicate that the pepsinolytic hydrolysates of elk velvet antler could be a good source of peptides with ACE inhibitory activity.

• Food Science and Biotechnology
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• 제16권4호
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• pp.565-571
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• 2007

This study was carried out to investigate an optimum condition for the high angiotensin-l converting enzyme (ACE) inhibitory activity and the yield on enzyme concentration, casein concentration, and hydrolysis time. The optimum condition was performed by response surface methodology for acquirement of casein hydrolysate of milk which shows high ACE inhibitory activity, Among 8 tested enzymes, Protamex showed the highest activation degree with 77.03 unit/g from casein. Their hydrolysis degrees of flovourzyme 500MG, protamex, mixture from 1% casein were 85.5, 88.5, and 93.5%, respectively. The ranges of enzyme concentration (0.25-1.25%), casein concentration (2.5-12.5%), and hydrolysis time (20-100 min) as 3 independent variables through preliminary experiments of the yield of casein hydrolysate and ACE inhibitory activity, and it shows optimum response surface at a saddle point. It shows enzyme concentration (0.64%), casein concentration (8.38%), and hydrolysis time (55.81 min) in the yield aspect and showed the highest activity at enzyme concentration (0.86%), casein concentration (5.97%), and hydrolysis time (63.86 min) in ACE inhibitory aspect. The $R^2$ value of a fitted optimum formula on the hydrolysis yield was 0.9751 as the significant level of 1%. The $R^2$ value of a fitted optimum formula on ACE inhibitory activity is 0.8398, and the significance is recognized in the range of 5%.

• Fisheries and Aquatic Sciences
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• 제12권2호
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• pp.79-85
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• 2009

Gelatin hydrolysates with a high inhibitory activity against angiotensin I-converting enzyme (ACE) were fractionated from Alaska pollock surimi refiner discharge. The ACE-inhibitory activity, expressed as $IC_{50}$ (mg/mL), was highest (0.49 mg/mL) in gelatin hydrolysates formed by sequential 2-hr treatments of Pronase and Flavourzyme. After fractionation through four different membrane filters with molecular weight cut-offs of 3, 5, 10, and 30 kDa, the highest ACE-inhibitory activity (0.21 mg/mL) was observed with the 3-kDa filtrate.

• 한국식품영양학회지
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• 제31권2호
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• pp.213-219
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• 2018

This study was performed to determine the optimal time of harvest for ramie leaves with the two varieties (Seocheon Seobang and Seoncheon Baekpi) by comparison of physiological activity and physicochemical characteristics. The crude protein, minerals, ascorbic acid, folate, chlorophyll, ACE inhibitory activity and AChE inhibitory activity were determined. The amount of crude protein in ramie leaf, which was collected in Seocheon-gun, Chungcheongnam-do, grew up steadily from early May to September. The content of calcium in was higher in Baekpi than in Seobang. Seobang displayed its highest value of 3,569.90 mg% in September, while Baekpi displayed its highest value of 3,163.84 mg% in October. Although, folate and vitamin C contents in the two varieties were slightly different, they were higher as the growth date grew in October. The highest value of chlorophyll content was observed in October, which was later in the vegetative state. ACE inhibitory activity and AChE inhibitory activity appeared to be higher in Baekpi than in Seobang. Between June and August, ACE inhibitory activity was highest in Baekpi variety.

• KSBB Journal
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• 제31권3호
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• pp.165-170
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• 2016

This study was carried out for investigate that physiological activity, quantification and qualitative were sinigrin of Dolsan leaf mustard pickle (DLMP) during storage. sinigrin contains high amounts of nutritional and medicinal compounds, which are important for maintaining optimum health. ACE inhibitory activity was ranged between 43.2 and 79.4%. DLMP methanol extracts demonstrated highest ACE inhibitory activity at 79.4% on day 14, whereas DLMP ethanol extracts demonstrated highest Angiotensin I-converting Enzyme (ACE) inhibitory activity of 43.2% at day 0. The ${\alpha}-glucosidase$ inhibitory activity of positive control 0.02% (v/v) acarbose was 78%. The DLMP methanol extracts had the highest ${\alpha}-glucosidase$ inhibitory activity at 64.0% on day 14, whereas DLMP ethanol extracts had the lowest ${\alpha}-glucosidase$ inhibitory activity of 42.8% at day 28. Sinigrin was high in DLMP methanol extracts at $49.55{\mu}g/ml$ on day 14 of storage. Sinigrin standard was eluted at 2.73 min and MS analysis was m/z 283.03 along with fragment ions at m/z 204 and 149.06. These data show that sinigrin formed desulfo-glucosinolates $[M-SO_3-2H_2O+K+2H]^+$. Sinigrin concentration increased until day 14 and then decreased after that. DLMP methanol extracts had consistently higher sinigrin concentration than DLMP acetonitrile extracts during 28 days of storage.

• 한국축산식품학회지
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• 제31권6호
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• pp.886-892
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• 2011

This study investigated the ACE-inhibitory effect of yogurt beverage fortified with hydrolysates as well as the suitability of hydrolysates as a nutraceutical additive to yogurt beverage. Three whey protein hydrolysates hydrolyzed by alcalase, protamex, and trypsin were each added to yogurt beverage at concentrations of 1.25, 2.5, and 5 mg/mL. Yogurt beverage fortified with 2.5 mg/mL of hydrolysates had 61-69% ACE-inhibitory activity, whereas yogurt beverage fortified with 5 mg/mL of hydrolysates showed 74% ACE-inhibitory activity. There were no significant differences in ACE-inhibitory activity between the alcalase or protamex hydrolysates during storage; however, trypsin hydrolysate exhibited significant differences. On the other hand, physicochemical characteristics such as pH (3.47-3.77), titratable acidity (0.81-0.84%), colority, viable cell count, and sensory qualities were not significantly different among the tested yogurt beverage samples during storage. These results showed that yogurt beverage fortified with whey protein hydrolysates maintained antihypertensive activity and underwent no unfavorable changes in physicochemical characteristics regardless of enzyme type.