• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.2
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• pp.226-233
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• 1993

Enzymatic hydrolysates of food proteins (defatted soybean cake, egg albumin and casein) were tested for inhibitory activity against angiotensin-I converting enzyme (ACE). Food proteins were hydrolysed with complex enzyme, bromelain, alcalase, $\alpha$-chymotrypsin, trypsin, papain and pepsin by heating method. The hydrolysates obtained from the treatment of complex enzyme and bromelain showed the higher ACE inhibitory activity. ACE inhibitory activity of hydrolysates exhibited a tendency to be increased until 8hrs and increased with increment of concentration. The activity was also stable by heat treatment at 10$0^{\circ}C$ for 20min. Molecular weight of active fraction was about 1, 400 and defatted soybean cake hydrolysate below 1, 400 in case of defatted soybean cake hydrolysate treated with alcalase. Amino acid of the active fractions was abundant in Asp, Glu, Lys, lle, Leu, Ala and Val.

• Korean Journal of Plant Resources
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• v.21 no.1
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• pp.12-18
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• 2008

Antioxidative activity and inhibitory activity of angiotensin I converting enzyme(ACE), aminopeptidase N(APN) and $\alpha$-amylase were investigated in the methanol extracts from 25 fern plants native to Jeju Island, in order to screen the plant species containing bioactive materials for functional foods or medicines. The antioxidative activity was higher in Cytomium fortunei(41.9%) and Rumohra standishii(34.1%) than in leaves of Thea sinensis(30.9%), a small tree for antioxidative beverage. Inhibitory activities of ACE and APN were relatively high in Cytomium fortunei as 26.7% and 28.2% respectively. $\alpha$-Amylase inhibitory activity was higher than 50% in 10 species. Particularly, Cytomium fortunei(87.4%) and Dryopteris erythrosora(71.6%) showed the inhibitory activities higher than those of other form plants. Of 25 fern plants investigated here, Cytomium fortunei showed not only the highest antioxidative activity but also the highest inhibitory activity of ACE, APN and $\alpha$-amylase. It suggests that Cytomium fortunei could be potentially used as a resource of bioactive materials for fuctional foods or medicines.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 2005.10a
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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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• v.5 no.2
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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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• v.10 no.3
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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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• v.16 no.4
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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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• v.12 no.2
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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.

• The Korean Journal of Food And Nutrition
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• v.31 no.2
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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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• v.31 no.3
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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.

• Food Science of Animal Resources
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• v.31 no.6
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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.