• 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.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 2005.10a
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• pp.290-293
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• 2005

장내 단백질 가수분해효소에 의한 casein 분해산물들의 ACE 저해 활성을 비교하기 위하여 인공위액, 인공장액 및 인공위액과 장액 연속처리를 각각 반응조건으로 일정시간 casein을 가수분해한 후 각 효소 가수분해물이 혈압상승 peptide 생성효소인 Angiotensin converting enzyme(ACE)에 대한 저해활성을 측정하였다. 각 소화액에 따른 가수분해물은 모두 ACE 저해활성을 나타내었으며, 2시간 효소처리를 하였을 때, 인공위액, 인공장액, 인공위액과 장액 가수분해물은 각각 69%, 80% 및 88%로 최대 ACE 저해활성을 보였다. 그리고 casein의 가수분해 정도를 확인하기 위한 SDS-PAGE에서는 인공위액으로 처리한 군보다 인공장액으로 처리한 군이 더 작은 분자량으로 분해되는 것을 확인할 수 있었고, 인공위액과 장액을 함께 처리한 군에서는 1시간 안에 대부분의 분해가 이루지는 것을 관찰할 수 있었다.

• Korean Journal of Medicinal Crop Science
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• v.10 no.5
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• pp.399-402
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• 2002

Angiotensin converting enzyme(ACE) belongs to the class of zinc protease and plays an important role in the regulation of blood pressure. In this experiment, we investigated the inhibitory activities of medicinal plant extracts on ACE. Fifty medicinal plants were selected and the extracts were prepared by refluxing with 70% methanol. Among the extracts, eleven medicinal plant extracts such as Sedum sarmentosum Bunge, Petasites japonicus(s.et z.) Max, Rubus coreanus, Morus bombycis Koidz, Acorus calamus var. angustatus, Glycyrhiza glabra, Equisetum hyemale, Portulaca oleracea L., Prunella vulgaris var. lilacina Nakai, Sorbus commixta Hedl, Allium thunbergii showed more than 50% inhibitory activities, and Paeonia suffruticosa Andr., lnula helenium, Acanthopanax senticosus Harms, Dendrobium moniliforme, Juglans mandshurica, Zizyphus jujuba, Leonurus artemisia, Aster scaber Thunb, Vitex rotundifolia, Platycodon grandiflorum, Prunus persica, Ligularia fischeri showed $40{\sim}49%$ inhibitory activities. Therefore these extracts which contain high ACE inhibitory activities may be useful as antihypertension agents and to the treatment of hypertension.

• Korean Journal of Food Science and Technology
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• v.27 no.2
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• pp.230-234
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• 1995

Angiotensin converting enzyme(ACE) inhibitory peptides lowering blood pressure were fractionated from a commercial soybean paste(Doenjang). When the freeze-dried sample of soybean paste was extracted with cold water, the recovery yield of total nitrogen(TN) was shown to be 73.3% in 30 minutes. The cold water extract was filtered through PM-10 membrane(Amicon) for 3 hours in order to remove high molecular weight polypeptides. The TN and salt of ultrafiltrate were recovered to 80.8% and 99.2%, respectively, and its ACE $IC_{50}$ was $41.8{\mu}g/ml$. When the ultrafiltrate was divided into 7 fractions by reverse phase prep-HPLC, F5 fraction showed the highest ACE inhibitory activity ($IC_{50}=6.8{\mu}g/ml$) and salt could be collected into F1 fraction. Subsequently, the F5 fraction was divided into another five fractions by ion exchange prep-HPLC, all of which appeared to be high ACE inhibitory activity($IC_{50}=2.5{\sim}8.3{\mu}g/ml$). Among them, F53 fraction had the highest ACE inhibitory activity, and its main amino acid component was found to be histidine.

• Food Science of Animal Resources
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• v.30 no.2
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• pp.286-290
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• 2010

Angiotensin-converting enzyme (ACE) inhibitory activity and production optimization of ovotransferrin hydrolysates were studied. Ovotransferrin was hydrolyzed by several enzymes (protamex, alcalase, trypsin, pepsin, neutrase, and flavorzyme) and acid (0.03 N HCl). Ovotransferrin hydrolysate reduced ACE activity by 60.2%, 55.8%, and 42.6% when treated with trypsin, acid, and pepsin, respectively. Trypsin was selected for production of peptide having maximum AC inhibitory effect, which was greatest with 7 h hydrolysis. Central composite design determined that optimum composition of ACE inhibitory substances using substrate concentration of 20-35%, temperature of $35-55^{\circ}C$, and pH of 6.0-8.0. The optimum composition was 1% trypsin, substrate concentration of 26.32%, $51.29^{\circ}C$, and pH 6.32. Under this conditions, a maximum ACE inhibitory effect of 69.1% was evident, similar to the predicted value.

• Asian-Australasian Journal of Animal Sciences
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• v.32 no.3
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• pp.430-436
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• 2019

Objective: This study identified angiotensin I-converting enzyme (ACE) inhibitory peptides in beef M. longissimus injected with thermolysin (80 ppm) and stored for 3 days at $5^{\circ}C$. Methods: Crude peptides (molecular weight <3 kDa) were obtained from the thermolysin hydrolysate and separated into seven fractions. Fraction V showing the highest ACE inhibitory activity was further fractionated, yielding subfractions V-15, V-m1, and V-m2, and selected for superior ACE inhibitory activity. Finally, twelve peptides were identified from the three peak fractions and the ACE inhibitory activity ($IC_{50}$) of each peptide was evaluated. Results: The Leu-Ser-Trp, Phe-Gly-Tyr, and Tyr-Arg-Gln peptides exhibited the strongest ACE inhibitory activity ($IC_{50}$ values of 0.89, 2.69, and 3.09 mM, respectively) and had higher concentrations (6.63, 10.60, and 29.91 pg/g; p<0.05) relative to the other peptides tested. Conclusion: These results suggest that the thermolysin injection process is beneficial to the generation of bioactive peptides with strong ACE inhibitory activity.

• Fisheries and Aquatic Sciences
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• v.16 no.4
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• pp.237-242
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• 2013

We investigated the antioxidant and angiotensin I converting enzyme (ACE) inhibitory activities of red snow crab Chionoecetes japonicas shell (RSCS) hydrolysate by enzymatic hydrolysis and its molecular weight cut-off fractions. The RSCS hydrolysate was fractionated through two ultrafiltration membranes of 3 and 10 kDa cut-offs. Three fractions (<3 kDa, 3-10 kDa, and >10 kDa) were evaluated for total amino acid composition, antioxidant activities using 2'-azino-bis[3-ethylbenzthiazoline-6-sulfonic acid] ($ABTS^+$) radical scavenging and superoxide dismutase (SOD)-like activities and reducing power assays, and ACE inhibitory activity using Hou's method. Although all fractions showed activity, the <3 kDa fraction of RSCS hydrolysate exhibited the greatest $ABTS^+$ radical scavenging, SOD-like and ACE inhibitory activities. However, these fractions exhibited low reducing power. These results suggest that the low-molecular-weight enzymatic hydrolysate of RSCS could be used as a functional ingredient to control oxidative stress and ACE activity.

• Food Science and Biotechnology
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• v.18 no.2
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• pp.541-545
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• 2009

Water and ethanol extracts were prepared from the haesongi mushroom (Hypsizigus marmoreus) to measure functional components. The ability of the extracts to inhibit angiotensin-converting enzyme (ACE) and their hypoglycemic effects were also determined; the latter was measured by $\alpha$-amylase and glucosidase inhibition. Extraction yield, protein content, total phenol, and $\beta$-glucan in the water extracts were 55.86, 17.71, 1.89, and 21.93%, respectively. The respective values for the ethanol extracts were lower than those for water extracts. Both water and ethanol extracts showed dosedependent ACE inhibition, the effect of the former being greater. The water extract inhibited ACE activity by 95.34% at 40 mg/mL. The $IC_{50}$ values of the water extracts were 63.32 and 0.41 mg/mL for $\alpha$-amylase and glucosidase, respectively. Thus, the water extracts had a greater hypoglycemic effect than the ethanol extracts. From these results, water is a better solvent than ethanol to extract from the haesongi mushroom functional components that show ACE inhibition and have hypoglycemic effects.

• Journal of Dairy Science and Biotechnology
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• v.32 no.1
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• pp.7-16
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• 2014

Angiotensin-I-converting enzyme (ACE) inhibitory peptides have functional and potential properties of casein hydrolysates that are used in the development of food ingredients and anti-hypertensive hydrolysates derived from sodium caseinate enzymatic hydrolysates. Sodium caseinate could be treated by various kinds of commercial proteases, and then could be treated with the enzyme combination. Ultrafiltration treatment can be used to generate hydrolysates that can be used to determine ACE inhibitory activity. In general, hydrolysate quality can be evaluated by changes in hydrolysis characteristics, ACE inhibitory activity, as well as functional properties such as solubility, foam capacity, cytotoxicity, free radical-scavenging effects, and sensory evaluation. In this review, we present an overview of the ACE inhibitory peptides obtained by performing enzymatic hydrolysis on various sources to identify food ingredients and functional foods that reduce hypertension.

• Journal of Life Science
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• v.22 no.2
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• pp.220-225
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• 2012

The peptides of enzymatic hydrolysates from oyster were determined by inhibitory activity against angiotensin-converting enzyme. The ACE inhibitory activity of enzymatic oyster hydrolysates increases with hydrolysis time. Among enzymatic oyster hydrolysates, oyster hydrolysates incubated with Protamex showed the best ACE inhibitory activity after 10 h. Hydrolysates were filtered through a HiSep ultrafiltration membrane (M.W. cut-off 30 kDa, 10 kDa) to obtain the peptide fractions with ACE inhibition activity. These fractions were applied to an HPLC column (watchers 120 ODS-AP $250{\times}4.6$ ($5{\mu}m$)). Six active fractions were collected and the range of ACE inhibition was from 29.56 to 85.85%. Peptide was purified from fraction B, showing the highest ACE inhibitory activity, and its sequence was Leu-Gln-Pro. These results suggest that PEH may be beneficial for developing antihypertensive food and drug.