• Preventive Nutrition and Food Science
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• v.13 no.3
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• pp.196-203
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• 2008

Hwangtae, dried Alaska pollack, is a major storage product in the fish processing industry. Hwangtae is prepared by removing the internal organs and drying outdoors during the cold witner months by allowing it to thaw during the daytime and re-freeze at night under sub-zero ($-10^{\circ}C$) conditions and gradually dry from December until the next April for around 5 months from Myungtae. In this study, ground Hwangtae was hydrolyzed using two proteolytic enzymes (pepsin and alcalase) which produced five soluble active peptides from Hwangtae (yellowish dried Pollack, Theragra chalcogramma) protein. Two different peptides with strong antioxidative activity were isolated from the hydrolysate using consecutive chromatographic methods of Sephadex G-25 gel, ion-exchange chromatography on a Sepharose-Sephadex C-25 gel, and high-performance liquid chromatography. The isolated peptides, APO1 and APO2, were composed of 16 and 13 amino acid residues, respectively. Both peptides contained a Gly residue at the C-terminus and the repeating motif Gly-Pro-Hyp. The peptide with a molecular weight less than 1,000 Daltons (APACE) obtained from enzymatic hydrolysates of Hwangtae exhibited the highest ACE inhibitory activity. The APACE peptides was composed of 4 amino acid residues (Gly-Leu-Leu-Pro). These results suggest that Hwangtae hydrolysates could be a good source of peptides with ACE inhibitory activity. Biochemical analysis indicated that two 70 kDa peptides (APG1 and APG2) isolated from the hydrolysate had gelatinoytic activity, which was shown to be a calcium dependent protease type as showed by gelatin SDS PAGE.

• 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.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.27 no.1
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• pp.1-6
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• 1994

Hydrolyzates which inhibit the angiotensin-I converting enzyme(ACE) were prepared from defatted anchovy meal by pepsin. These were tested for inhibitory activity against ACE, which is one of the hypertension inducing factors. The ACE inhibitory activity of the hydrolyzates increased until 20hrs of hydrolysis had elapsed but slightly decreased after that time. And presence of $50\%$ ethanol soluble peptide-nitrogen increased slowly up to 12hrs of hydrolysis, and then mainly increased until 20hrs of hydrolysis was completed. From the profiles of gel permeation chromatography on a Bio-gel P-2 of $50\%$ ethanol soluble fraction obtained from hydrolyzate for 20hrs, the higher active fractions were 2'($IC_{50}=45\;{\mu}g\;protein/ml$) and 4'($IC_{50}=76\;{\mu}g\;protein/ml$). Amino acid analysis showed major quantities of glutamic acid, leucine, lysine for 2'and aspartic acid, threonine for 4' respectively.

• Food Science of Animal Resources
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• v.26 no.4
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• pp.511-516
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• 2006

The objectives of this study was to compare the probiotic characteristics of lactic acid bacteria (LAB) for their ability to assimilate cholesterol, production of bacteriocin, inhibition of angiotensin I-converting enzyme (ACE), and viability under artificial gastrointestinal fluids. Among tested lactic acid bacteria, L167 strain exhibited the highest ACE inhibitory activity (58.75%). The production of ACE inhibitory peptide derived from fermented milk by L167 strain started at the beginning of stationary phase with maximum activity occurring late of the stationary phase. The highest ACE inhibitory activity was observed at 20 h in 10% skim milk medium. L155 strain exhibited cholesterol assimilation activity compared with probiotic strains such as Lactobacillus acidophilus ATCC 43121. With addition of bacteriocin culture, viable cells of Staphylococcus aureus in fermented sausage were slightly decreased during storage. Among selected strains of LAB, 3 strains weve identified as L. plantarum (L155, L165, L167), and two strains were identified as Pediococcus damnosus (L12) and L. paracasei ssp. paracasei (P113) by use of API carbohydrate fermentation pattern and physiological tests.

• Preventive Nutrition and Food Science
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• v.3 no.4
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• pp.379-381
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• 1998

An angiotensin converting enzyme (ACE) inhibitor was isolated and partially purified from bovine blood plasma. Bovine blood plasma was obtained after removing blood cells by centrifugation, followed by the addition of anticoagulant to whole bovine blood. To precipitate plasma proteins, bovine blood plasma was treated with 4% trichloroacetic acid (TCA) as a final concentration .An ACE inhibitor was isolated from TCA supernatnat, using ultrafiltration, gel permeation chormatography, and reverse-phase high pressure liquid chromatogrpahy. The ACE inhibitor purified from TCA supernatant had IC50 values of 9.4$\mu$M.

• Asian-Australasian Journal of Animal Sciences
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• v.16 no.9
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• pp.1384-1389
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• 2003

In order to clarify one of the biological functions of pork, we investigated whether a peptic hydrolysate of denatured porcine crude myosin showed inhibitory activity against angiotensin I-converting enzyme (ACE), which contributed to hypertension. Our results indicated that this hydrolysate showed relatively strong activity, and we therefore attempted to separate the involved peptides, which were considered to be active substances. To isolate these active peptides, the hydrolysate was separated using a solidphase separation, gel filtration high-performance liquid chromatography (HPLC), and two kinds of reverse phase HPLC. In each stage of separation, many fractions were detected, almost all of which showed ACE inhibitory activity. Thus, we suggested that the activity of the hydrolysate as a whole was a result of the activities of the many individual peptides. Six peaks were distinguished, with yields from 34 to 596 ppm of original crude myosin. In addition to the six peaks, many other active fractions were found throughout the separation steps, strongly suggesting that whole porcine crude myosin itself had ACE inhibitory activity. Moreover, pork as food was considered to function as an ACE inhibitory material in vivo, because pork proteins consist primarily of crude myosin, which included almost all the myofibrillar structural proteins.

• Journal of the Korean Society of Food Science and Nutrition
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• v.38 no.2
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• pp.177-181
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• 2009

The peptides from Aroase AP10 enzymatic hydrolysates of octopus proteins were isolated and tested for inhibitory activity against angiotensin converting enzyme (ACE). The Aroase AP10 hydrolysates were filtered through PM-10 membrane (M.W. cut-off 10,000) to obtain the peptides fractions with ACE inhibition activity. These fractions were applied to a Biogel P-2 column. Three active fractions (A, B, and C) were collected and applied to a SuperQ-Toyopearl 650S column chromatography, leading to the isolation of four active fractions (A-1, A-2, B-1, and C-1). Among the active fractions, C-1 had the highest ACE inhibitory activity ($IC_{50}=3.10{\mu}g$). The main composition of its amino acids is arginine, lysine, histidine and leucine, which cover about 60% of the total amino acids.

• Food Science of Animal Resources
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• v.35 no.6
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• pp.738-747
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• 2015

Angiotensin-converting enzyme (ACE) inhibitory activity was evaluated for the low-molecular-weight fraction (<3 kDa) obtained from milk fermentation by Bifidobacterium longum KACC91563. The ACE inhibitory activity in this fraction was 62.3%. The peptides generated from the <3 kDa fraction were identified by liquid chromatography-electrospray ionization quantitative time-of-flight mass spectrometry analysis. Of the 28 peptides identified, 11 and 16 were identified as β-casein (CN) and α_s1-CN, respectively. One peptide was identified as κ-CN. Three peptides, YQEPVLGPVRGPFPIIV, QEPVLGPVRGPFPIIV, and GPVRGPFPIIV, from β-CN corresponded to known antihypertensive peptides. We also found 15 peptides that were identified as potential antihypertensive peptides because they included a known antihypertensive peptide fragment. These peptides were as follows: RELEELNVPGEIVE (f1-14), YQEPVLGPVRGPFP (f193-206), EPVLGPVRGPFPIIV (f195-206), PVLGPVRGPFPIIV (f196-206), VLGPVRGPFPIIV (f197-206), and LGPVRGPFPIIV (f198-206) for β-CN; and APSFSDIPNPIGSENSEKTTMPLW (f176-199), SFSDIPNPIGSENSEKT- TMPLW (f178-199), FSDIPNPIGSENSEKTTMPLW (f179-199), SDIPNPIGSENSEKTTMPLW (f180-199), DIPNPIGSENSEKTTMPLW (f181-199), IPNPIGSENSEKTTMPLW (f182-199), PIGSENSEKTTMPLW (f185-199), IGSENSEKTTMPLW (f186-199), and SENSEKTTMPLW (f188-199) for α_s1-CN. From these results, B. longum could be used as a starter culture in combination with other lactic acid bacteria in the dairy industry, and/or these peptides could be used in functional food manufacturing as additives for the development of a product with beneficial effects for human health.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 2005.05a
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• pp.226-230
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• 2005

본 연구는 고혈압을 억제하는 ACE inhibitory peptide가 한우에 함유되어 있는지를 조사하기 위한 기초연구로 한우의 우둔과 등심으로부터 Myosin B를 추출하여 가열한 것과 가열하지 않은 것으로 구분하여 pepsin으로 0, 1, 3, 6시간 동안 $37^{\circ}C$에서 가수분해 시켰다. 가수분해물을 전기영동을 실시하여 pepsin 처리시간에 따른 단백질의 변화를 검토하였고, ACE 저해 활성을 측정하였다. 전기영동의 결과 가열한 것은 가열하지 않은 것에 비해서 단백질의 변성과 소멸이 많이 일어나 밴드의 수가 적었다. Pepsin으로 가수분해한 시간이 길어짐에 일부 단백질이 소실되었고, 저분자의 단백질이 생성되었다. Pepsin으로 가수분해함에 따라 등심과 우둔에서 25, 32, 40 및 44 kDa는 소실되었고, 37 kDa의 분자량을 갖는 밴드는 생성되었으며, 27 kDa의 단백질은 처음상태 그대로 유지되었다. 가수분해물을 이용하여 ACE 저해활성도를 측정한 결과, 등심은 1시간 가수분해시 유의차가 있었으나, 우둔은 가열여부에 따라 유의차가 발견되지 않았다. 반면 등심과 우둔 모두 가수분해 시간이 증가하면 ACE 저해율은 상승하는 경향을 보였다. 이와 같은 결과를 토대로 한우로부터 추출한 Myosin B의 ACE 억제활성이 우수한 단백질분획을 찾아 아미노산 염기서열을 밝히고 고혈압 억제제로 합성 개발하는 연구를 차후 추진할 예정이다.

• Food Science and Biotechnology
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• v.14 no.6
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• pp.772-777
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• 2005

The goal of this study was to screen and characterize the physiological functions of Korean traditional wines (TW) and liquors (TL). Forty-two TW and TL were collected and evaluated for quality and cardiovascular activities. Ethanol content ranged from $9.0%{\sim}41%$, and pH ranged from $3.0{\sim}7.8$, and they also contained 0.01% to 0.67% of total acid. Samples contained a maximum of 2.0% of crude protein and $0.1%{\sim}14.0%$ of reducing sugar. Commercial CM-wine showed the highest antihypertensive angiotensin I-converting enzyme (ACE) inhibitory activity, 85.9%. The greatest fibrinolytic activity and platelet aggregation inhibitory activity were also found in commercial CM-wine (31.8U) and commercial SS2-wine (38.6 %), respectively. Commercial SHBI-liquor showed the highest HMG-CoA reductase inhibitory activity, 78%. The ACE inhibitor from commercial CM-wine was a peptide compound and also showed an antihypertensive effect in spontaneous hypertensive rats at a dosage of 1.5 mg/kg.