• Food Science and Biotechnology
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• 제27권6호
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• pp.1781-1789
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• 2018

In this study, whey proteins were fermented with 34 lactic acid bacteria for 48 h at $37^{\circ}C$ and their ability to inhibit angiotensin 1-converting enzyme (ACE) activity were compared. All the lactic acid bacteria displayed varying proteolytic abilities in whey. Their fermentates also displayed varying abilities to inhibit ACE in vitro. Seven fermentates showed strong ACE inhibitory abilities between $84.70{\pm}0.67$ and $52.40{\pm}2.1%$ with $IC_{50}$ values between $19.78{\pm}1.73$ and $2.13{\pm}0.7mg/ml$. Pediococcus acidilactici SDL1414 showed the strongest ACE inhibitory activity of $84.7{\pm}0.67%$ ($IC_{50}=19.78{\pm}1.73{\mu}g/ml$). Mass spectrometry revealed that more than half (57.7%) of the low molecular weight peptides (< 7 kDa) in the P. acidilactici SDL1414 fermented samples were ACE inhibitory peptides. Our results show that P. acidilactici SDL1414 could be used as a starter culture in the dairy industry to develop antihypertensive functional foods for hypertension management.

• 한국축산식품학회지
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• 제26권4호
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• pp.511-516
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• 2006

발효 소시지의 제조에 starter로 사용한 균주를 선발하기 위해 각 유산균 균주들의 ACE 저해 활성, 콜레스테롤 흡착능력, 발효 육제품 저장 중 S. aureus에 대한 저해 황성을 평가하였다. ACE 저해 활성은 L. plantarum L167이 가장 우수하였고(58.75%), 콜레스테롤 흡착 능력이 우수한 균주로는 L. plantarum L155를 선발하였다. 박테리오신을 생산하는 P. damnosus를 starter로 이용하여 제조한 발효 소시지에 S. aureus를 접종하여 상온 저장 중 생균수를 측정한 결과 저장 35일째에 대조구에 비하여 1 log의 균수 감소 효과가 나타났다.

• 한국식품과학회지
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• 제29권6호
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• pp.1316-1318
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• 1997

산 casein으로부터 FPLC를 이용하여 gel permeation column으로 ${\kappa}-Casein$을 분획한 다음, 이를 chymosin, pepsin, trypsin 으로 각각 처리하여 3% TCA에서 soluble한 부분을 증류수로 투석(MW cut-off 1kDa)시킨 후 ACE저해 효과를 측정한 결과, trypsin으로 분해 시킨 경우 ACE 저해율이 94.7%로 가장 높게 나타났으며, chymosin 가수분해물은 가장 낮았다. GMP를 투석막의 종류에 따라 투석 시킨 후 $IC_{50}$을 측정한 결과, MW cut-off 의 크기가 증가할수록 ACE저해효과는 감소하는 것으로 나타났으며, MW cut-off 2 kDa의 경우가 가장 높은 저해율을 보였고 MW cut-off 5kDa에서는 저해율이 가장 낮았다.

• Mycobiology
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• 제39권2호
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• pp.109-112
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• 2011

Vitis hybrid (Sheridan)-Robus coreanus red wine was vinified by fermentation of a mixture of Vitis hybrid and Robus coreanus must at $25^{\circ}C$ for 10 days. The Vitis hybrid-Robus coreanus red wine had ethanol contents of 10.9%. It had high antihypertensive angiotensin I-converting enzyme (ACE) inhibitory activity of 57.8% and antioxidant activity of 64.8%. Changes in the physicochemical properties and functionality of the Vitis hybrid-Robus coreanus red wine was investigated during a post-fermentation period of three months. The ACE inhibitory activity of the red wine increased as the post-fermentation period prolonged, and showed the highest ACE inhibitory activity of 70.4% 60 days post-fermentation. However, the antioxidant activity declined significantly to 47.2% during the post-fermentation period of 60 days. In terms of sensory evaluation, the Vitis hybrid-Robus coreanus red wine had the best acceptability 60 days post-fermentation.

• 한국식품영양과학회지
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• 제36권12호
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• pp.1511-1516
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• 2007

두충의 기능성 식품으로서 이용 가능성을 평가하기 위하여, 두충의 항고혈압 활성 물질을 분리 및 확인하였고, 각 부위별(잎, 껍질, 줄기) 추출물의 관련물질의 함량 및 ACE 저해활성을 조사하였다. 두충에서 분리한 항고혈압성 물질로 추정되는 8A는 순도 95.64%의 pinoresinol-4,4'-di-O-${\beta}$-D-glucoside(PDG)로서 자연건조 및 볶은 껍질에서 가장 높았으며, 각각 135.13 mg%와 163.67 mg%였다. 또한 두충 추출물의 ACE 저해활성은 10 mg/mL 농도로 처리하였을 때 볶은 잎, 자연건조 껍질 및 볶은 껍질에서 각각 77.56%, 75.73%, 75.73%로 높은 활성을 나타내었으며, 줄기는 상당히 낮게 나타났다. 두충에서 분리한 PDG를 1 mg/mL 처리할 때, ACE 저해활성은 91.87%로서 $Enalapril^{(R)}$의 97.06%보다는 조금 낮았지만, $Captopril^{(R)}$의 90.32% 보다는 약간 높은 항고혈압 활성을 나타내었다.

• Asian-Australasian Journal of Animal Sciences
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• 제16권9호
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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 Microbiology and Biotechnology
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• 제14권6호
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• pp.1318-1323
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• 2004

This study describes the purification and characterization of a novel antihypertensive angiotensin 1­converting enzyme (ACE) inhibitory peptide from Saccharomyces cerevisiae. Maximal production of the ACE inhibitor from Saccharomyces cerevisiae was obtained from 24 h of cultivation at $30^{\circ}C$ and its ACE inhibitory activity was increased by about 1.5 times after treatment of the cell-free extract with pepsin. After the purification of ACE inhibitory peptides with ultrafiltration, Sephadex G-25 column chromatography, and reverse-phase HPLC, an active fraction with an $IC_{50}$ of 0.07 mg and $3.5\%$ yield was obtained. The purified peptide was a novel decapeptide, showing very low similarity to other ACE inhibitory peptide sequences, and its amino acid sequence was Tyr-Asp-Gly-Gly-Val-Phe-Arg-Val-Tyr-Thr. The purified inhibitor competitively inhibited ACE and also showed a clear antihypertensive effect in spontaneously hypertensive rats (SHR) at a dosage of 1 mg/kg body weight.

• Mycobiology
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• 제33권3호
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• pp.142-146
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• 2005

To produce a novel antihypertensive angiotensin I-converting enzyme (ACE) inhibitor from yeast, a yeast isolate, designated G-14 showing the highest ACE inhibitory activity was obtained and identified as Malassezia pachydermatis based on morphological, biochemical and cultural characteristics. The maximal extracellular ACE inhibitor production was obtained from M. pachydermatis G-14 when the strain was cultured in YEPD medium containing 0.5% yeast extract, 3.0% peptone and 2.0% glucose at $30^{\circ}C$ for 24 h and the final ACE inhibitory activity was 48.9% under the above condition.

• Mycobiology
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• 제38권3호
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• pp.206-209
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• 2010

To produce bioactive compound enriched yeast using medicinal Gugiga (Lycium chinensis Mill), several edible Saccharomyces species were cultured in Gugija extracts added yeast extract, peptone and dextrose medium (GE - YEPD medium) at $30^{\circ}C$ for 24 hr, and their growth were determined. Growth of Saccharomyces cerevisiae K-7 and Sacchromyces cerevisiae ACTC 7904 were better than those of the other yeasts. Two yeasts were selected and then determined their some physiological functionalities after cultivated the yeasts in the GE - YEPD medium and compared those grown on YEPD medium. Antihypertensive angiotensin I-converting enzyme (ACE) inhibitory activity of S. cerevisiae K-7 grown on GE - YEPD medium was about 20% higher than that grown on YEPD medium. Superoxide dismutase-like activity of S. cerevisiae ACTC 7904 was also about 12% more high. However, the other physiological functionalities were almost same or lower. Optimal addition concentration of Gugija extract was 10%, and maximally growth and ACE inhibitory activity of S. cerevisiae K-7 were shown when the strain was cultured in 10% Gugija extracts containing YEPD medium at $30^{\circ}C$ for 12 hr.

• 한국식품영양과학회지
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• 제37권2호
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• pp.136-140
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• 2008

번데기 단백질의 최적 가수분해 조건을 선정하기 위해 4종의 가수분해 효소를 이용하여 번데기분말 첨가량별 및 가수분해시간에 따른 단백질 용해지수, 각각의 가수분해물의 ACE 저해활성 및 항산화활성 등을 조사하였다. 탈지번데기 분말의 최적 분산농도는 $5{\sim}10%$ 범위였으며 가수분해시간은 18시간이었고, ACE 저해활성은 neutrase, trypsin, pepsin 및 alcalase 효소처리 시 각각, 85.16, 83.46, 70.45 및 65.39%로 모든 효소 처리구가 비효소 처리구(24.94%)에 비해 높은 활성을 나타내었다. 가수분해물의 항산화활성($IC_{50}$)은 상업용 효소인 neutrase와 alcalase의 경우 각각 352.75 및 $396.09\;{\mu}g/mL$로 비효소처리구($327.24\;{\mu}g/mL$)와 유사한 값을 보였고, pepsin 및 trypsin은 각각 626.09 및 $677.44\;{\mu}g/mL$로 비효소처리구보다 낮게 나타났다.