• Journal of Animal Science and Technology
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• 제49권1호
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• pp.129-136
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• 2007

본 실험은 한우 육단백질의 가수분해물로부터 항고혈압 활성을 측정하기 위하여 실시한 것으로서 한우 등심과 우둔으로부터 추출한 myosin B를 pepsin으로 가수분해하여 가수분해물들의 전기영동 결과, 가열처리와 가수분해 시간의 증가에 따라 단백질의 소실이 증가하였다. 항 고혈압 활성을 측정한 결과 10 ug/ml의 희석된 가수분해물의 ACE 억제효과는 1시간 이상 가수분해 시키면 약 40%의 억제율을 가졌다. 가수분해물 원액으로 ACE 억제효과를 살펴본 결과에서는 등심이 우둔보다 높았으며 (p<0.05), 비가열 가수분해물이 가열한 가수분해물 보다 억제율이 높게 나타났다 (p<0.05). 또한, 가수분해 시간별 처리구에서는 1시간 이상 가수분해 시키면 약 70% 이상의 억제율을 갖는 것으로 나타나 한우의 myosin B를 1시간 이상 가수분해하면 ACE 억제율이 증진되는 것으로 사료된다.

• 한국식품영양학회지
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• 제18권1호
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• pp.11-18
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• 2005

Angiotensin Ⅰ converting enzyme(ACE) inhibitory activities of laver(Porphyra tenera) protein hydrolysates were investigated by enzymes used for hydrolysis, molecular fractions and drying methods. For the enzymatic hydrolysis, crude laver protein, separated by filtration of water extract of dried laver extracted with 20 times(w/v) water for 3 hours at boiling temperature, were hydrolyzed with three commercial protease, Pepsin, alcalase and maxazyme NNP at optimal conditions. The yield of hydrolysis and ACE inhibitory activities of which were high in order of pepsin, alcalase and maxazyme NNP. ACE inhibitory activities of laver hydrolysates by molecular levels were high in order of 3 kDa > 10 kDa > 3∼10 kDa, and the IC/sub 50/ ACE inhibitory activities by molecular lebels were 4 mg/mL(3 kDa), 5 mg/mL(total hydrolysate), and 20 mg/mL(10 kDa), respectively. The storage stability of dried laver hydrolysates at 20℃ were strongly affected by drying methods, hot air dried of which were much stabler than freeze-dried one.

• ALGAE
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• 제21권3호
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• pp.343-348
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• 2006

This study was conducted to screen in vitro angiotensin - I converting enzyme (ACE) inhibitory activities of methanol (MeOH) and aqueous extracts at 20°C and 70°C, respectively, prepared from twenty-six red algae obtained from the coast of Jeju Island in Korea. Among aqueous extracts at 20°C (20AE) from red algae Lomentaria catenata showed the strongest ACE inhibitory activity and Lithophyllum okamurae recorded the second highest activity. From MeOH extract at 20°C (20ME) Ahnfeltiopsis flabelliformis possessed the strongest ACE inhibitory activity. Remarkable activities from MeOH extracts at 70°C (70ME) were observed in Grateloupia filicina, Sinkoraena lancifolia and Grateloupia lanceolata. However, no significant activity was found in aqueous extracts at 70°C (70AE). The IC50 values, which are concentrations required to inhibit 50% activity of ACE, for ACE inhibitory activities of 20AE from Lithophyllum okamurae and L. catenata were 13.78 and 12.21 μg mL–1, respectively. The IC50 values of 20ME from A. flabelliformis and Laurencia okamurae were 13.84 and 106.15 μg mL–1. Those of the 70ME from Bonnemaisonia hamifera, Grateloupia filicina, Sinkoraena lancifolia, G. lanceolata, Gracilaria vermiculophylla and L. okamurae ranged from 25.82 to 124.69 μg mL–1.

• Food Science and Biotechnology
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• 제17권4호
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• pp.873-877
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• 2008

Native soy protein isolate (SPI) was hydrolyzed with 4 different proteolytic enzymes, including bromelain, papain, Neutrase, and Flavourzyme. SPI hydrolysates with the degree of hydrolysis (DH) in range of 6 to 15% were prepared by each enzyme. The angiotensin 1 converting enzyme (ACE) inhibitory and the antioxidant activities of the SPI hydrolysates, such as superoxide dismutase-like activity and inhibition of the linoleic acid autoxidation, were evaluated. Overall, as the DH increased, all evaluated bioactivities of the SPI hydrolysates significantly increased. The significantly highest ACE inhibitory and antioxidant activities were found in hydrolysates made with papain and bromelain, respectively. SPI hydrolysates by Flavourzyme showed the significantly lowest activity in all tested bioactivities. The results suggested that ACE inhibitory and antioxidant activities of SPI hydrolysates were determined by the DH and by the enzyme used.

• 한국식품영양과학회지
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• 제44권10호
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• pp.1538-1542
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• 2015

장류 발효기술과 유용 천연물을 활용한 프리미엄 발효소스의 개발을 목적으로 소맥분과 콩의 발효물(페이스트 형태), 미더덕 껍질, 뽕잎, 양파 추출물을 단독 또는 혼합하여 첨가한 발효소스를 제조한 후, ACE 저해능과 DPPH 라디칼 소거능을 측정하였다. 그 결과 무첨가 대조구에 비하여 추출물 첨가 발효소스의 ACE 저해능과 라디칼 소거능은 증가하였다. 특히 뽕잎과 양파 추출물을 혼합하여 첨가한 발효소스가 대조구에 비하여 상대적으로 ACE 저해능이 26.92% 증가하였고, DPPH 라디칼 소거능은 40.66% 증가하였다. 이러한 결과는 항고혈압능과 항산화능을 보유한 고품질 소스의 제조에 소맥분과 콩의 발효물, 뽕잎과 양파 추출물 등이 활용될 수 있음을 시사한다.

• Fisheries and Aquatic Sciences
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• 제19권7호
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• pp.29.1-29.6
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• 2016

In the present study, we investigated to the antioxidant and angiotensin I-converting enzyme (ACE) inhibitory activities of the northern shrimp (Pandalus borealis) by-products (PBB) hydrolysates prepared by enzymatic hydrolysis. The antioxidant and ACE inhibitory activities of five enzymatic hydrolysates (alcalase, protamex, flavourzyme, papain, and trypsin) of PBB were evaluated by the 2, 2'-azino-bis [3-ethylbenzothiazoline-6-sulfonic acid] ($ABTS^+$) radical scavenging and superoxide dismutase (SOD)-like activities, reducing power and Li's method for ACE inhibitory activity. Of these PBB hydrolysates, the protamex hydrolysate exhibited the most potent ACE inhibitory activity with $IC_{50}$ value of $0.08{\pm}0.00mg/mL$. The PBB protamex hydrolysate was fractionated by two ultrafiltration membranes with 3 and 10 kDa (below 3 kDa, between 3 and 10 kDa, and above 10 kDa). These three fractions were evaluated for the total amino acids composition, antioxidant, and ACE inhibitory activities. Among these fractions, the < 3 kDa and 3-10 kDa fractions showed more potent $ABTS^+$ radical scavenging activity than that of > 10 kDa fraction, while the > 10 kDa fraction exhibited the significant reducing power than others. In addition, 3-10 kDa and > 10 kDa fractions showed the significant ACE inhibitory activity. These results suggested that the high molecular weight enzymatic hydrolysate derived from PBB could be used for control oxidative stress and prevent hypertension.

• Asian-Australasian Journal of Animal Sciences
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• 제16권3호
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• pp.417-424
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• 2003

Inhibitory activities against angiotensin I-converting enzyme (ACE) of enzymatic hydrolysates of porcine skeletal muscle proteins were investigated. Myosin B, myosin, actin, tropomyosin, troponin and water-soluble proteins extracted from pork loin were digested by eight kinds of proteases, including pepsin, $\alpha$-chymotrypsin, and trypsin. After digestion, hydrolysates produced from all proteins showed ACE inhibitory activities, and the peptic hydrolysate showed the strongest activity. In the case of myosin B, the molar concentration of peptic hydrolysate required to inhibit 50% of the activity increased gradually as digestion proceeded. The hydrolysates produced by sequential digestion with pepsin and $\alpha$-chymotrypsin, pepsin and trypsin or pepsin and pancreatin showed weaker activities than those by pepsin alone, suggesting that ACE inhibitory peptides from peptic digestion might lose their active sequences after digestion by the second protease. However, the hydrolysates produced by sequential digestion showed stronger activities than those by $\alpha$-chymotrypsin, trypsin or pancreatin alone. These results suggested that the hydrolysates of porcine meat were able to show ACE inhibitory activity, even if they were digested in vivo, and that pork might be a useful source of physiologically functional factors.

• Mycobiology
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• 제39권1호
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• pp.67-69
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• 2011

A cell-free extract of Saccharomyces cerevisiae containing the angiotensin I-converting enzyme (ACE) inhibitory peptide was treated in a successive simulated gastric-intestinal bioreactor (step 1: amylase digestion, step 2: gastric fluid digestion, step 3: intestinal fluid digestion) to illustrate the absorption pattern of antihypertensive ACE inhibitory peptide, and the ACE inhibitory activities of each step were determined. Total ACE inhibitory activities of step 1, step 2, and step 3 were 55.96%, 80.09%, and 76.77%, respectively. The peptide sequence of each steps was analyzed by MS/MS spectrophotometry. Eleven kinds of representative peptide sequences were conserved in each step, and representative new peptides including RLPTESVPEPK were identified in step 3.

• Fisheries and Aquatic Sciences
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• 제16권4호
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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.

• 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.