• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.35 no.5
• /
• pp.529-533
• /
• 2002

The peptides inhibiting angiotensin converting enzyme (ACE) were isolated from the hydrolysate of manila clam (Ruditapes philippinamm) proteins prepared with thermolysin. The thermolysin hydrolysate was pretreated with membrane filter (MW cut-off 10,000) to obtain the peptide fraction with ACE inhibition. The crude peptides were applied to a Sephadex LH-20 column and eluted with $30\%$ methanol. The three active fractions (A, B and C) were collected and concentrated, and then applied to a SP-Toyopearl 650S column equilibrated with distilled water and was eluted with a linear gradient of NaCl concentration (0 to 1 M). The four active fractions (A-1, A-2, B-1 and C-1) were collected and concentrated, and then applied to a SuperQ-Toyopearl 650S column equilibrated with distilled water and was eluted with a linear gradient of NaCl concentration (0 to 1 M). The maximum inhibitory activity was observed in the fraction B-1Q showed the IC_{50} values of 0.748 $\mu$g. The abundant amino acids obtained from active fraction B-1Q were leucine, isoleucine, alanine and threonine.

• Korean Journal of Microbiology
• /
• v.46 no.1
• /
• pp.9-14
• /
• 2010

In this study, lactic acid bacteria with high angiotensin converting enzyme inhibitor activity were isolated from Korean fermented food, such as kimchi and salted seafood. The strain HLJ59, isolated from salted shrimp showed the highest angiotensin converting enzyme inhibitor activity in DeMan Rogosa Sharpe broth. Optimum growth temperature of Lactobacillus brevis HLJ59 was at $34^{\circ}C$. Acid treatment at pH 3.0 for 1.5 h decreased cell viability from $9.9{\times}10^8$ CFU/ml to $3.11{\times}10^4$ CFU/ml. The bile extract concentration of 0.3%, 0.5%, and 1.0% in MRS broth did not inhibit the growth of HLJ59. Isolated strain HLJ59 showed more sensibility to amikacin, gentamycin, neomycin, streptomycin, kanamycin, cefmetazole, cephalothin, ampicillin, ticarcillin, sulbactam+ampicillin, amoxicillin+clavulanic acid (AMC), tetracycline, and sulfamethoxazole+trime thoprim (SXT) as compare to other 7 different antibiotics. However, it showed more resistance to cefoxatin, ceftnaxone, penicillin, ciprofloxacin, nalidixic acid, lincomycin, and chloramphenicol.

• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.26 no.4
• /
• pp.321-329
• /
• 1993

The present study was conducted to elucidate the body modulating function of fermented seafood products. Angiotensin converting enzyme (ACE) acts in blood pressure regulation, converting angiotensin I to the potent vasoconstrictor angiotensin II and inactivating the vasodilator bradykinin to raise blood pressure. Salted and fermented anchovy which is one of the traditional fermented seafood in Korea was tested for inhibitory activity against ACE. ACE inhibitory activity of salted anchovy during the period of fermentation was increased with the elapse of fermentation days until fermentation of 60 days, but thereafter decreased inversely. When the fermented product was extracted with $50\%$ ethanol, the ACE inhibitory activity was the highest. And the ACE inhibitory activity was proportion to the content of $50\%$ ethanol soluble peptide-nitrogen of the fermented product. From the profiles of gel permeation chromatography on a Bio-Gel P-2 of $50\%$ ethanol soluble fraction obtained from salted and fermented anchovy fermented for 60 days at an ambient temperature, the higher activity fractions were C'($IC_{50}=97{\mu}g\;protein/ml$) and D'($IC_{50}=65{\mu}g\;protein/ml$). Amino acid analysis showed that the large quantify of threonine, glutamic acid, lysine for C' and serine, proline for D', respectively.

• Food Science of Animal Resources
• /
• v.31 no.5
• /
• pp.663-667
• /
• 2011

This study was performed to measure the angiotensin I-converting enzyme (ACE) inhibitory activity of peptide extracts derived from the enzymatic proteolysis of Hanwoo Musculus longissimus (M. longissimus) during cold storage. Thermolysin (80 ppm, w/w) and protease type XIII (100 ppm, w/w) were injected separately or in combination for the enzymatic proteolysis of sarcoplasmic and myofibrillar proteins prior to storage at $5^{\circ}C$ (T1) or at $-1^{\circ}C$ (T2) in a chilling room for 9 days. Beef injected with thermolysin (E2) and thermolysin+protease type XIII (E3) showed a significantly higher degree of hydrolysis at both storage temperatures (p<0.05). During the storage period, T1E2 at day 6 and T1E3 at day 9 showed the strongest ACE inhibitory activity with sarcoplasmic and myofibrillar protein proteolysates. Macromolecules greater than 10,000 Da were removed by ultra filtration, and the filtrates were separated into fractions using gel filtration. Five and three major fractions were collected from S-T1E2-6 and M-T1E3-9 extracts, respectively, and the $4^{th}$ fraction of the S-T1E2-6 extracts showed the highest ACE inhibitory rate of $61.96{\pm}7.41%$.

• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.34 no.2
• /
• pp.164-172
• /
• 2001

The angiotensin-I converting enzyme (ACE) inhibitors from laver hydrolysate was isolated. Among the 13 kinds of proteases, Maxazyme NNP was most effective for preparing the high ACE inhibitory compound. In extraction conditions of ACE inhibitory peptide from laver hydrolysate, ACE inhibitory activity of hydrolysate treated with diethylether for decolorization and that of $70\%$ ethanol soluble fraction among the different ethanol concentrations were higher than other preparations. Low molecular fraction less than 3,000 dalton of layer hydrolysate separated by ultrafiltration had the highest ACE inhibitory activity, for further separation of ACE inhibitory peptide from laver hydrolysate, gel filtration chromatography (Sephadex G-25), reverse-phase HPLC (ODS & Vydac C-18) and gel permeation chromatography (Superdex Peptide HR) were performed. The molecular mass of the ACE inhibitory peptide fractions of gel permeation chromatography determined by electrospray-mass spectrometer were 413.48 (S1O2V2V1P),346.86 (S1O2V2V2P) and 320.32 (S2O6V3V1P) dalton and their amino acid sequence were Val-Gln-Gly-Asn, Thr-Glu-Thr and Phe-Arg, respectively.

• Korean Journal of Food Science and Technology
• /
• v.25 no.5
• /
• pp.456-460
• /
• 1993

The present study was conducted to investigate Angiotensin I-converting enzyme(ACE) inhibition activity of the components of traditional tea materials in Korea. Angiotensin I-converting enzyme(ACE) inhibition activity of water soluble fractions obtained from the samples were strong in Zingiberis rhizoma, Acantopanacis cortex, Schizandrae fructus, Perilla semen, Cassiae torae semen, Zizyphy fructus in order. ACE inhibition activity of fractions obtained from methanol extract of Cassiae torae semen were strong in ethyl acetate fraction, ethyl ether fraction, water fraction, chloroform fraction in order. Compound C showed the strongest ACE inhibition activity among compound A, B, C, D separated from Cassiae torae semen, but Compound C separated from Cassiae torae semen was lower than bradykinin in the ACE inhibition activity.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.39 no.1
• /
• pp.8-13
• /
• 2010

The angiotensin converting enzyme (ACE) inhibition effect of soybean protein isolate hydrolysate was studied using protease. Soybean protein isolate was hydrolysed by seven enzymes (Alcalase 2.4 L, Flavourzyme 500 MG, GC 106, Multifect Neutral, Neutrase 0.8 L, Papain 30,000 and Protamex), enzyme concentrations (0, 0.5, 1.0 and 1.5%), at various hydrolysis times (0, 1, 2, 3, 4, 5 and 6 hr) and suspension concentrations (1, 5, 7, 10 and 15%). Absorbance at 280 nm, brix and ACE inhibitory activity of soybean protein isolate hydrolysates were investigated. Absorbance at 280 nm and brix of Alcalase 2.4 L treatment were higher than other enzyme treatments. The optimum condition of hydrolysis was Alcalase 2.4 L, 1% enzyme concentration, 5% suspension concentration for 4 hr. $IC_{50}$ value of ACE inhibitory activity of soybean protein isolate hydrolysate was $79.94 {\mu}g/mL$. These results suggest that soybean isolate protein hydrolysate from Alcalase 2.4 L may be of benefit for developing antihypertensive therapeutics.

• Journal of Dairy Science and Biotechnology
• /
• v.32 no.1
• /
• pp.7-16
• /
• 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 the Korean Society of Food Science and Nutrition
• /
• v.29 no.3
• /
• pp.395-400
• /
• 2000

양파 조미액으로부터 ACE 저해활성 물질을 분리하기 위해 hexane, ethylether, ethylacetate, butanol과 물로 분획시, 4.8g의 당 함량과 31.9 mg의 phenol성 물질을 함유한 butanol 분획이 82.1%의 ACE 저해활성을 나타내었고, 70.3%의 ACE 저해활성을 보인 양퍄 조미액보다 높은 저해활성을 보였다. Butanol 분획을 Amberite XAD-2column으로 분리한 결과, ACE 저해활성을 보이는 미흡착 분획(F1)를 얻었다. 활성분획 F1을 Sephadex LH-20column으로 분획한 결과, 4개(F1-1,F1-2,F1-3,F1-4)의 분획을 얻었으며, 이중 F1-3 분획의 ACE 저해활성은 93%로 가장 높은 저해활성을 보였다. Sephadex LH-20 column chromatography에 의해 얻어진 활성분획F1-3을 Supercosil LC-18 column을 이용하여 분리한 결과, 6분대에서 ACE 저해활성을 가지는 단일 peak(F1-3a)를 얻었다. 각 정제 과정에서 얻은 분획들은 전형적인 flavonoid의 band I과 bandII의 피크를 보였다. 또한 ACE에 대한 저해기작은 flavonoid 물질이 보이는 전형적인 비경쟁적 저해양상을 보였다.

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