• Korean Journal of Fisheries and Aquatic Sciences
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• v.31 no.6
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• pp.875-881
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• 1998

To develop functional food material with angiotensin converting enzyme (ACE) inhibitory peptides, muscle protein of anchovy, Engraulis japonica was hydrolyzed during 48 hrs by digestive pretenses such as pepsin, trypsin, $\alpha$-chymotrypsin, and commercial proteases such as papain, bromelain, complex enzyme, Elavourzyme, Novozym, Neutrase, Protamex and Alcalase. The only $50\%$ ethanol soluble hydrolysates were tested for inhibitory activity against ACE and yield of $50\%$ ethanol soluble peptide-nitrogen ($ESPN_{50}$). ACE inhibition effects and yield of $ESPN_{50}$ occurred as hydrolysis time increased to 8 hrs, Among those pretenses tested, hydrolysates by Alcalase and $\alpha$-chymohypsin had greater ACE inhibitory activity (80 and $74\%$, reipectively) with eletated levels of $ESPN_{50}$ (48 and 58 mg/ml, respectively), while Protamex hydrolysates had greater ACE inhibitory activities ($73\%$) with reduced levels of $ESPN_{50}$ (7.2mg/ml) than others. Amino acid compositions of $50\%$ ethanol solubles obtained from those hydrolysates were rich in glutamic acid, aspartic acid, cysteine and leucine.

• Journal of Microbiology and Biotechnology
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• v.16 no.5
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• pp.757-763
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• 2006

Angiotensin I-converting enzyme (ACE) inhibitors have generally been very useful to remedy or prevent hypertension. This study describes the extraction and characterization of an ACE inhibitor from the fruiting body of Pholiota adiposa ASI 24012, which can be used as an antihypertensive drug. The maximal ACE inhibitory activity $(IC_{50};0.25mg)$ was obtained when the fruiting body of Pholiota adiposa ASI 24012 was extracted with distilled water at $30^{\circ}C$ for 12 h. After the purification of ACE inhibitor with ultrafiltration, Sephadex G-25 column chromatography, and reverse-phase HPLC, an active fraction with an $IC_{50}$ of 0.044 mg was obtained. The purified ACE inhibitory peptide was a novel pentapeptide, showing very little similarity to other ACE inhibitory peptide sequences. The molecular mass of the purified ACE inhibitor was estimated to be 414 daltons with a sequence of Gly-Glu-Gly-Gly-Pro, and showed a clear antihypertensive effect on spontaneously hypertensive rats (SHR) at a dosage of 1 mg/kg.

• Journal of the Korean Society of Food Science and Nutrition
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• v.41 no.9
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• pp.1191-1196
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• 2012

The purpose of this study was to investigate the tyrosinase, xanthine oxidase, angiotensin converting enzyme (ACE) inhibitory effects, and nitrite scavenging abilities of Jubak (alcohol filter cake, AFC) hot water and ethanol extracts. Tyrosinase inhibitory effects of Jubak hot water and ethanol extracts were above 85%. Nitrite scavenging ability was higher at pH 1.2 than at pH 4.2 and 6.0. Nitrite scavenging abilities of water and ethanol extracts were above 90% at pH 1.2. Xanthine oxidase inhibitory effect of Jubak hot water and ethanol extracts showed a lower, and the effect did not different by hot water and ethanol. ACE inhibitory effects of Jubak hot water and ethanol extracts were approximately 43~53% and 36~47%, respectively. Overall, our results indicate that Jubak hot water and ethanol extracts may have tyrosinase and ACE inhibitory effects and nitrite scavenging ability, but no xanthine oxidase inhibitory effect. Therefore, Jubak has potential as a cosmetic raw material. Additionally, Jubak could be used as a food additive.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.42 no.5
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• pp.426-433
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• 2009

Fish scales have potential in functional food preparation due to their antioxidant and antihypertensive properties. We investigated the angiotensin I converting enzyme (ACE) inhibitory activity of Tilapia mossambica scale extracts. Hydrolysates of tilapia scales were prepared by enzymatic extraction using five proteases (${\alpha}$-chymotrypsin, Alcalase, Kojizyme, Protamex and trypsin) after scales were treated with hot water for 3 hr. Scale enzymatic hydrolysates prepared using both hot water and enzyme treatments exhibited elevated hydrolysis (about 25%-55%) compared to only enzyme treatment (about 15%-45%). Enzymatic hydrolysates (1 mg/mL) prepared by both hot water and enzyme treatments also showed significantly increased ACE inhibitory activities from about 20%-75%. The pattern of ACE inhibitory activities was similar to the degree of hydrolysis. Alcalase and ${\alpha}$-chymotrypsin hydrolysates displayed the highest ACE inhibitory activities ($IC_{50}$ = 0.83 mg/mL and 0.68 mg/mL, respectively). In addition, the ACE inhibitory effects of $IC_{50}$-chymotrypsin hydrolysates increased with decreasing molecular weight (5 kDa>, 10 kDa> and 30 kDa>), with the 5 kDa> fraction displaying the highest ACE inhibitory activity (about 89.9% and $IC_{50}$ = 0.1 mg/mL). We suggest that the peptide compounds of enzymatic hydrolysates prepared from tilapia scale enhances ACE inhibitory activity and might be useful as an antihypertensive material.

• Journal of Microbiology and Biotechnology
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• v.12 no.1
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• pp.59-64
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• 2002

An angiotensin I-converting enzyme (EC 3.4.15.1) (ACE), which can convert inactive angiotensin I into angiotensin II, a vasoconstrictor, is one of the key enzymes in controlling hypertension. It is suggested that the inhibition of ACE prevents hypertension, and many inhibitory peptides have already been reported. In the current study, oligonucleotides encoding ACE inhibitory peptides (IY, VKY) were chemically synthesized and designed to be multimerised due to isoschizomer sites (BamHI, BglII). The cloned gene named AP3 was multimerised up to 6 times in pBluescript and expressed in BL2l containing pGEX-KG. The fusion protein (GST-AP3) was easily purified with a high recovery by an affinity resin, yielding 38 mg of synthetic AP3 from a 1-1 culture. The digestion of AP3 by chymotrypsin exhibited an $IC_50$ value of $18.53{\mu}M$. In conclusion, the present experiment indicated that AP3 could be used as a dietary antihypertensive drug, since the potent ACE inhibitory activity of AP3 could be activated by chymotrypsin in human intestine.

• Journal of Microbiology and Biotechnology
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• v.22 no.3
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• pp.339-342
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• 2012

This study describes the characterization of a new angiotensin I-converting enzyme (ACE) inhibitory peptide from a Korean traditional rice wine. After purification of the ACE inhibitor peptides with ultrafiltration, Sephadex G-25 column chromatography, and successively $C_{18}$ and SCX solid-phase extraction, reverse-phase HPLC, and size exculsion chromatography, two types of the purified ACE inhibitors with $IC_{50}$ values of 0.34 mg/ml and 1.23 mg/ml were finally obtained. The two purified ACE inhibitors (F-1 and F-2) were found to have two kinds of novel oligopeptides, showing very little similarity to other ACE inhibitory peptide sequences. The amino acid sequences of the two purified oligopeptides were found to be Gln-Phe-Tyr-Ala-Val (F-1) and Ala-Gly-Pro-Val-Leu-Leu (F-2), and their molecular masses were estimated to be 468.7 Da (F-1) and 357.7 Da (F-2), respectively. They all showed a clear antihypertensive effect on spontaneously hypertensive rats at a dosage of 500 mg/kg.

• Journal of Dairy Science and Biotechnology
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• v.25 no.1
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• pp.1-7
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• 2007

A Whey-based medium was formulated with Lactobacillus brevis to investigate whether any functional peptides could derive from whey protein. The optimal concentrations of the ingredients of the medium for the growth of Lactobacillus were determined as 2% whey protein concentrate and 1% glucose and 0.5% yeast extracts. The growth of Lb. brevis was improved with the supplementation of yeast extracts than glucose. The viable cells counts of Lb. brevis reached to 2.0 × 10$^8$CFU/mL in the whey-based medium. The whey protein hydrolysates recovered from the supernatant after centrifugation at 10,000 x g for 10min induced strong inhibitory activity against ACE. When the whey protein hydrolysate were partially purified by a membrane tubing below 8,000Da, the partially purified fraction remained 64.7 ${\pm}$ 3.6% of the ACE inhibition activity of the whey protein hydrolysates and IC$_{50}$ was 38.8 ${\pm}$ 2.2mg/mL. The whey-based medium was proved to be effective in producing ACE inhibitory peptides by lactic bacteria fermented whey protein.

• Microbiology and Biotechnology Letters
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• v.31 no.1
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• pp.51-56
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• 2003

The angiotensin I converting enzyme (ACE) has an important role in the maintenance of blood pressure. The ACE inhibitory activities of foods have recently been studied. We tried to isolate ACE inhibitory peptides from the Flavourzyme (FZ), Pescalase (PE), and Thermolysine (TH) protease digests of corn gluten, which was restricted to the use the source of food for digestion problem. The FZ, PE, TH/PE protease hydrolyzed corn gluten and the inhibitory activities of the hydrolyzates for ACE were measured. Major fractions were isolated from the digests using ODS chromatography after treating with ethanol in step gradient. The ACE inhibitors were further purified by Bio-Gel P-2 column and reverse phase HPLC. Five inhibitory peptides were isolated. Their amino acids were sequenced as LPF ($IC_{50}$ = 40$\mu$M), GPP ($IC_{50}$ = 17.6$\mu$M), PNPY ($IC_{50}$ = 30.7$\mu$M), SPPPFYL ($IC_{50}$ = 63 $\mu$M), and SQPP ($IC_{50}$ = 17.2$\mu$M).

• KSBB Journal
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• v.31 no.3
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• pp.165-170
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• 2016

This study was carried out for investigate that physiological activity, quantification and qualitative were sinigrin of Dolsan leaf mustard pickle (DLMP) during storage. sinigrin contains high amounts of nutritional and medicinal compounds, which are important for maintaining optimum health. ACE inhibitory activity was ranged between 43.2 and 79.4%. DLMP methanol extracts demonstrated highest ACE inhibitory activity at 79.4% on day 14, whereas DLMP ethanol extracts demonstrated highest Angiotensin I-converting Enzyme (ACE) inhibitory activity of 43.2% at day 0. The ${\alpha}-glucosidase$ inhibitory activity of positive control 0.02% (v/v) acarbose was 78%. The DLMP methanol extracts had the highest ${\alpha}-glucosidase$ inhibitory activity at 64.0% on day 14, whereas DLMP ethanol extracts had the lowest ${\alpha}-glucosidase$ inhibitory activity of 42.8% at day 28. Sinigrin was high in DLMP methanol extracts at $49.55{\mu}g/ml$ on day 14 of storage. Sinigrin standard was eluted at 2.73 min and MS analysis was m/z 283.03 along with fragment ions at m/z 204 and 149.06. These data show that sinigrin formed desulfo-glucosinolates $[M-SO_3-2H_2O+K+2H]^+$. Sinigrin concentration increased until day 14 and then decreased after that. DLMP methanol extracts had consistently higher sinigrin concentration than DLMP acetonitrile extracts during 28 days of storage.

• Asian-Australasian Journal of Animal Sciences
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• v.16 no.3
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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.