• Food Science of Animal Resources
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• v.22 no.1
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• pp.87-93
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• 2002

Angiotensiri-I converting enzyme(ACE) catalyst the removal of the C-terminal dipeptide from the angiotensin-I to give the angiotensin-II, a potent peptide that causes constriction of regulation of blood pressure. Recently, ACE inhibitor peptides have been isolated from enzymatic digests of food protein. The aim of this study was to identify bovine casein hydrolysates with ACE inhibitory properties in different enzymatic hydrolysis conditions. The casein were hydrolyzed neutrase, alcalase, protamax, flavourzyme, premed 192, sumizyme MP, sumizyme LP and pescalase alone and with an enzyme combination. Premed 192 produced ACE inhibitory peptides most efficiently. In order to ACE inhibitory peptide produced enzymatic hydrolysis condition were premed 192 added to casein ratio of 1:100(w/w), and incubated at 47$\^{C}$ for 12hrs. Casein hydrolysate gave 50% inhibition(IC$\_$50/ value) of ACE activity at concentration with 248ug/ml(general method) and 265ug/ml(pretreatment method) respectively.

• 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).

• Journal of the Korean Society of Food Science and Nutrition
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• v.30 no.4
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• pp.594-599
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• 2001

This study was attempted to isolate and identify the strain revealing high angiotensin converting enzyme (ACE) inhibitory activity from various soy fermented foods, i.e. meju, soybean paste and soy sauce. Forty-two strains with morphologically different characteristics were selected and the ACE inhibitory and proteolytic activities were examined. Of the strains tested, SS103 which was isolated from soy sauce showed the highest ACE inhibitory and proteolytic activities and was finally selected for further studies. The SS103 strain showed motility, rod form and ellipsoidal spores. The shape of colonies on the agar media was irregular, mucoidal and surface dull. The strain could grow under aerobic conditions of pH 5~9 and 10~$50^{\circ}C$. Main cellular fatty acid was $C_{15:0}$ anteiso, $C_{17:0}$ cis and $C_{17:0}$ iso, which was 33.9%, 18.8% and 16.5%, respectively. Based upon these morphological, biochemical and cultural properties, SS103 was identified as a Bacillus subtilis. Optimum cultural condition of Bacillus subtilis SS103 was pH 8.0, $37^{\circ}C$ and 48 hr.48 hr.

• Food Science of Animal Resources
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• v.31 no.6
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• pp.886-892
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• 2011

This study investigated the ACE-inhibitory effect of yogurt beverage fortified with hydrolysates as well as the suitability of hydrolysates as a nutraceutical additive to yogurt beverage. Three whey protein hydrolysates hydrolyzed by alcalase, protamex, and trypsin were each added to yogurt beverage at concentrations of 1.25, 2.5, and 5 mg/mL. Yogurt beverage fortified with 2.5 mg/mL of hydrolysates had 61-69% ACE-inhibitory activity, whereas yogurt beverage fortified with 5 mg/mL of hydrolysates showed 74% ACE-inhibitory activity. There were no significant differences in ACE-inhibitory activity between the alcalase or protamex hydrolysates during storage; however, trypsin hydrolysate exhibited significant differences. On the other hand, physicochemical characteristics such as pH (3.47-3.77), titratable acidity (0.81-0.84%), colority, viable cell count, and sensory qualities were not significantly different among the tested yogurt beverage samples during storage. These results showed that yogurt beverage fortified with whey protein hydrolysates maintained antihypertensive activity and underwent no unfavorable changes in physicochemical characteristics regardless of enzyme type.

• YAKHAK HOEJI
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• v.45 no.2
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• pp.214-219
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• 2001

Nineteen hydrolysable tannins isolated from the Euphorbia helioscopia (Euphorbiaceae) were tested for the inhibitory effect on mushroom tyrosinase activity in vitro. Inhibitory effect of gallotannin group exhibited more potent than that of phenolcarboxylic acid and ellagitannin groups against the enzyme activity. The inhibitory activity by pentagalloyl glucose on mushroom tyrosinase was more potent ($IC_{50}$/, 4.9 $\mu$M) than that of kojic acid ($IC_{50}$/, 8.7 $\mu$M).

• KSBB Journal
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• v.14 no.5
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• pp.600-605
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• 1999

For the production of angiotensin I converting enzyme inhibitory peptides as a material for antihypertensive functional foods from animal blood produced in slaughterhouse, the optimum condition for enzymatic hydrolysis to yield a peptide fraction of the highest activity were investigated with a respect of industrial production. Among several industrially-usable enzymes tested, $Alcalase^？$ produced hydrolysates of the highest activity from total plasma and purified albumin. $IC_50$ values of albumin hydrolysate and its third fraction separated by gel chromatography were 0.5 and 0.02 mg/mL, respectively. The fraction was found to be obtained by a simple ultrafiltration using a membrane of MW cutoff 1,000. The possibility for the industrial production of antihypertensive peptides from animal blood plasma protein was suggested.

• Journal of Animal Science and Technology
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• v.47 no.1
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• pp.83-90
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• 2005

ACE-inhibitory peptides derived from goat's whey hydrolyzed by various proteolytic enzymes were separated and purified for antihypertension materials. The highest ACE-inhibitory activity of goat's whey hydrolysates was 85.5 % by pepsin for 72 hrs. Also the highest ACE-inhibitory activity of goat's whey hydrolysates was F-4 by pepsin for 72 hrs by Sephadex G-25 gel chromatograms. F-4e and F-4ed from F-4 by RP-HPLC to first and second purification were the highest in ACE-inhibitory activity, respectively. The most abundant amino acid was leucine(I 8.54 %) in F-4ed of ACE-inhibitory peptides after second purification. Amino acid sequence of F-4ed of ACE-inhibitory peptides showed Leu-Lys-Asp-Tyr-Gly-GlyVal- Ser-Leu and Leu-Gly-Asp-Gly-Ala-Gly- Asp-Val-Ala-Phe. $IC_{50}$ calibrated in peptic hydrolysates(72 hrs), F-4, F-4e and F-4ed from goat's whey hydrolysates by pepsin for 72 hrs were 33.93, 28.75, 11.74 and 1.09 mg/ml, respectively. From the results of this experiment, goat's whey hydrolysate by pepsin was shown to have ACE-inhibitory activity.

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

• Journal of Periodontal and Implant Science
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• v.24 no.1
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• pp.144-154
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• 1994

Final goal of periodontal treatment is to reconstruct the destructed periodontal tissue as well as to remove the necrotic pathologic elements. The purpose of this study is to investigate on the effect of Zizyphi extract to the inhibitory ability on collagenolytic activity of P gingivalis, biologic activity of gingival fibroblasts, and on the collagen and protein synthesis of gingival fibroblasts. Gingival fibroblast from giniva of first bicuspids from patient for orthodontic treatment were used and cultured. For the measurement of inhibitory ability of collagenolytic activity, crude enzyme was extracted and used on the basis of modified Ono's method. On the inhibition of collagenolytic enzyme from herbal extracts, collagenokit CLN-100 were used. The cellular activity of gingival fibroblast, were studied using MTT solution and measured optical density on 570mm by ELISA reader. To measure the effects on the ability of whole protein and collagen synthesis, cell membrane was destructed with ultrasonic grinder after culturing, centrifuged and counted by liquid scintilation counter. The inhibitory effects on producing of $IL-l{\beta}$ by monocyte, after promotion of producing $IL-l{\beta}$ by LPS, were compared with the mixture of herbal extracts and other drugs using thymocyte stimulation assay. About inhibitory effects of $PGF_2$. by gingival fibroblasts, herbal extract was compared with the addition of the other control groups using enzyme imunoassay. On the inhibition of collagenolytic activity by P. gingivalis, benzene extracts showed the most efficient inhibitory effects among the $19{\mu}g/ml$ of the compared extracts and 40.5% by Tetracycline. On the cellular activity promoting effects, compared extracts showed a bit of more effects than PDGF of $100{\mu}g/ml$ concentration and IGF of $20{\mu}g/ml$ concentration. All of the PDGF, IGF, Zizyphi Fructus extract should increase in collagen synthesis, but especially 70% ethylalcohol extracts of Zizyphi Fructus showed comparably high effects among the compared extracts. Effects on whole protein synthesis were slightly increased on every extract but especially 70% ethylalcohol extract showed significantly effective than any other estract. On the inhibitory effects of Zizyphi Fructus $IL-l{\beta}$ production by monocyte, compared extracts showed 70% of highly inhibitory effect than that of 60% inhibition effects on controlled group and each extracts showed no significant difference. In $PGF_2$ production inhibitroy effect of Zizyphi Fructus gingival fibroblasts, Herbal extracts showed 70% of inhibition comparing with tat of 90.2% of controlled group, but each extracts showed similar effects excluding the $H_2O$ extracts. These results suggested that Zizyphi Fructus might be useful medicine for inhibition of inflammatory mediator including $IL-l{\beta}$ and $PGF_2$.

• 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.