• Korean Journal of Pharmacognosy
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• v.30 no.3
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• pp.269-274
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• 1999

To analyze scientifically the prescription principle of polyprescriptions (Gamchotang, Daewhanggamchotang, Jakyakgamchotang, Gamchogungangtang and Gilkyungtang) containing Glycyrrhizae Radix, the transforming rate of glycyrrhizin in these polyprescriptions to 18 ${\beta}-glycyrrhetinic$ acid and their inhibitory effect on ${\beta}-glucuronidase$, hyaluronidase, phosphodiesterase and trypsin were investigated. When Glycyrrhizae Radix containing polyprescriptions were extracted with water, the contents of glycyrrhizin in water extract of Glycyrrhizae Radix with Rhei Rhizoma or with Zingiberis Rhizoma were higher than that of Glycyrrhizae Radix only, but that in water extract of Glycyrrhizae Radix with Platicodi Radix was lower than that of Glycyrrhizae Radix only. By human intestinal bacteria, glycyrrhizin was metabolized to 18 ${\beta}-glycyrrhetinic$ acid. These metabolism of glycyrrhizin in polyprescriptions containing Glycyrrhizae Radix was inhibited by Rhei Rhizoma, Paeoniae Radix and Platicodi Radix, but was not affected by Zingiberis Rhizoma. The inhibitory activity of Glycyrrhizae Radix on hyaluronidase and ${\beta}-glucuronidase$, was synergistic with Rhei Rhizoma or Zingiberis Rhizoma, but was antagonistic by Platicodi Radix.

• 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 the Korean Society of Food Science and Nutrition
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• v.36 no.7
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• pp.881-888
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• 2007

For the use of skipjack tuna cooking drip (STC) as a source of functional seasoning, the STC was hydrolyzed with various commercial enzymes, such as Alcalase, Flavourzyme, Neutrase and Protamex, and its hydrolysate was also investigated on the food component characteristics. The hydrolysate incubated with Alcalase for 30 min (HA30) showed 56.8% for angiotensin I converting enzyme (ACE) inhibitory activity and 1.18 for antioxidative activity, which were high or similar compared to the other enzymatic hydrolysates. There were no differences in ACE inhibitory activity and antioxidative activity among HA30, two-step enzymatic hydrolysates, and ultrafilterates (molecular weight cut off, 10 kDa). The HA30 was very stable on the digestive enzymes, such as chymotrypsin, pepsin, trypsin according to the TCA (trichloroacetic acid) soluble index. The results suggested that skipjack tuna cooking drip could be used as a source for preparing functional seasoning sauce.

• Journal of the Korean Society of Food Science and Nutrition
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• v.39 no.6
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• pp.783-788
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• 2010

The purpose of this study is to investigate the antioxidative activity and digestive enzyme inhibition of grape seed extract (GSE). The GSE was tested for its effect on various antioxidative potentials (scavenging activities of DPPH radical, superoxide anion radical and hydroxyl radical) and inhibitory effect of various digestive enzymes (trypsin, $\alpha$-chymotrypsin, $\alpha$-amylase, $\beta$-glucosidase and lipase). DPPH radical scavenging activity ($SC_{50}$, 50% scavenging concentration) of GSE was 4.76${\pm}$0.27 ppm while those of positive controls (EGCG and vitamin C) were 2.22${\pm}$0.12 ppm and 9.50${\pm}$0.72 ppm, respectively. $SC_{50}$ value of GSE against superoxide anion radical and hydroxyl radical were 3.82${\pm}$0.07 ppm and 803.23${\pm}$27.16 ppm, respectively. In addition, $IC_{50}$ values of GSE against trypsin, $\alpha$-chymotrypsin, $\alpha$-amylase, $\alpha$-glucosidase and lipase were 2.17${\pm}$0.59 ppm, 7.46${\pm}$1.25 ppm, 18.25${\pm}$3.54 ppm, 12.30${\pm}$1.12 ppm, and 653.23${\pm}$79.34 ppm, respectively. These results suggest that GSE may be useful for the prevention or treatment of obesity.

• Food Science of Animal Resources
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• v.32 no.5
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• pp.652-658
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• 2012

This study was carried out to identify the ACE (Angiotensin converting enzyme) inhibitory activity of casein hydrolysates for development of anti-hypertensive hydrolysates. Sodium caseinate was treated with six kinds of commercial proteases such as Flavourzyme, Protamex, Neutrase 1.5, Alcalase, Protease M, and Protease S for 8 h individually, and was then treated with the enzyme combination for 4 h at $45^{\circ}C$. The hydrolysate which had the highest ACE inhibitory effect was then hydrolysed successively with three digestive enzymes: pepsin, trypsin, and ${\alpha}$-chymotrypsin, at $37^{\circ}C$ for 4 h under conditions mimicking those of the gastrointestinal tract. UF (ultra filtration) treatment was applied to one of the secondary hydrolysates to determine ACE inhibitory activity. When sodium caseinate was hydrolysed by commercial proteases, the degree of hydrolysis (DH) showed 2.54 to 4.25% and after secondary hydrolysis, DH showed 4.30 to 5.22%. ACE inhibitory activity and $IC_{50}$ values decreased, and inhibition rates increased during hydrolysis. Protamex treatment showed the lowest $IC_{50}$ value ($516{\mu}g/mL$) and Flavourzyme hydrolysate showed the highest $IC_{50}$value ($866{\mu}g/mL$). As the first hydrolysate was treated with Flavourzyme, the ACE inhibitory activity increased. Neutrase hydrolysate had the highest activity with an $IC_{50}$ value ($282{\mu}g/mL$). When Neutrase plus Flavourzyme treatment was hydrolyzed by digestive enzymes, the $IC_{50}$ value ($597{\mu}g/mL$) was decreased statistically (p<0.05). As Neutrase plus Flavourzyme hydrolysate is treated by UF with MW cut-off 10,000, permeate showed $273{\mu}g/mL$ of $IC_{50}$ value, showed no difference, but retentate which has over MW 10,000 showed statistically different $IC_{50}$ value, $635{\mu}g/mL$ (p<0.05).

• Fisheries and Aquatic Sciences
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• v.14 no.3
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• pp.174-178
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• 2011

This study aimed to determine the degree of hydrolysis and angiotensin-I-converting enzyme (ACE)-inhibitory activity of Giant Jellyfish Nemopilema nomurai (jellyfish) hydrolysates. The degree of hydrolysis using six proteolytic enzymes (Alcalase, Flavozyme, Neutrase, papain, Protamex, and trypsin) ranged from 13.1-36.8% and the inhibitory activities from 20.46-79.58%. Using papain hydrolysate, we newly isolated and characterized ACE-inhibitory peptides with a molecular weight of 3,000-5,000 Da that originated from jellyfish collagen. The purified peptide (FII-b) was predicted to be produced from an alpha-2 fragment of the type IV collagen of jellyfish. The N-terminal sequence of FII-b was Asp-Pro-Gly-Leu-Glu-Gly-Ala-His-Gly- and showed 87% identity to the collagen type IV alpha-2 fragment of Rattus norvegicus and a predicted protein from Nematostella vectensis, indicating that the ACE-inhibitory peptide originated from the collagen hydrolysate and had an $IC_{50}$ value of 3.8 ${\mu}g$/mL. The primary structure of the fragment is now being studied; this peptide represents an interesting new type of ACE inhibitor and will provide knowledge of the potential applications of jellyfish components as therapies for hypertension.

• Journal of Marine Bioscience and Biotechnology
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• v.7 no.1
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• pp.19-27
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• 2015

The objective of the current study was to evaluate the inhibitory and antioxidant activities of powdered katsuobushi (dried bonito) protein hydrolysates and their corresponding fractions. The powdered katsuobushi (dried bonito) hydrolysates were obtained by enzymatic hydrolysis using Alcalase, ${\alpha}$-chymotrypsin, Neutrase, pepsin, papain, and trypsin. The antioxidant efficacy of the respective hydrolysates were evaluated using 2,2-diphenyl-1-picrylhydrazyl (DPPH), hydroxyl, superoxide, and alkyl radical-scavenging activities. Among the hydrolysates, the peptic-derived hydrolysate exhibited the highest antioxidant activity compared to other enzymatic hydrolysates. Therefore, the peptic-derived hydrolysate was further analyzed, and was found to contain an active peptide with an amino acid sequence identified as Pro-Met-Pro-Leu-Asn-Ser-Cys (756 Da). The purified peptides from powdered katsuobushi (dried bonito) had an $EC_{50}$ value of $105.82{\mu}M$, and exhibited an inhibitory effect against DNA oxidation induced by hydroxyl radicals. Taken together, these results suggests that powdered katsuobushi (dried bonito) could be used as a natural antioxidant in functional foods and prevent oxidation reactions in food processing.

• Journal of Animal Science and Technology
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• v.53 no.3
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• pp.223-226
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• 2011

The current study was undertaken to determine the effect of retinoic acid (RA) on proliferation and differentiation of preadipocytes from male and female pigs. The preadipocytes were isolated from new-born male and female pigs by collagenase digestion and washed three times one day after seeding (designated as day 0 of culture). RA was included in the media at various concentratives from day 0 to 2. The cell number was measured on day 2 with hematocytometer after trypsin digestion. Cell differentiation was determined on day 6 by measuring glycerol-3-phosphate dehydrogenase activity. RA (0.1, 1 and 10 uM) showed no effect on proliferation of preadipocytes from both male and female pigs. However, RA significantly decreased differentiation of pig preadipocytes. Degree of differentiation with 0.1 uM, 1 uM and 10 uM of RA treatment was 80%, 41% and 29% respectively, compared with control. Similar inhibitory effect was found in the female pigs; 77%, 28% and 16% respectively. It is interesting that RA treated on cell proliferation stage had no effect on proliferation but had a strong inhibitory effect on differentiation which is happening in the late stage of cell culture.

• Microbiology and Biotechnology Letters
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• v.17 no.5
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• pp.529-532
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• 1989

A strain of Streptomyces sp. (YS-221-B) extracellularly produced an inhibitory substance for $\alpha$-D-Glucosidase. The substance was purified 96-fold from culture filtrate by dialysis, heat treatment, adsorption on active carbon, Bio-Gel P-10 and Sephadex G-75 column chromatography with yield of 9.2%. The substance was stable in pH range from 7.0 to 11.0 at 37$^{\circ}C$, and a treatment at 10$0^{\circ}C$ for 20 min diminished only 15% of the original activity. The inhibitor was not inactivated by the treatment of $\alpha$-, $\beta$-amylases, glucoamylases, trypsin and chymotrypsin but inactivated by pyoteases from Streptomyces griseus and Tritirachium album.

• The Korean Journal of Food And Nutrition
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• v.11 no.6
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• pp.678-682
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• 1998

A strain of Streptomyces sp. SK-862, isolated from soil in Wonju city, was able to prodce a biologically active substance that has a strong inhibitory activity against proteolsis by trypsin. The inhyibitory substance was extracted by n-butanol, and then purified by the adsorption chromatography followed by the reverse-phase high performacne liquid chromatography. The purified substance was stable over the pH range from 2 to 10, but was unstable when treated at 8$0^{\circ}C$ for 60 min. This substance was soluble in water, methanol, ethanol nd butanol, but insoluble in chlorofrom and ethylacetate. The Rf value of the purified substance on the thin layer chromatography were 0.56 in n-butanol : methanol : water(5 : 3 : 1v/v) solvent system compare dto 0.23 in ethanol : ammonium hydoxide : water(8 : 1 : 1v/v) solvent system. This substance has maximum absorption at 259 nm. The chemical reaction of the substance was negative for sugar but positive for ninhydrine and iodine reaction.