• Food Science of Animal Resources
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• v.42 no.5
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• pp.800-815
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• 2022

This study aimed to obtain high Fischer's ratio oligopeptides from goat whey (HFO) and investigate antioxidant property of it. Hydrolysis of goat whey was done with the approach of sequential digestion of pepsin and flavourzyme. With the adsorption of aromatic amino acids by activated carbon, HFO with a Fischer's ratio of 27.070 and a molecular weight of 200-1,000 Da were obtained, and the branched-chain amino acids accounted for 22.87%. Then the antioxidant activity of HFO was evaluated. At the concentrations of 2.0 mg/mL and 0.50 mg/mL, HFO scavenged 77.27% and 99.63% of 1,1-diphenyl-2-picrylhydrazyl and 3-ethylbenzthiazoline-6-sulphonate free radicals respectively. The scavenging rate of HFO against hydroxyl radicals reached 92.31% at the concentration of 0.25 mg/mL. Animal experiments demonstrated that HFO could moderate the changes of malondialdehyde, superoxide dismutase and glutathione peroxidase caused by CCl₄-induced oxidative stress in vivo. This study indicated that HFO from goat whey was capable of oxidation resistance both in vivo and in vitro, which provided a scientific basis for the high-value processing and application of goat milk whey.

• Proceedings of the Ginseng society Conference
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• 1993.09a
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• pp.124-126
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• 1993

• Applied Biological Chemistry
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• v.6
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• pp.89-106
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• 1965

• 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.

• Applied Biological Chemistry
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• v.15 no.2
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• pp.111-142
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• 1972

An experimental Chung-Kook-Jang was prepared using the strain Bacillus subtilis sp. isolated by the author Samples were taken in 12 hrs interval during the fermentation and the oligopeptides were separated by the method of molecular sieving using the ion exchange resin column of Dowex-50. Only the X-16 fraction of oligopeptides was taken and the components of oligopeptides were developed in two dimensional thin layer chromatograms. The each peptide spot was eluted and each peptide was isolated. The pattern and kinds of amino acids, and N and C-terminal amino acids were studied. Fourteen different oligopeptides could be detected by the two dimensional thin layer chromatography, all of which were consisted of $4{\sim}9$ kinds of amino acids. No dipeptides and no tripeptides could be found. The N and C-terminal amino acids and the residual component amino acids of all these 14 peptides could be summarized as the follows. [P]-I. Pro (Cys Ala Asp Trp Ile Val) Glu [P]-II. Val (His Arg Glu Thr Ala Met) Asp [P]-III. Glu (Cys Lys Asp Thr Met) Ala [P]-IV. Glu(His Ser Ala) Met) [P]-V. Ile (Cys Asp Arg Gly Pro T.p Phe) His [P]-VI. Gly(Asp ser) Lys [P]-VII. Thr(Pro Tyr Phe) Asp [P]-VIII. Phe(Tyr Leu Ile) Val [P]-IX. Trp (Phelle) Thr [P]-X. Ile (Arg Leu) Phe [P]-XI. Asp (Lys His Ser Gly Glu Pro) Ala [P]-XII. Glu (Cys Asp Gly) Ser [P]-XIII. Ala (Arg Tyr) Glu [P]-XIV. Met (Glu Ala) His It appears that the protease of the Bacillus subtilis K-27 syrain has rather wider range of specificity than proteases of Aspergoillus soya, pepsin, chymotrypsin, and trypsin.

• Journal of Sericultural and Entomological Science
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• v.50 no.2
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• pp.161-165
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• 2012

Antimicrobial peptides of insects are found and reported as immune defence system against infectious agents. The peptides are produced by fat body cells and thrombocytoids, a blood cell type. Defensin is 38-45 amino acids long and consists of an ${\alpha}$-helix linked by a loop to an antiparallel ${\beta}$-sheet. Defensin from a bumblebee, Bombus ignitus, is known to comprise 52 amino acid residues. This peptide consists of two ${\alpha}$-helixes; ACAANCLSM and KTNFKDLWDKRF and one ${\beta}$-sheet; GGRCENGVCLCR. We carried out antibacterial activity test by radial diffusion assay against Staphylococcus aureus (Gram positive), Escherichia coli (Gram negative), Pseudomonas syringae (Gram negative), Candida albicans (fungi), MDRPA, MRSA, and VRE (antimicrobial resistant microbes) with synthetic oligopeptides from Peptron (Daejeon, Korea). The predicted curtailment fragment (GGRCEVCLCR-$NH_2$) for ${\beta}$-sheet had strong antibacterial activity when internal amino acids were removed. But, curtailment fragments (ACAANCLSM-$NH_2$ and TNFKDLWDKR-$NH_2$) of ${\alpha}$-helix were not showed antibacterial activity. These synthetic oligopeptides were showed the great activity against Gram positive and negative bacteria.

• 대한치주과학회:학술대회논문집
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• 2002.11a
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• pp.46-47
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• 2002

• Applied Biological Chemistry
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• v.30 no.1
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• pp.88-94
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• 1987

To investigate ginseng oligopeptides with biological activities, the water extract was purified by ultra-filtration, gel filtration, ion-exchange and thin layer chromatography. Ultra-filtered water extract exhibited antilipolytic activity, inhibiting epinephrine-induced lipolysis in the isolated fat cells of rat epididymal adipose tissue. The filtrate was separated into 3 fractions by Sephadex G-25 gel filtration. Peptides were found only in the first fraction(S-FI). Saponine and sugars were also detected in tie fraction. S-FI fraction resolved further into 6 fractions by Dowex 50 ion-exchange chromatography. The sugar and saponine depleted fraction(P-F2) from the second chromatography showed antilipolytic activity. The P-F2 fraction revealed 6 spots on TLC. The 6 spots were isolated by TLC and identified as peptides.

• Korean Journal of Microbiology
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• v.7 no.3
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• pp.115-124
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• 1969

The mash of Takjoo, Korean flour wine, is fermented through two brewing processes ; the primary brewing process to saccharify and the main one to produce ethyl alcohol. The activities of acid proteinase (pH3), weak acid proteinase (pH 6), and alkaline proteinase (Ph 80 on the processes are determined with time by the Folin phenol method as a strength of casein digestion. Hydrogen ion concentration, the content of total organic acids, protein, free amino acids and oligopeptides, which effect the activities of proteinase, are also measured. The results are briefly summarized as follows : 1. In general, the activities of acid proteinase and weak acid proteinase in the mesh of primary brewing process are stronger than those in main brewing process. 2. The activities of acid proteinase are remarkably stronger than those of weak acid proteinase in both processes. It reveals that they decrease slowly through the fermentation. Activities of alkaline proteinase are weaker than others. 3. As the raw materials are mixtured, the total amount of organic acids is equivalent to 0.150 mg/ml acetic acid in the mesh of primary brewing process and 0.02 mg/ml acetic acid in the main one. They increase gradually with time. 4. Hydrogen ion concnetration shows 3.9 in the mesh of main brewing process and 3.28 in the primary one. They increase to the maximum in 60-72 hrs., and decrease since 108 hrs. 5. The content of crude protein shows 66.90mg/ml in the mesh of main brewing process, while shows 64.29mg/ml in the mesh of primary one. they decrease slowly with time. it seems that a small content of crude protein, as a substrate, converts into amino acids and soluble nitrogen compounds by proteinase. 6. The content of free amino acids and oligopeptides shows 0.36 mg/ml in the mesh of primary brewing process and 0.24mg/ml in the main brewing process. It is evident that the reason they increase continuously through the fermentation is the effect of proteinase. 7. According to the results, the strong activities of proteinase in primary brewing process has been derived from the decrease of hydrogen ion concentration due to the production of organic acids.

• Journal of fish pathology
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• v.24 no.2
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• pp.75-84
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• 2011

The amino acid sequence of glycoprotein of Korean VHSV isolate (KR'01-1) was analyzed using the DNAStar Protean system. Based on the flexibility, hydrophilicity, antigenic index and surface probability, three regions (Gp1, Gp2 and Gp3) were selected as potential antigenic determinants. Three oligopeptides containing the amino acid sequences of the three regions were synthesized and polyclonal antibodies were raised against them. The activities of the antibodies were analyzed by Western blotting and virus neutralization test. The results showed that antibodies raised against oligopeptides Gp1 and Gp2 neutralized the infectivity of VHSV, suggesting that they can be possible candidates for subunit vaccines against VHS diseases in olive flounder.