• Proceedings of the Korea Society of Poultry Science Conference
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• 2000.11a
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• pp.75-77
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• 2000

Retaining migratory activity is a prerequisite for the manipulation and use of PGCs. This study was conducted to examine whether migratory activity is retained in the primordial germ cells(PGCs) from gonads at the later embryonic developmental stage. In the present study, gonads were dissected from 5-, 6- and 10-day-old quail embryos and treated with trypsin-EDTA for the degradation of gonadal tissue. Gonadal PGCs (gPGCs) were purified by Ficoll density gradient centrifugation and labeled with PKH26 fluorescent dye. The PKH26-labeled gPGCs were microinjected into the blood vessels of recipient quail embryo. After further incubation of 3 days, the manipulated recipients were embedded in paraffin and sectioned. The gPGCs were detected by their fluorescence under the fluorescent microscopy and the confocal laser microscopy. As a result, 10-day-old quail gPGCs as well as 5-and 6-day-old gPGCs, could migrate to recipient embryonic gonads and settle down. These results suggest that the 10-day-old gPGCs have the properties of circulating PGCs at early stage. Therefore the PGCs from 10-day old embryonic gonads can be used for the tools of genetic manipulation.

• Food Science of Animal Resources
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• v.22 no.1
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• pp.72-76
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• 2002

Bovine serum albumin(BSA), $\alpha$-lactalbumin($\alpha$-LA), $\beta$-lactoglobulin($\beta$-LG) and bovine immunoglobulin G (IgG) were investigated the cytotoxicity on tumor cell lines. $\alpha$-LA was showned a tendency of dose dependaent on cytotoxicity using WiDr. The growth of WiDr was inhibited 82% by 1mg/ml of $\alpha$-LA. However, IgG, BSA and $\beta$-LG were not shown the cytotoxicity on WiDr. When $\alpha$-LA was purified by using high pressure liquid chromatography(HPLC), the main component($\alpha$-LA) was eluted at 33.057 min and extremely small quantities eluted at 32.310 min. The cytotoxicity of main component (eluted at 33.057 min peak) was lower than commercial $\alpha$-LA. And the cytotoxic activity of hydrolyzed $\alpha$-LA and $\alpha$-LA treated with EDTA were lower than commercial $\alpha$-LA on tumor cells.

• Animal Bioscience
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• v.37 no.6
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• pp.1077-1084
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• 2024

Objective: The present work was conducted to evaluate suitable variables and develop prediction equations using chemical composition and physical characteristics for estimating standardized ileal digestibility (SID) of lysine (Lys) in full-fat soybeans (FFSB). Methods: The chemical composition and physical characteristics were determined including trypsin inhibitor activity (TIA), urease activity (UA), protein solubility in 0.2% potassium hydroxide (KOH), protein dispersibility index (PDI), lysine to crude protein ratio (Lys:CP), reactive Lys:CP ratio, neutral detergent fiber, neutral detergent insoluble nitrogen (NDIN), acid detergent insoluble nitrogen (ADIN), acid detergent fiber, L* (lightness), and a* (redness). Pearson's correlation (r) was computed, and the relationship between variables was determined by linear or quadratic regression. Stepwise multiple regression was performed to develop prediction equations for SID of Lys. Results: Negative correlations (p<0.01) between SID of Lys and protein quality indicators were observed for TIA (r = -0.80), PDI (r = -0.80), and UA (r = -0.76). The SID of Lys also showed a quadratic response (p<0.01) to UA, NDIN, TIA, L*, KOH, a* and Lys:CP. The best-fit model for predicting SID of Lys in FFSB included TIA, UA, NDIN, and ADIN, resulting in the highest coefficient of determination (R² = 0.94). Conclusion: Quadratic regression with one variable indicated the high accuracy for UA, NDIN, TIA, and PDI. The multiple linear regression including TIA, UA, NDIN, and ADIN is an alternative model used to predict SID of Lys in FFSB to improve the accuracy. Therefore, multiple indicators are warranted to assess either insufficient or excessive heat treatment accurately, which can be employed by the feed industry as measures for quality control purposes to predict SID of Lys in FFSB.

• Food Science of Animal Resources
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• v.44 no.3
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• pp.533-550
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• 2024

Peptides with bioactive effects are being researched for various purposes. However, there is a lack of overall research on pork-derived peptides. In this study, we reviewed the process of obtaining bioactive peptides, available analytical methods, and the study of bioactive peptides derived from pork. Pepsin and trypsin, two representative protein digestive enzymes in the body, are hydrolyzed by other cofactors to produce peptides. Bicinchoninic acid assay, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, chromatography, and in vitro digestion simulation systems are utilized to analyze bioactive peptides for protein digestibility and molecular weight distribution. Pork-derived peptides mainly exhibit antioxidant and antihypertensive activities. The antioxidant activity of bioactive peptides increases the accessibility of amino acid residues by disrupting the three-dimensional structure of proteins, affecting free radical scavenging, reactive oxygen species inactivation, and metal ion chelating. In addition, the antihypertensive activity decreases angiotensin II production by inhibiting angiotensin converting enzyme and suppresses blood pressure by blocking the AT1 receptor. Pork-derived bioactive peptides, primarily obtained using papain and pepsin, exhibit significant antioxidant and antihypertensive activities, with most having low molecular weights below 1 kDa. This study may aid in the future development of bioactive peptides and serve as a valuable reference for pork-derived peptides.

• Journal of the Korean Society of Food Science and Nutrition
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• v.11 no.4
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• pp.7-12
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• 1982

Growth of soybean sprouts(Glycine Max L.) and amounts of some chemical components were measured when they were exposed to blue light (120lux, 3hrs/day) during their growth. Hypocotyl length of irradiated soybean sprouts exceeded slightly that of control (dark) soybean sprouts, but the tfresh weight of whole sprouts as well as each part of the sprout showed no difference between the two groups. Chlorophyll content of cotyledon under blue light increased significantly with the lapse of days (3.57 and $8.45\;{\mu}g/100g$ fresh weight on the 3rd and 7th day). Bluelight irradiated sprouts contained more vitamin C than control sprouts (21.7% and 30.8% higher for the cotyledon and hypocotyl). Total amount of protein was not affected. Hypocotyl protein content was 8% of that in original soybean. Blue light did not affect the activity of trypsin inhibitor of sprouts. Similar activity of the inhibitor was observed in the cotyledon whereas hypocotyl showed activity corresponding to 23.7% of original bean. Polyacrylamide gel electrophoretogram for the protein showed 10, 9, and 11 bands in the original bean. 5th day cotyledon and hypocotyl respectively. Especially, band 3 of low Rm value was major protein component for the hypocotyl. Band 5 and 11 could be seen only in the protein of hypocotyl from bluelight irradiated sprouts, whereas no effect of blue light on the electrophoretogram was observed for the cotyledon.

• KSBB Journal
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• v.25 no.3
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• pp.289-296
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• 2010

Lectins are carbohydrate-binding and a cell-agglutinating proteins, and are concerted with a plants defence mechanism. In particular, chitin-binding lectins in locular fluid of cherry tomato fruit seemed to have a role in defending plants against fungi. The antifungal activity using lectin isolated from locular fluid of cherry tomato fruit was measured in the plant pathogen Cladosporium cucumerinum, Monosporascus cannonballus, Fusarium oxysporum, and Rhizoctonia solani. Amoung the four strains, a potent antifungal activity was detected in Cladosporium cucumerinum and Monosporascus cannonballus, not in Fusarium oxysporum, and Rhizoctonia solani. The molecular weight of this lectin isolated as double protein bands by SDS-PAGE was calculated to be 87 kDa and 47 kDa from the relative mobilities compared with those of reference molecular weight markers. The isolated lectin agglutinated human red blood cells (A, B, AB, O) treated with trypsin, and the most activity was found at B. The optimal temperature of isolated lectin was at $30^{\circ}C$. For the thermal stability, lectin was stable at $20-80^{\circ}C$. The optimal pH of this lectin was at 7.2, and showed complete loss below pH 9.0.

• Journal of Life Science
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• v.25 no.2
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• pp.180-188
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• 2015

The bacterial strain isolated from Kimchi showed antibacterial activity against Micrococcus luteus IAM 1056. The selected strain was identified as Lactococcus lactis by 16S rRNA nucleotide sequence analysis and named as Lactococcus sp. KD 28. The treatment of culture supernatant with proteinase K removed antibacterial activity, indicating its proteinaceous nature, a bacteriocin. This bacteriocin was sensitive to hydrolytic enzymes such as ${\alpha}$-chymotrypsion, trypsin, proteinase K, lipase, ${\alpha}$-amylase and subtilisin A. The bacteriocin was highly thermostable and resistant to heating at $80^{\circ}C$ for up to an hour but 50 % of the total activity was remained at $100^{\circ}C$ for 30 min. The pH range from 2.0 to 8.0 had no effect on bacteriocin activity and it was not affected by solvents such as acetonitrile, isopropanol, methanol, chloroform and acetone up to 50% concentration. The bacteriocin showed antibacterial activity against M. luteus IAM 1056, Lactobacillus delbrueckii subsp. lactis KCTC 1058, Enterococcus faecium KCTC 3095, Bacillus cereus KCTC 1013, B. subtilis KCTC 1023, Listeria ivanovii subsp. ivanovii KCTC 3444, Staphylococcus aureus subsp. aureus KCTC 1916, B. megaterium KCTC 1098 and B. sphaericus KCTC 1184. The bacteriocin was purified through ammonium sulfate concentration, SP-Sepharose chromatography and RP-HPLC. The molecular weight was estimated to be about 3.4 kDa by tricine-SDS-PAGE analysis.

• Asian-Australasian Journal of Animal Sciences
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• v.23 no.4
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• pp.430-436
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• 2010

The objective of the present studies was to develop and validate a system for isolation, purification and extended culture of pigment-producing cells in alpaca skin (melanocytes) responsible for coat color and to determine the effect of alpha melanocyte stimulating hormone treatment on mRNA expression for the melanocortin 1 receptor, a key gene involved in coat color regulation in other species. Skin punch biopsies were harvested from the dorsal region of 1-3 yr old alpacas and three different enzyme digestion methods were evaluated for effects on yield of viable cells and attachment in vitro. Greatest cell yields and attachment were obtained following dispersion with dispase II relative to trypsin and trypsin-EDTA treatment. Culture of cells in medium supplemented with basic fibroblast growth factor, bovine pituitary extract, hydrocortisone, insulin, 12-O-tetradecanolphorbol-13-acetate and cholera toxin yielded highly pure populations of melanocytes by passage 3 as confirmed by detection of tyrosinase activity and immunocytochemical localization of melanocyte markers including tyrosinase, S-100 and micropthalmia-associated transcription factor. Abundance of mRNA for tyrosinase, a key enzyme in melanocyte pigment production, was maintained through 10 passages showing preservation of melanocyte phenotypic characteristics with extended culture. To determine hormonal responsiveness of cultured melanocytes and investigate regulation of melanocortin 1 receptor expression, cultured melanocytes were treated with increasing concentrations of ${\alpha}$-melanocyte stimulating hormone. Treatment with ${\alpha}$-melanocyte stimulating hormone increased melanocortin receptor 1 mRNA in a dose dependent fashion. The results demonstrated culture of pure populations of alpaca melanocytes to 10 passages and illustrate the potential utility of such cells for studies of intrinsic and extrinsic regulation of genes controlling pigmentation and coat color in fiber-producing species.

• Microbiology and Biotechnology Letters
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• v.36 no.1
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• pp.49-54
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• 2008

The gene encoding human pancreatic pro-carboxypeptidase B (CPB) was cloned and fused to Saccharomyces cerevisiae mating factor alpha-1 secretion signal $(MF{\alpha}1)$, in which the transcription of $MF{\alpha}1$-pro-CPB was under the control of GAL10 promoter. The constructed plasmid $pY{\alpha}$-hproCPB(7.72 kb) was transformed into S. cerevisiae 2805. The recombinant human pro-CPB (hproCPB) was successfully expressed in S. cerevisiae after induction of galactose, and could be secreted into the culture medium. By analyses of SDS-PAGE and western blotting, the molecular weight of the purified hproCPB was estimated to be a 45.9kDa. The activity of extracellular hCPB after removal of pro-region by trypsin treatment reached about 10.16 unit/ml at batch culture of S. cerevisiae $2805/pY{\alpha}$-hproCPB for 60 h. Also, the Km value of partially purified recombinant hCPB is about 0.43 mM.

• Journal of the Korean Society of Food Science and Nutrition
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• v.41 no.5
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• pp.721-726
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• 2012

Lactic acid bacteria (LAB) are able to secrete antimicrobial peptides called bacteriocins, which inhibit other bacteria such as pathogenic microorganisms. Therefore, bacteriocin-producing starters can be used as natural biopreservatives for various foods. The objective of this study was to screen and characterize bacteriocin-producing LAB from Kimchi and to investigate their applicability as a starter in Kimchi fermentation. To screen bacteriocin-producing LAB, gram-positive and gram-negative bacteria were used as indicators. To measure the antimicrobial activities of isolates, agar well diffusion assay method was used. According to the results, bacteriocin produced by $Lb.$ $sakei$ B16 showed antimicrobial activity against $Listeria$ $monocytogenes$ ATCC 19115, $Escherichia$ $coli$ KCTC 1467, and$Lactobacillus$ $plantarum$ KTCT 3104. Furthermore, bacteriocin was very stable after treatment with high temperature and high and low pH, but its effects were inhibited by treatment with proteolytic enzymes such as trypsin, proteinase K, and ${\alpha}$-chymotrypsin, revealing their bacteriocin-like protein- based structure. These results suggest that $Lb.$ $sakei$ B16 and its bacteriocin are good candidates as a functional probiotic and natural biopreservative, respectively, in fermented foods.