• Korean Journal of Food Science and Technology
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• v.23 no.5
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• pp.554-560
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• 1991

The physicochemical properties of Korean yam starches (D. aimadoimo, D. batatas and D. japonica) were investigated. The mean granular size of starches were 23.5 μm for D. aimadoimo, 23.9 μm for D. batatas and 18.2 μm for D. japonica. Amylose content, blue value and water binding capacity was $29{\sim}33%,\;0.42{\sim}0.51%\;and\;109.9{\sim}118.3%$, respectively. The optical transmittance of 0.3% (dry basis) yam starch suspensions were increased at $70{\sim}75^{\circ}C$ and D. japonica showed typical two-step transmittance curve. The swelling power and solubility patterns increased over $60^{\circ}C$, and D. aimadoimo was the highest values. Amylogram patterns of 5% (dry basis) yam starch suspensions, determined by Brabender amylograph, were similar to that of yam flours and the viscosity of D. aimadoimo had 630 BU, which was about 5 times higher than 130 BU for D. batatas and D. japonica. Observation under scanning electron microscope lefted marks of resistance to glucoamylase because these surfaces were similar to the natural granules. In rates of solubiliazation by dimethyl sulfoxide, D. aimadoimo showed the highest value. (3-Amylolysis limits of yam starches and their amylose were $71.8%{\sim}75.5%\;and\;90.2{\sim}92.1%$, respectively. Gel filtration patterns of debranched amylopectin by pullulanase were divided into 3 peaks. The weight ratios of peak III to peak II in yam starches were $2.15%{\sim}2.42%$.

• 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).

• Applied Biological Chemistry
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• v.46 no.3
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• pp.201-206
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• 2003

An apple wine was prepared by fermentation at $25^{\circ}C$ for 2 weeks using Saccha개myces cerevisiae KCCM 12224, followed by aging at $15^{\circ}C$ for 14 weeks, and its physicochemical and microbiological changes were investigated. The viable bacterial cell numbers, increased from $1.4{\times}10^3\;CFU/ml$ at the beginning of fermentation, to $2.8{\times}10^6\;CFU/ml$ after 2 weeks, but decreased to $1.0{\times}10^5\;CFU/ml$ after aging. The viable yeast cell numbers changed from $4.3{\times}10^4\;CFU/ml$ to $1.2{\times}10^7\;CFU/ml$ during the fermentation, and decreased to $1.2{\times}10^4\;CFU/ml$ after aging. Sugar content changed from $20.0^{\circ}Brix$ to $8.5{\circ}Brix$, and reducing sugar content was changed from 9.66% to 6.44%. Alcohol content and acidity increased to 7.0% and from 0.19% to 0.24%, respectively. No changes in acidity, pH, and sugar content were observed during the aging, but reducing sugar and solid contents decreased. When apple wine was fultered through $0.45\;{\mu}m$ nitrocellulose membrane followed by various ultrafiltration membranes with different molecular weight cut-off values, the initial flux $(121.2\;liter/m^2/h)$ and the average flux of Biomax 100k membrane were the highest among the membranes used. These membrane filtration treatments resulted in complete removal of microorganisms as well as decrease in turbidity and solid content without changes in other chemical properties. No changes in the physicochemical properties of the apple wine and no microorganisms were detected during the storage at $156{\circ}C$ for 6 weeks.

• The Korean Journal of Mycology
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• v.40 no.4
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• pp.244-253
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• 2012

The effect of fermented Rhus verniciflua stem bark (FRVSB) extract on the microbial count, enzyme activity, concentrations of free amino acids and organic acids, and physiochemical properties of doenjang (soybean paste) was evaluated during brine fermentation. The FRVSB extract increased the total free amino acid concentration by 1.3-3.1-fold on the $42^{nd}$ day of brine fermentation. After the filtration of brine, the following microbial counts were obtained in the doenjang: bacteria, $0.3{\times}10^8-12.0{\times}10^8$ cfu/g; mold, $3.0{\times}10^4-21.0{\times}10^4$ cfu/g; yeast, $1.0{\times}10^4-2.0{\times}10^4$ cfu/g; Escherichia coli, not detected; and Bacillus cereus, $3.0{\times}10^2-25.0{\times}10^2$ cfu/g. The FRVSB extract addition enhanced the protein and starch degrading activity by 13.8-26.0% and 16.1-35.1%, respectively. The extract increased the total free amino acid content by 1.4-3.0-fold. Lactic acid, acetic acid, and pyroglutamic acid were the predominant organic acids in doenjang. Moreover, the proximate composition, pH, moisture, ash, salt, and amino nitrogen content were increased.

• The Korean Journal of Nuclear Medicine
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• v.28 no.3
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• pp.364-370
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• 1994

The purpose of this study is to evaluate the clinical application of the no carrier added $[^{51}Cr]Cr(III)$-EDTA complexes, produced at Korea Cancer Center Hospital. The $[^{51}Cr]Cr(III)$-EDTA complexes, usefut for measurement of GFR were prepared at room temperature in the presence of bicarbonate catalysts. The radiochemical purity of $[^{51}Cr]Cr(III)$-EDTA was over 99% by paper electrophoresis. The time activity curves were obtained by counting the blood samples from 5 volunteers and counting the head and neck regions with whole body counter after injection of the $^{51}Cr$-EDTA, respectively. After the nonlinear regression, the area under curve was obtained. The plasma clearance of the $^{51}Cr$-EDTA was calculated with injected dose/AUC. The clearance rate calculated with the head and neck counting data was in good agreement with the result from the plasma sample radioactivity at 1-3 hrs after injection. From this result, the counting of head and neck region and the nonlinear regression by 2-compartment model could be applied for the measurement of the clearance rate. Using MIRD system, the absorbed radiation dose was calculated by residence $time{\times}S$. The absorbed whole body radiation dose was negligibly small.

• Korean Journal of Microbiology
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• v.44 no.3
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• pp.228-236
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• 2008

Validation of viral safety is essential in ensuring the safety of mammalian cell culture-derived biopharmaceuticals, because numerous adventitious viruses have been contaminated during the manufacture of the products. Mammalian cells are highly susceptible to Reovirus type 3 (Reo-3), and there are several reports of Reo-3 contamination during the manufacture of biopharmaceuticals. In order to establish the validation system for the Reo-3 safety, a real-time RT-PCR method was developed for quantitative detection of Reo-3 in cell lines, raw materials, manufacturing processes, and final products as well as Reo-3 clearance validation. Specific primers for amplification of Reo-3 RNA was selected, and Reo-3 RNA was quantified by use of SYBR Green I. The sensitivity of the assay was calculated to be $3.2{\times}10^0\;TCID_{50}/ml$. The real-time RT-PCR method was proven to be reproducible and very specific to Reo-3. The established real-time RT-PCR assay was successfully applied to the validation of Chinese hamster ovary (CHO) cell artificially infected with Reo-3. Reo-3 RNA could be quantified in CHO cell as well as culture supernatant. When the real-time RT-PCR assay was applied to the validation of virus removal during a virus filtration process, the result was similar to that of virus infectivity assay. Therefore, it was concluded that this rapid, specific, sensitive, and robust assay could replace infectivity assay for detection and clearance validation of Reo-3.

• Journal of fish pathology
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• v.18 no.1
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• pp.67-80
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• 2005

Phosphoinositide-specific phospholipase $C\delta$ $PLC\delta$) plays an important role in many cellular responses and is involved in the production of second messenger. The present study was conducted to obtain the biochemical characteristics of the expressed recombinant $PLC\delta$ in E. coli cloned from Misgurnus mizolepis and partially purified $PLC\delta$ enzymes from liver tissues of M. mizolepis (wild ML-$PLC\delta$). The ML $PLC\delta$ gene was cloned and expressed under the previous report (Kim et al., 2004), and purified the recombinant protein by successive chromatography using $Ni^{2+}$-NTA affinity column and gel iltration FPLC column. The wild ML-$PLC\delta$ protein was solublized with 2 M KCI and purified by successive chromatography on open heparin-Sephagel and analytical TSKgel heparin-5PW. Both the recombinant and wild ML-$PLC\delta$ form of protein showed a concentration-dependent PLC activity to phosphatidylinositol 4,5-bis-phosphate (PIP$_2$) or phosphatidylinositol (PI). Its activity was absolutely $Ca^{2+}$- dependant, which was similar to mammalian $PLC\delta$ isozymes. Maximal PI-hydrolytic activations of recombinant and wild ML- TEX>$PLC\delta$ was at pH 7.0 and pH 7.5, respectively. In addition, the enzymatic activities of recombinant and wild ML-$PLC\delta$ were increased in concentration-dependent manner by detergent, such as sodium deoxycholate SDC), phosphatidylethanolamine (PE) and phosphatidylcholine (PC). The activities decreased in contrast by a polyamine, such as spermine. Western blotting showed that several types of $PLC\delta$ isozymes exist in various organs. Taken together our results, it suggested that the biochemical characteristics of ML-$PLC\delta$ are similar with those of mammalian $PLC\delta1$ and ${\delta}3$ isozymes.

• Korean Journal of Food Science and Technology
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• v.40 no.5
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• pp.522-527
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• 2008

Low molecular peptides were isolated from Asterias amurensis via SDS-PAGE. The peptides were separated via consecutive gel filtration as five fractions (F1-F5) according to molecular weights, based on the results of MALDI-TOF MS analysis. The molecular weight of the most active peptide was estimated as 15,000 daltons. The peptide showed cytotoxicity on normal human fibroblast cells at levels as low as 20% when 1.0 mg/mL of the samples was added. The peptide also exhibited higher levels of nitric oxide production from macrophages than the lipopolysaccaharides. It was determined that prostaglendin $E_2$ production was significantly inhibited, up to 127.8% as compared to the control. The low molecular peptide inhibited hyaluronidase activity as 535.7 ${\mu}g/mL$ of $IC_{50}$. It can be concluded that the relatively low molecular weight peptide, fucoidan, from A. amurensis has excellent cosmetic and immunomodulatory activities, which can be considered as a possible resource of new cosmetic agents for skin immunomodulation.

• Korean Journal of Environmental Agriculture
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• v.31 no.4
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• pp.351-358
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• 2012

BACKGROUND: Constructed wetlands for wastewater treatment are vegetated by wetland plants. Wetland plants are an important component of wetlands, and the plants have several roles in relation to the livestock wastewater treatment processes. The objectives of this study were to investigate the growth characteristics and nutrient absorption of water plants in constructed wetlands for treating livestock wastewater. METHODS AND RESULTS: In this study, livestock wastewater treatment plant by constructed wetlands consisted of $1^{st}$ water plant filtration bed, $2^{nd}$ activated sludge bed, $3^{rd}$ vertical flow(VF), $4^{th}$ horizontal flow(HF) and $5^{th}$ HF beds. Phragmites communis TRINIUS(PHRCO) was transplanted in $3^{rd}$ VF bed, Iris pseudoacorus L(IRIPS) was transplanted in $4^{th}$ HF bed and PHRCO, IRIPS and Typha orientalis PRESEL(THYOR) were transplanted in $5^{th}$ HF. Growth of water plants in constructed wetlands were the highest in October. The IRIPS growth was higher than other plant as 264 g/plant in October. The absorption of nitrogen and phosphorus by IRIS were 3.38 g/plant and 0.634 g/plant, respectively. The absorption of K, Ca, Mg, Na, Fe, Mn, Cu and Zn by water plants were higher in the order of IRIPS > THYOR > PHRCO. CONCLUSION(S): The absorption of nutrients by water plants were higher on the order of IRIPS > THYOR > PHRCO in constructed wetlands for treating livestock wastewater.

• Food Science of Animal Resources
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• v.22 no.1
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• pp.59-65
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• 2002

This study was carried out to evaluate the effect of whey protein concentrate-80%(WPC-80) and whey protein isolate(WPI) on the growth of B. bifidum Bb-11. Whey proteins($\alpha$-lactalbumin, $\beta$-lactoglobulin) were digested with trypsin, then their hydrolyzates were separated into three fractions (>10,000Da, 3,000∼10,000Da, <3,000Da) by two-step ultrafiltration process with Centriprep 10 and Centricon-30. These three fractions by molecular weight were evaluate growth-promoting effects for the B. bifidum Bb-11. The results obtained were summarized as follows; The growth rate of B. bifidum Bb-11 tended to increase by supplementation of WPC-80 to basal medium, but decreased by supplementation of WPI. Two whey proteins were hydrolyzed by trypsin at 40$\^{C}$ for 6 hrs, and three fractions were collected by UF treatment and concentrated by Centricon-30. Collected concentrations of protein of F-I and F-II and F-III from $\alpha$-lactalbumin were 11.53mg, 7.79mg, and 5.21 mg and those of protein from $\beta$-lactoglobulin were 4.13mg, 5.30mg, and 9.351mg, respectively. Three fractions of $\alpha$-lactalbumin hydrolyzates promoted the growth rate of B. dbifidum Bb-11. Growth promoting activities of hydrolyzates(F-I and F-II) with molecular weight below 10,000Da were stronger than that of hydrolyzate(F-III) above 10,000Da. However, there was no significant difference between the hydrolyzate F-I and F-II. Three fractions of $\beta$-lactoglobulin hydrolyzates improves the growth rate of B.bifidum Bb-ll. The growth of B.bifidum Bb-ll was decreased after 24 hr incubation by supplementation of either F-II or F-III fraction compared to basal Whey medium, but maintained the enhancement by supplementation of F-I.