• Journal of the Korean Society of Food Science and Nutrition
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• v.17 no.4
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• pp.312-319
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• 1988

The functional properties of plasteins have been compared with those of sardine protein concentrate and egg albumin. The solubility of plasteins was higher than that of FPG and the glu-plastein had 84% solubility in the range of pH 3-10. The dispersibility of plasteins was lower than that of egg albumin, however those of plasteins was higher than that of sardine protein concentrate. The water holding capacity of plasteins was higher than that of egg albumin. Lipid absorption of leu-papain plastein was the highest, holding 2.2m119, and that of the other plastein was higher than that of egg albumin. The emulsifying activity of leu-papain plastein was the highest, holding 66.4%, and that of glu-papain plastein was the lowest, holding 51.2%, The emulsifying stability of plasteins was similar to that of the emulsifying activity. The foaming capacitt of leu-papain plastein was the highest, holding 460%, and those of the other plasteins was higher than that of egg albumin. The foaming stability of plasteins was superior to that of egg albumin. The viscosity of plasteins was lower than that of see albumin. The in vitro digestibility of plasteins was 67.6-78.0% range. The digestibility by four pretense were somewhat lower in the glu-papain plastein than in the FPG. The digest of plasteins treated with the microbiol pretense such as molsin and pretense(from Streptomyces griceus), which had a storage broth taste.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.20 no.6
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• pp.582-590
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• 1987

Plasteins were synthesized from a peptic filefish protein hydrolysate by papain, $\alpha-chymotrypsin$ and protease(from Streptomyces griceus) under the optimum conditions of previous paper. L-glutamic acid diethylester and L-leucine ethylester were incorporated into plastein during the plastein reaction by papain. The structural changes of freeze-dried filefish meat, peptic hydrolysate, FPC and plasteins were observed by Scanning Electron Microscopy(SEM). The functional properties of plasteins also were measured. The solubility of plasteins was higher than that of FPC and the Glu-plastein had $95\%$ solubility in the range of pH 3-10. The dispersibility of Glu-plastein and protease plastein was similar to that of egg albumin, but those of the other plasteins were lower. The water holding capacity of plasteins was lower than that of egg albumin and C. Lipid absorption of Leu-plastein was tile highest, holding 1.80 ml/g, and that of the other plasteins was similar to that of egg albumin. The emulsifying activity of Leu-plastein was the highest, holding $61.2\%$, and that of Glu-plastein was the lowest, holding $50.7\%$. The emulsifying stability of plasteins was similar to that of the emulsifying activity. The emulsifying capacity of Leu-plastein was 384 ml/g(the highest), but that of Glu-plastein and $\alpha-chymotrypsin$ plastein was 248 ml/g(the lowest). The Leu-plastein shelved the highest foaming capacity, $373\%$. The foaming capacity of other plasteins was higher than that of egg albumin. The foaming stability of plasteins was superior to that of egg albumin. The viscosity of plasteins was lower than that of egg albumin. The microstructure of $\alpha-chymotrypsin$ plastein by SEM wassimilar to that of papain plastein, but other plasteins showed differences in their microstructure. The microstructure of Glu-plastein had a smooth shape.

• The Korean Journal of Food And Nutrition
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• v.9 no.3
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• pp.253-258
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• 1996

Stabilities of sweets potato f-amylase on various reagents were studied. The enzyme was stabilized by bovine serum albumin, Triton X-100 and 2-mercaptoethanol of 0.04%. Among them, bovine serum albumin was the most effective. And enzyme stability was increased by using the deairated solution. The enzyme activity was remained 0% in the absence of glycerol, 25% in the presence of 20% glycerol and 50% in the presence of 40% glycerol at 37$^{\circ}C$, for 15 hours in pH 11. SDS inhibited the enzyme, and 2-mercaptoethanol and dithiothreitol stabilized it.

• Polymer(Korea)
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• v.37 no.3
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• pp.262-268
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• 2013

pH-sensitive P(MAA-co-PEGMA) hydrogel particles were prepared and their feasibility as smart delivery carriers for cosmetic ingredients was evaluated. P(MAA-co-PEGMA) hydrogel particles having an average size of approx. $2{\mu}m$ were synthesized via dispersion photopolymerization. There was a drastic change in the swelling ratio of P(MAA-co-PEGMA) particles at a pH of around 5 due to the ionization of MAA in the hydrogel and as the amount of MAA in the hydrogel increased, the swelling ratio increased at a pH above 5. The P(MAA-co-PEGMA) hydrogel particles showed a pH-sensitive release behavior. Thus, at pH 4 almost none of the albumin permeated through the skin while at pH 6 relatively high skin permeability was obtained. The albumin loaded in the P(MAA-co-PEGMA) hydrogel particles was hardly degraded in the presence of pepsin and its stability was maintained.

• The Korean Journal of Nuclear Medicine
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• v.23 no.1
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• pp.63-69
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• 1989

In order to develop technetium-99m-labelled human albumin microsphere (HAM) for lung scintigraphy, various experimemts such as preparation and fractionation of HAM, establishment of optimal labelling conditions, determination of radiochemical purity, stability test and biodistribution of $^{99m}Tc-HAM$ were carried out. HAM was prepared from the suspension of 1ml aqueous human serum albumin (25%) in 130 ml of olive oil at $130\sim135^{\circ}$ with vigorous stirring. The resulting HAM was fractionated with microsieve to get the desired particle size $(15\sim50\mu)$ and autoclaved for sterilizaiton. The HAM particles were treated with stannous chloride and the pH of the suspension was adjusted to $3.0\sim3.5$ with phosphate buffer. After freeze-drying the contents of single reaction vial containing 5 mg of HAM and 0.2 mg of $SnCl_2$ it was reacted with $Na^{99m}TcO_4$. The labelling yield was higher than 99.5% and the stability of $^{99m}Tc-HAM$ was high enough to maintain 99.1% of radiochemical purity up to 24 hours. Lung and liver uptake in mice was found to be 94% and 0.9%, respectively. Excellent rabbit and human lung scans were also obtained.

• Korean Journal of Microbiology
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• v.39 no.1
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• pp.62-65
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• 2003

A procedure to increase the stability of 6B capsular polysaccharide on microbead surface in the mutibead assay, a serotyping method for Streptococcus pneumoniae, was studied. Pneumococcal capsular polysaccharide 6B was conjugated to bvine serum albumin (BSA), and the coating efficiency and the stability of the 6B-BSA complex was measured. The 6B-BSA complex showed about 200-fold higher coating efficiency to polystyrene surface than 6B polysaccharide. And the stability of the 6B- BSA to be used in the multibead assay for 30 days after coating.

• Clean Technology
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• v.27 no.1
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• pp.55-60
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• 2021

Antibiotics are compounds broadly used to treat patients with infectious diseases and to enhance productivity in agriculture, fisheries, and livestock industries. However, due to the overuse of antibiotics and their low biodegradability, a substantial amount of antibiotics is leaking into the sewer, subsequently resulting in pollution and the emergence of antibiotic-resistant bacteria. This study explores biodegradable serum albumin's potential as an adsorbent to remove antibiotics from water. Serum albumin is a natural blood protein that transports various metabolites and hormones to all tissues' extravascular spaces. While serum albumin is highly water-soluble, it has intrinsic binding sites which readily accommodate ionic, hydrophilic, or hydrophobic molecules, rendering it a good building block for a nano-adsorbent. To induce coacervation, a desolvating agent, ethanol, was added dropwise into the aqueous albumin solution, resulting in dehydration and liquid-liquid phase separation of albumins into albumin nanoparticles within a size range of 150 ~ 170 nm. The addition of glutaraldehyde as a cross-linker improved the size stability and homogeneity of albumin nanoparticles. Adsorption of amoxicillin antibiotics on albumin nanoparticles was dependent upon glutaraldehyde concentration used in desolvation and pH during adsorption. The maximum adsorption capacity measured by spectrophotometry was found to be 12.4 micrograms of amoxicillin per milligram of albumin nanoparticle. These results demonstrate serum albumin's potential as a building block for fabricating a natural nano-adsorbent to remove antibiotics from water.

• Bulletin of the Korean Chemical Society
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• v.28 no.5
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• pp.730-736
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• 2007

The interaction of a polyoxometal (POM), K6SiW11Co(H2O)O39.10H2O (K6) as a Keggin, with human serum albumin (HSA) was studied by different methods and techniques. Binding studies show two sets of binding sites for interaction of POM to HSA. Binding analysis and isothermal calorimetery revealed that, the first set of binding site has lower number of bound ligand per mole of protein (ν), lower Hill constant (n), higher binding constant (K), more negative entropy (ΔS) and more electrostatic interaction in comparison to the second set of binding site. In addition, differential scanning calorimetery (DSC) and spectrophotometery data showed that, there are two energetic domains. The first domain is less stable (lower Tm and Cp) which corresponds to the tail segment of HSA and another with more stability is related to the head segment of HSA. Polyoxometal also decreases the stability of protein as Tm, secondary and tertiary structure as well as quenching of the fluorescence decrease. On other hand, perturbations in tertiary structure are more than secondary structure.

• Biotechnology and Bioprocess Engineering:BBE
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• v.11 no.3
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• pp.268-272
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• 2006

A dense, pellicular UpFront adsorbent ($p=1.5 g/cm^3$, UpFront Chromatography, Cophenhagen, Denmark) was characterized in terms of hydrodynamic properties and protein adsorption performance in expanded bed chromatography. Cibacron Blue 3GA was immobilised into the adsorbent and protein adsorption of bovine serum albumin (BSA) was selected to test the setup. The Bodenstein number and axial dispersion coefficient estimated for this dense pellicular adsorbent was 54 and $1.63{\times}10^{-5}m^2/s$, respectively, indicating a stable expanded bed. It could be shown that the BSA protein was captured by the adsorbent in the presence of 30% (w/v) of whole-yeast cells with an estimated dynamic binding capacity $(C/C_o = 0.01)$ of approximately 6.5 mg/mL adsorbent.

• Archives of Pharmacal Research
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• v.14 no.4
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• pp.336-341
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• 1991

The effect of bovine serum albumin (BSA) on the encapsulation efficiency and stability of liposomes containing methotrexate (MTX) having different surface charges and cholesterol contents were investigated. The encapsulation efficiency of MTX was lower and the release of MTX was faster by the addition of BSA. The leaking of MTX from lipid bilayer depends upon the BSA concentrations. These results may be derived from the interaction of BSA with lipid bilayers. The dynamic structural changes of BSA were monitored indirectly using circular dichroism spectra. Observed dynamic structural changes of BSA with liposomes are presumed to reflect the interaction of BSA with liposomes. Negatively charged liposomes have more strong interaction with BSA than neutral and positively charged liposomes. BSA attacks lipid bilayers whether it is at the inner or at the outer phase of lipid bilayer and induces leakage of entrapped MTX. Especially, negatively charged liposomes are more sensitive than others. The inclusion of cholesterol in the lipid layers inhibits the interaction of BSA with liposomes and shows protective effect against BSA-induced leakage of MTX. To endure the attacking of BSA liposomes as drug carriers should be made using cholesterol.