• Environmental Engineering Research
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• v.22 no.3
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• pp.255-265
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• 2017

Polyelectrolytes are commonly used as flocculants in drinking water treatment. However the growing concerns about their toxicity have motivated the search for biocompatible flocculants. Here, we show that gelatin, a natural amphoteric polyelectrolyte, can be effectively adsorbed on clay surfaces and can potentially be a suitable substitute for existing flocculants. The adsorption of gelatin from its aqueous solution onto the mineral clay surfaces at different conditions was systematically investigated using the design of experiments methodology. The gelatin adsorption was found to vary considerately with pH variation showed a maximum adsorption at its isoelectric point. The amount of adsorbed gelation increased with increasing pH from 3 to 5, attained a maximum at pH 5 and then decreased with increasing pH from 5 to 11. Similarly, the amount of adsorbed gelatin showed decreasing trends around salt concentration of 0.05 M and temperature $35^{\circ}C$. On the other hand, the adsorption was continuously increased with time and polymer concentration in the range of 0.1-0.9 mg/dL. Finally, the jar tests confirmed the ability of gelatin for using a natural flocculant for water treatment.

• Microbiology and Biotechnology Letters
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• v.23 no.5
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• pp.573-579
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• 1995

A Bacillus strain capable of producing an extracellular malto-oligosaccharides forming $\alpha $-amylase was isolated from soil and designated as Bacillus sp. SUH4-2. The enzyme was purified by ammonium sulfate fractionation, DEAE-Toyopearl and Mono-Q HR 5/5 column chromatographies using a FPLC system. The specific activity of the enzyme was increased by 16.1-fold and the yield was 13.5%. The optimum temperature for the activity of $\alpha $-amylase was 60-65$\circ$C and more than 50% of initial activity was retained after the enzyme was incubated at 60$\circ$C for 40 min. The enzyme was stable over a broad pH range of 5.0-8.0 and the optimum pH was 5.0-6.0. The molecular weight of the enzyme was determined to be about 63.6 kD and isoelectric point was around 5.8. The enzyme activity was strongly inhibited by Mn$^{2+}$, Ni$^{2+}$, and Cu$^{2+}$ ; slightly by Ca$^{2+}$. The purified enzyme produced starch hydrolyzates containing mainly maltose and maltotriose from soluble starch. The starch hydrolyzates were composed of 11% glucose, 59% maltose, 25% maltotriose and 5% maltotetraose.

• YAKHAK HOEJI
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• v.41 no.3
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• pp.359-364
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• 1997

Resistance gene mphK was cloned from Escherichia coli 209K strain which is highly resistant to erythromycin (EM). By using the cloned plasmid pGE64, E. coli NM522 was transformed. The comparison of macrolide-phosphotransferase K [MPH(K)] activity between E. coli 209K and E. coli NM522(pGE64) showed that the total enzyme activity of MN522(pGE64) was fifty-fole higher than that of 209K. To identify characteristics of MPH(K) more precisely. MPH(K) was isolated and purified from the NM522 (pGE64). The final purification f MPH(K) through several stages of purification process was 89 fole and the overall recovery was 11%. This enzyme was monomer with the molecular weight of 34 kDa and its isoelectric point (pI) was 5.0. The optimal pH and temperature for activity were 8.0 and $40^{\circ}C$, respectively.

• Korean Journal of Materials Research
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• v.15 no.2
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• pp.112-114
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• 2005

Dispersion stability of the $Sm_xCe_{1-x}O_{2-2/x}$ nanoparticles, which was produced by hydrothermal process, was studied in aqueous suspension using ESA (Eletrokinetic Sonic Amplitude). The average particle size of the synthesized $Sm_xCe_{1-x}O_{2-2/x}$ at nanoparticles was about $5{\pm}2nm$. The dispersion and rheological behavior of the $Sm_xCe_{1-x}O_{2-2/x}$ nanoparticles aqueous suspension was investigated using $NH_4OH\;and\;HNO_3$ as a disperse agent. The colloidal stability of aqueous suspensions with $Sm_xCe_{1-x}O_{2-2/x}$ nanoparticles at different pH values has been investigated by means of zeta potential, average particle size, and the distribution of synthesized $Sm_xCe_{1-x}O_{2-2/x}$ nanoparticles. The isoelectric point of the $Sm_xCe_{1-x}O_{2-2/x}$ nanoparticles was at pH around 11 and the value of zeta potential was at its maximum near pH 6.5.

• Bulletin of the Korean Chemical Society
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• v.32 no.8
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• pp.2611-2616
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• 2011

We studied the physical properties of the mercaptopyruvic-acid layer formed on gold surfaces, which has the interactions with the titanium dioxide surface for design of gold- titanium dioxide distribution. Surface force measurements were performed, using the atomic force microscope (AFM), between the surfaces as a function of the salt concentration and pH value. The forces were analyzed with the DLVO (Derjaguin-Landau-Verwey-Overbeek) theory, to evaluate the potential and charge density of the surfaces quantitatively for each salt concentration and each pH value. The difference in the properties reflected the effect of the isoelectric point on the surface forces. The forces were interpreted for the evaluation with the law of mass action and the ionizable groups on the surface. The salt concentration dependence of the surface properties, found from the measurement at pH 8.0, was consistent with the prediction from the law. It was found that the mercaptopyruvic-acid layer had higher values for the surface charge densities and potentials than the titanium dioxide surfaces at pH 8, which may be attributed to the ionized-functional-groups of the mercaptopyruvic-acid layer.

• Journal of the Korean Home Economics Association
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• v.28 no.2
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• pp.37-45
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• 1990

The purpose of this study was to determine the foaming properties of two small red bean protein isolates at various conditions. Data concerning the effects of pH, temperature, MaCl concentration, sugar concentration and protein concentration on the properties such as solubility, foam expansion, foam stability were presented. The results were summarized as follows : 1. The crude protein contents of two small red beans were 26.14% and 22.71%. The percentage of nonpolar amino acid group was the highest and that of sulfur containing amino acid group was the lowest. 2. Protein solubility showed the minimum at pH 4.5 which is isoelectric point of small red bean protein isolate adn heat treatment lowered solubility(P<0.05). At pH 4.5, solubility increased sighificantly as 0.4M NaCl was added. However, the effect of sugar concentration in the solubility was not significant. 3. Foam expansion of two small red bean protein isolates was high at pH 4.5 and heat treatment at 10$0^{\circ}C$ lowered foam expansion(P<0.05). While addition of NaCl, sugar did not affect the foma expansion, gradual increment of the protein isolates concentration up to 9% decreased the foma expansion slightly. 4. Foam stability was significantly high at pH 4.5 and heat treatment at 10$0^{\circ}C$ lowered foam stability. Addition of sugar caused slight decrease in foam stability. From 1% to 9% suspension, foma stability increased significantly as protein concentration increased(P<0.05)

• BMB Reports
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• v.31 no.5
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• pp.484-491
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• 1998

Acetylation of lysine residues within the aminoterminal domains of the core histones plays a critical role in chromatin assemhly as well as in regulation of gene expression. To study the biochemical function of histone acetylation, we have cloned a cDNA encoding the catalytic subunit of human histone acetyltransferase, Hat1. Analysis of the predicted amino acid sequence of human Hat1 revealed an open reading frame of 419 amino acids with a calculated molecular mass of 49.5 kDa and an isoelectric point of 5.5. The amino acid sequence of human Hat1 is homologous to those of known and putative Hat1 proteins from various species throughout the entire open reading frame. The recombinant human Hat1 protein expressed in bacteria possesses histone H4 acetyltransferase activity in vitro. Both RbAp46 and RbAp48, which participate in various processes of histone metabolism, enhance the histone acetyltransferase activity of the recombinant human Hat1, indicating that they are both able to functionally interact with the human Hat1 in vitro.

• BMB Reports
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• v.51 no.6
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• pp.265-273
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• 2018

Tau protein is encoded in the microtubule-associated protein tau (MAPT) gene and contributes to the stability of microtubules in axons. Despite of its basic isoelectric point and high solubility, tau is often found in intraneuronal filamentous inclusions such as paired helical filaments (PHFs), which are the primary constituent of neurofibrillary tangles (NFTs). This pathological feature is the nosological entity termed "tauopathies" which notably include Alzheimer's disease (AD). A proteinaceous signature of all tauopathies is hyperphosphorylation of the accumulated tau, which has been extensively studied as a major pharmacological target for AD therapy. However, in addition to phosphorylation events, tau undergoes a number of diverse posttranslational modifications (PTMs) which appear to be controlled by complex crosstalk. It remains to be elucidated which of the PTMs or their combinations have pro-aggregation or anti-aggregation properties. In this review, we outline the consequences of and communications between several key PTMs of tau, such as acetylation, phosphorylation, and ubiquitination, focusing on their roles in aggregation and degradation. We place emphasis on the structure of tau protofilaments from the human AD brain, which may be good targets to modulate etiological PTMs which cause tau aggregation.

• Asian-Australasian Journal of Animal Sciences
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• v.13 no.12
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• pp.1770-1774
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• 2000

Extended use of porcine blood in food ingredients depends on the decolorization of red blood cell concentrates and the modification of its functional properties. The purpose of this study is to compare the relative effect of cation ion exchanger for decolorization of porcine red blood globin. The globin extract is freeze-dried for determination of various functional properties, such as solubility, emulsion capability and foaming ability. Since the isoelectric point of blood globin is located at pH 6.8, which is the neutral pH ranges (6-8), so its functionalities are inferior around these pHs. This weakness has been the main reason, which limit the extended use of blood globin in food industry. Acetylation and succinylation of blood globin can be an alternative way to improve its functionalities. These results may provide new information to understand the decolorization mode by cation ion exchanger for the blood globin. With chemical, the functionalities of blood globin could be obviously improved. The above findings could enable food industry to extend the use of blood globin as a food ingredient.

• Food Science of Animal Resources
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• v.30 no.4
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• pp.551-559
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• 2010

Among the food constituents, proteins differ in coagulation properties as compared to other constituents in food system. Especially milk protein coagulate through different pathways thus this coagulability can be used for manufacture of various dairy products or as a determinant of dairy product analysis. These milk coagulation methods include organic solvent, isoelectric point, trichloroacetic acid, Ca-sensitive casein, heavy metal ion and rennet coagulation. The coagulation experiment was performed using above parameters at $0^{\circ}C$ and $25^{\circ}C$ to find the dehydration conditions before coagulating for precheese powder making. After different chemical treatments, there was no coagulation at $0^{\circ}C$ rather at $25^{\circ}C$ whatever the mode of coagulation methods was. The appearance of precipitate with coagulation methods was quite different from above mentioned methods of coagulation illustrated by scanning electron microscope. These powders were used for fabrication of camembert cheese by renneting coagulation at $0^{\circ}C$, showing the possibility of cheese materials and of food additives for fabrication of products.