• Membrane and Water Treatment
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• v.11 no.3
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• pp.201-206
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• 2020

Electrodialysis (ED) is used in wastewater treatment, during the processing and recovery of beneficial materials, to produce usable water. In this study, sulfate and chlorine ions, which are the anions majorly used for electroplating, were studied as factors affecting the recovery of copper, nickel and water from wastewater by electrodialysis. Although the removal rates of copper and nickel ions were slightly higher with the use of chlorine ions than of sulfate ions, the removal efficiencies were above 99.9% under all experimental conditions. The metal ions of the plating wastewater flowed through the ion exchange membrane of the diluate tank and the concentrate tank while all the water moved together due to electro-osmosis. The migration of water from the diluate tank to the concentrate tank was higher in the presence of a monovalent chloride ion compared to that of a divalent sulfate ion. When sulfate was the anion used, the recoveries of copper and nickel increased by about 25% and 30%, respectively, as compared to the chloride ion. Therefore, when divalent ions such as sulfate are present in the electrodialysis, it is possible to reduce the movement amount of water and highly concentrate the copper and nickel in the plating wastewater.

• Biotechnology and Bioprocess Engineering:BBE
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• v.10 no.3
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• pp.280-283
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• 2005

The adsorption of a model protein bovine serum albumin (BSA) in expanded bed chromatography was undertaken by exploiting a commercially available expanded bed column (20 mm i.d.) from UpFront Chromatography and Streamline DEAE $(\rho=1.2g/cm^3)$ from Amersham Pharmacia Biotechnology. The influence of whole yeast cells on the adsorption capacity of column was explored by employing yeast cells in a concentration ranged of 0 to $15\%(w/v)$. Equilibrium isotherms for adsorption of BSA on Streamline DEAE were correlated by using Langmuir equation. The presence of yeast cells resulted in decreased of BSA binding capacity in both batch binding and expanded bed chromatography. Results indicated that the yeast cells act as competitor for proteins to bind to the sites on adsorbents.

• International Journal of Industrial Entomology and Biomaterials
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• v.2 no.1
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• pp.55-59
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• 2001

The vitellin of the red flour beetled Tribolium castaneum Herbst was purified and characterized. The vitellin of T. castaneum was purified by the FPLC techniques, anion exchange chromatography and gel permeation chromatography. In native-polyacrylamide gel electrophoresis, vitellin of T. castaneum was detected as a single band. This native vitellin has molecular weight of 440 kDa. The vitellin of T. castaneum is composed of three polypeptides, designated Vnl (178 kDa), Vn2 (168 kDa) and Vn3 (52 kDa) in SDS-polyacrylamide gel electrophoresis. Three subunits of vitellin were presented in the female adult hemolymph and egg extracts, but not observed in the male. These three polypeptides gradually decreased during embryogenesis. Polyclonal antiserum raised against purified vitellin reacted with the three polypeptides, Vnl, Vn2 and Vn3. Antisera raised against Vn1 and Vn2 cross-reacted with the two large subunits, Vnl and Vn2, respectively. Another subunits Vn3, however, was not cross-reacted with these two antisera. Also, antiserum raised against Vn3 did not cross-react with the Vn1 and Vn2.

• Parasites, Hosts and Diseases
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• v.39 no.2
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• pp.119-132
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• 2001

An immunoelectron microscopy employing immunogold labeling method was performed to detect tissue origin of Dl fraction (DIA) among 5 antigenic protein fractions partially purified by DEAE- anion exchange chromatography from water- soluble crude antigen (PIWA) of adult Paragonimus iloktsuenensis. Immune reactions of adult worm tissues with rabbit serum immunoglobulin immunized with crude antigen (PI-Ig) and D1 antigen (D1-Ig), as well as rat serum immunoglobulin infected with P. iloktsuenensis were observed. DlA showed strong antigenicity in the intestinal epithelium of the worms during the early infection period of 2-4 weeks after infection. The vitellaria also showed stronger antigenicity than the other tissue sites in immune reaction of tissues against all immunoglobulins from 4 to 33 weeks after vitelline development. Therefore, it is suggested that DlA was mainly originated from the intestinal epithelial tissues before the development of vitelline gland of the parasites. Immune-reactivity of two immunoglobulins (PI-Ig, Dl-Ig) was significantly different in intestinal epithelial cytoplasmic protrusions (CP) and intestinal epithelial secretory granules (SG). In the experimental group with Dl-Ig, gold particles were labeled significantly in CP than in SG when compared to the PI-Ig group. Thus, the major antigenic materials in Dl antigen having a strong antigenicity in the early infection period was considered to be originated from the intestinal epithelial tissue .

• Parasites, Hosts and Diseases
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• v.38 no.2
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• pp.95-97
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• 2000

A 17 kDa protein from Clonorchis sinensis adults was purified by a procedure including Sephacryl S-200 HR gel filtration and Q-Sepharose anion exchange chromatography. The protein was proved to be a cysteine protease as it showed hydrolytic activity toward Cbz-Phe-Arg-AMC in the presence of dithiothreitol and was inhibited by specific inhibitors such as iodoacetic acid or trans epoxy-succinly-L-leucyl-amido(4 guanidino) butane. The polyclonal antibody raised against the protein reacted to 17 kDa proteins of trematodes such as Paragonimuf westermani, Fasciola hepatica, Opisthorchis viverrini, Gymnophalloides seoi, and Metagonimus yokogawai. The antibody recognized the 17 kDa and 16 kDa cysteine proteases purified from C. sinensis, P. westemani, and G. seoi as well. These results suggest that the 17 kDa protein may be a cysteine protease commonly present in trematodes.

• BMB Reports
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• v.32 no.6
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• pp.541-546
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• 1999

When we compared the chitinase activity of various plant sources using colorimetric or active gel-staining assay methods, the specific activity of pumpkin leaves was the highest among the samples we analyzed. The highly active chitinase from pumpkin leaves (designated PL-ChtIII) was purified to homogeneity using affinity chitin gel and HPLC Mono-Q anion-exchange cloumn chromatographies. In contrast to other members of the class III chitinase family, PL-ChtIII showed a strong binding affinity to the regenerated chitin gel column. The apparent molecular weight of PL-ChtIII was estimated to be 29 kDa on SDS-PAGE gel, while its optimum pH and temperature were shown to be pH 6.0 and $60^{\circ}C$, respectively. Analyzing the reaction products of PL-ChtIII with swollen chitin as substrate, the dimer and tetramer of N-acetylglucosamine were produced as major products in the first hour of the enzymatic reaction along with a small amount of monomers and trimers. As the reaction time increased, dimeric N-acetylglucosamine became the predominant form of reaction product.

• BMB Reports
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• v.32 no.6
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• pp.579-584
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• 1999

Mantis egg fibrolase (MEF-3) was purified from the egg cases of Tenodera sinensis using ammonium sulfate fractionation, gel filtration on Bio-Gel P-60, DEAE Affi-Gel blue gel affinity chromatogragphy, and MONO-Q anion-exchange chromatography. This protease had a molecular weight of 35,600 Da as determined by SDS-polyacrylamide gel electrophoresis under reducing conditions and its isoelectric point was 6.0. The N-terminal amino acids sequence was Ala-Thr-Gln-Asp-Asp-Ala-Pro-Pro-Gly-Leu-Ala-Arg-Arg. This sequence was 80% homologous to the serine protease from Tritirachium album. MEF-3 readily digested the ${\alpha}$-and ${\beta}$-chains of fibrinogen and more slowly the ${\gamma}$-chains. It showed strong proteolytic and fibrinolytic activities. Phenylmethanesulfonyl fluoride and chymostatin inhibited its proteolytic activity, while EDTA, EGTA, cysteine, ${\beta}$-mercaptoethanol, elastinal, tosyl-lysine chloromethylketone, and tosyl-amido-2-phenylethyl chloromethyl ketone did not affect its proteolytic activity. Among the chromogenic protease substrates, the most sensitive one to the hydrolysis of MEF-3 was benzoyl-Phe-Val-Arg-p-nitroanilide. Based on these experimental results, we speculated that MEF-3 is a serine protease with a strong fibrin(ogen)olytic activity.

• Analytical Science and Technology
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• v.10 no.5
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• pp.307-314
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• 1997

Inductively coupled plasma atomic emission spectrometry(ICP/AES) was used for the determination of uranium and thorium in geological materials. Samples were predecomposed by mixed acid digestion technique. The separation of the uranium and thorium was achieved by systematic solvent extraction with TTA(thenoyltrifluoroacetone) and TOA (tri-n-octylamine) and back extraction into HCl. The results for standard rock sample, NIST SRM 278, showed a good agreement with those certified from NIST as well as found values by other non-destructive techniques. Additional purification for extracted portions was carried out by anion exchange chromatography for measurement of several natural radioisotopes of uranium and thorium by alpha spectrometry.

• Korean Journal of Environmental Biology
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• v.21 no.4
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• pp.358-365
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• 2003

A bacterial strain capable of producing a novel bioflocculant was isolated from a biofilm sample and identified as Bacillus megaterium G31. The highest biopolymer yield was achieved when the organism was cultivated in a medium containing acetate as the sole carbon source and ($NH_4)_2HPO_4$as the nitrogen source. In kaolin suspension, the flocculating activity was highest at 170 mg I$^{-1}$ and decreased at the higher bioflocculant concentrations. The crude bioflocculant produced by the organism was purified by ethanol precipitation and gel permeation chromatography. The FTIR spectrum of the purified bioflocculant revealed that the bioflocculant might be a heterogeneous polysaccharide composed of hexosamines and neutral sugars. The analysis of sugar components of the bioflocculant using high performance anion-exchange chromatography showed that the sugar constituents of the bioflocculant were glucosamine, fucose, galactosamine, galactose, glucose, mannose in approximate molar ratio of 4 : 1 : 6 : 3 : 8 : 19. Its flocculating activity was stimulated by various cations. The bioflocculant was thermo-stable and retained 64% of its original activity after heating at $100^{\circ}C$ for 50 min.

• Food Science and Biotechnology
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• v.18 no.4
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• pp.872-877
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• 2009

By-products of marine organisms including salmon, skate, flatfish, and yellow goosefish were investigated to search for new source of chondroitin sulfate (CS). Agarose gel electrophoresis with chondroitinase depolymerization showed that purified chondroitin sulfate did not contain any other glycosaminoglycans. 1H-nuclear magnetic resonance (NMR) spectra were acquired to confirm the structure and purity. The average molecular weight ranging from 22 to 64 kDa was determined by high performance size exclusion chromatography. Disaccharide compositions and purities were determined by strong anion exchange-high performance liquid chromatography (SAX-HPLC) after chondroitinase ABC depolymerization. SAX-HPLC data exhibited that the purity was from $81.7{\pm}1.3$ to $114.2{\pm}2.5%$ and the yield was from 1.3 to 12.5%. All analytical results indicate that salmon cartilage, skate cartilage, and yellow goosefish bone could be promising sources of CS to substitute shark cartilage CS in commercial neutraceuticals.