• Current Research on Agriculture and Life Sciences
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• v.17
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• pp.45-52
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• 1999

This study was conducted to evaluate the effects of microbial inoculation on sewage sludge composting. The number and species of microorganisms in sewage sludge sampled on February were higher than those sampled on August. The composting of sewage sludge is inhibited by the polyacrylamide cation, which was used as a coagulant and known to repress the growth of microorganisms. The growth of all microorganisms was inhibited by the addition of the polyacrylamide cation at a concentration of more than 0.8%. The species and viable counts of microorganisms were observed to increase during composting sewage sludge by inoculation of the effective microorganisms and addition of the pine tree sawdust as a bulking agent, compared with those without inoculation. A variety of organisms in compost(sewage sludge plus sawdust) were observed after composting for 30 days, such as Fragilaria sp., Proales sp., Vorticella sp., Schizothrix sp., Anabaena sp., Zoothaminium sp., Epstylis sp., Arcella sp., Balantidium sp., Actinophrys sp., Synedra sp., Euglypha sp., Ulothrix sp., Anacystis sp., and Clostium sp.

• Journal of Environmental Health Sciences
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• v.24 no.2
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• pp.104-109
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• 1998

The objective of this study was to examine the effect of polymer coating on the initial microorganism attachment and the biofilm growth. Such as nonion(polyacrylamine), anion(CMC-Na) and cation polymer coagulant(chitosan and PEI) were used for coating material of the support carrier(acryl plate). When polymer coagulant was coated with 5, 10, 20, 35, 50, 100 and 200 mg/l on the surface of acryl plate, initial microorganism attachment increased and optimum concentration for the attachment was 35 mg/l. Biofilm growth experiments were conducted with the substrate loading of 12.7gSCOD/$m^2\cdot$ day using RBC. The polymer coagulants such as CMC-Na, polyacrylamide, PEI and chitosan coating on the acryl plate facilitated the biofilm growth of microorganisms. Until the biofilm dry weight grows up to 0. 0038g/cm$^2$, biofilm growth on the plate coated with cation polymer like chitosan was better than that on the coated plate of nonion(polyacrylamine), anion(CMC-Na) polymer coagulant.

• Journal of Plant Biology
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• v.33 no.4
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• pp.293-301
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• 1990

We have purified and characterized a deoxyribonuclease from zygotes of the eukaryotic green alga, Chlamydomonas reinhardtii and investigated effects of the polyamines, putrescine, spermidine and spermine on the purifed endonuclease-catalyzed cleavage of plasmid DNA. The enzyme has a molecular weight of about 37 kDa as measured by gel filtration and SDS-polyacrylamide gel electrophoresis. There is no requirement for a divalent cation. The activity is sensitive to ionic strength, as NaCl and KCl result in inhibition. The cleavage of plasmid DNA by the purified endonuclease was effectively inhibited by polyamines. The enzyme activity was inhibited more effectively by spermine than by spermidine. The inhibition by putrescine was lower than the other two polyamines.

• Journal of Bio-Environment Control
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• v.14 no.3
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• pp.196-202
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• 2005

This research was conducted to determine the amount of water absorbed by a polyacrylamide hydrogel such as Stocksorb C (STSB), effect of salts on inhibition in hydration of STSB, and the hydrogel effects on changes of nutrient concentration in external solution. Absorption of deionized water by STSB reached a maximum of 180 $mL{\cdot}g^{-1}$. Monovalent soluble salts such as $KH_2PO_4,\;KNO_3$, and $(NH_4)_2SO_4$ reduced absorption of the hydrogel, but the degrees of inhibition in absorption were similar in three kinds of salts. Twenty milliequivalents per liter of $Ca_{2+}\;or\;Mg_{2+}$ reduced water absorption of STSB to $14\%$ compared to those of deionized water. Solution absorption was consistently lower in the presence of divalent cations than in the presence of the monovalent cations. But the absorption was unaffected by the uncharged salt such as urea in all concentrations tested. The final $K^+\;and\;NH_4^+-N$ concentrations of the solution remaining after absorption by STSB was higher than those of the initial solution. The soaking of STSB to full strength of Hoagland solution resulted in increase of $NO_3^--N,\;H_2PO_4^-\;and\;SO_4^{2-}$ concentrations in external solution compared to initial solution, reaching 5,300, 250 and 1,500 $mL{\cdot}g^{-1}$, respectively, at 24 hrs after soaking.

• The Korean Journal of Zoology
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• v.22 no.4
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• pp.141-152
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• 1979

Feline leukemia virus DNA polymerase was purified by ion-exchange and nucleic acid affinity chromatographies. The enzyme consists of a single polypeptide chain of approximately 72, 000 molecular weight as determined by both of a glycerol density gradient centrifugation and SDS-polyacrylamide gel electrophoresis. The preferred divalent cation for DNA synthesis is $Mn^2+$ on a variety of template-primers, and its optimum concentration appears to be significantly lower than reported results of other mammalian type-C viral enzymes. The divalent cation requirement for maximum activity of RNase H is similar to those of DNA polymerase. Both DNA polymerase and RNase H activities appear to reside on the same molecule as demonstrated by the copurification of both activities through various purification steps. An additional RNase H without detectible polymerase activity was generated by a limited chymotrypsin digestion. This RNase H activity was inhibited equally effectively as RNase H in the intact reverse transcriptase by antisera prepared against reverse transcriptase of feline leukemia virus. Neutralization and binding test showed that antibody binding to reverse transcriptase molecule did not completely inhibit the polymerase activity.

• Applied Biological Chemistry
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• v.46 no.3
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• pp.176-182
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• 2003

An alkaline fibrinolytic protease-producing bacteria was isolated front Korean traditional soy sauce and identified as Bacillus subtilis K7 from the results of analyses of its morphological and physiological properties, $API^{\circledR}$, and Biolog system. The enzyme was purified by 75% ammonium sulfate fractionation, QAE-Sephadex anion and SP-Sephadex cation exchange column chromatography and Sephadex G-100 gel filtration. The specific activity of the purified enByme was 233.9 unit/mg protein and the yield of enzyme was 3.8%. The homogeneity of the purified enzyme was confirmed by polyacrylamide gel electrophoresis. Molecular mass of the enzyme was estimated about 21,500 Da by SDS-polyacrylamide get electrophoresis and gel chromatography. The optimum temperature and pH for the enzyme activity were $40^{\circ}C$ and 9.0, respectively. The enzyme was stable in a pH range of 5.0 to 12.0, and 60% of its activity was lost on heat treatment at $50^{\circ}C$ for 20 min. The activity of the purified enzyme was inhibited by the presence of $Fe^{2+},\;Ag^{2+},\;Cu6{2+}$, iodoacetate, ethylene diamine tetraacetic acid (EDTA), and trans-1,2-diaminocycloheane-N,N,N',N'-tetraacetic acid (CDTA). The results indicates that the enzyme requires a metal ion for its enzymatic activity.

• Journal of the Korea Institute of Building Construction
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• v.2 no.3
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• pp.131-138
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• 2002

The objective of the study is to examine the characteristic correlations between reinforcing carbon fiber and interfacial adhesion agent since the interfacial adhesion strength between reinforcing carbon fiber and matrices is believed to be an essential element influencing the physical properties in carbon fiber reinforced cement composite using slurry method. The integrity of interfacial adhesion between reinforcing fiber and cement not only affects the quality of fiber reinforced cement composite but also influences to a large degree the physical properties of the cement composite when producing carbon fiber reinforced cement composite using slurry method. Having analyzed the physical properties 1.e., water content, tensile strength, flexural strength and flexural toughness of carbon fiber reinforced cement composite specimens, C-PAM(cation polyacrylamide) was determined to be an optimum interfacial adhesion agent. The study has also demonstrated that interfacial adhesion strength varies largely on the content and type of the reinforcing fiber. Judging from magnified view of the tensile shear cross-section using VMS(video microscope system), interfacial adhesion strength between reinforcing fiber and matrices is affected by the type of interfacial adhesion agent. According to the result of the experiments, C-PAM was determined to be an ideal interfacial adhesion agent when using carbon fiber in producing carbon fiber reinforced cement composite with the optimum content of carbon fiber being established.

• Preventive Nutrition and Food Science
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• v.7 no.1
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• pp.43-47
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• 2002

Crude caseinomacropeptide (CMP) was prepared from Na-caseinate using a commercial renneting enzyme. Most of the crude CMP was released from the Na-caseinate by hydrolyzing with the enzyme for 40 min. The hydrolysis of the k-casein with carbohydrate was slower than that of the k-casein without carbohydrate, as shown by the analyses of the sialic acid content and the tricine-SDS-polyacrylamide gel electrophoresis. The yield of crude CMP from Na-caseinate was 3.7%. Cation exchange chromatography showed that the crude CMP consisted of 40.5% CMP and 59.5% caseinogylcomacropetide (CGP). The effect of the TCA concentration on the solubility of CMP and CGP was determined by using crude CMP. The amounts of crude CMP and sialic acid decreased in the proportion to the increase of trichloroacetic acid (TCA) concentration from 2 to 12%, suggesting that the CGP containing carbohydrate, as well as the CMP having no carbohydrate, was precipitated in a range of 4 to 12%, depending on the TCA concentration. This result supports the hypothesis that the different non-glycosylated and glycosylated forms of CMP have different sensitivities to TCA precipitation.

• Bulletin of the Korean Chemical Society
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• v.15 no.9
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• pp.719-724
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• 1994

Major cellulase components, such as three endoglucanases (endoglucanases I, II, and III) and one exoglucanase (exoglucanase II), were isolated from a commercial cellulase (Meicelase TP 60) derived from the fungus Trichoderma viride by a series of chromatography procedures. These procedures were the gel filtration on Bio-Gel, the anion exchange on DEAE-Bio-Gel A, the cation exchange on SP-Sephadex C50, and the affinity chromatography on Avicel cellulose. The average molecular weights determined by SDS-polyacrylamide gel electrophoretic analysis were 51,000, 59,000, 41,000 and 62,000 Da for endoglucanases I, II and III and exoglucanase II, respectively. The extinction coefficients, ${\varepsilon}^{1%}$ 280 nm, of these enzymes were 11.7, 3.3, 7.2 and 11.3, respectively. Among them, the endoglucanase II showed the very low value of the coefficient compared with the others. On the other hand, it was found that endoglucanase II and III were of more random hydrolytic mode on carboxymethylcellulose as compared with those of endoglucanase I and exoglucanase II. Especially, endoglucanase I showed less random action than that of exoglucanase II. In the hydrolysis of insoluble cellulose by the enzyme components, cellobiose was the major product, but glucose was the major product by endoglucanase III.

• Korean Journal of Veterinary Research
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• v.36 no.2
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• pp.379-387
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• 1996

The objects of the present study were to establish the method of purification, subunit dissociation of verotoxin-2 (VT2) produced by Escherichia coli O157:H7, and to investigate the characteristics of purified verotoxin-2 such as molecular weight and composition of amino acid. The results were summerized as follows; Verotoxin-2 was extracted by addition of polymyxin B sulfate into bacterial cell lysate prepared from Escherichia coli O157:H7(KSC109). As an initial step, the bacterial cell lysate was precipitated with 30% saturated ammonium sulfate. The precipitated crude toxin was then subjected to anion-exchange, chromatofocusing and cation-exchange chromatography. Using this scheme, we obtained highly purified toxin with a specific activity of $1.1{\times}10^9$ $CD_{50}/mg$. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-PAGE) for purified VT2 showed two protein bands. The upper band, approximately 32 Kd, was supposed as A subunit and the lower band, approximately 7.7 Kd, was supposed as B subunit. When the toxin was separated in the subunit-dissociating solution, two peaks emerged with retention times of 15 and 28 min by HPLC. These peaks represented A subunit and B subunit, respectively. The amino acid composition of purified VT2 were made up in order of glutamic acid, histamine, asparaginic acid, histidine, lysine, alanine and leucine etc. The largest amount among the amino acid composing VT2 was methionine.