• Preventive Nutrition and Food Science
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• v.4 no.2
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• pp.139-144
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• 1999

Lipoprotein lipase (LPL) I san enzyme that catalyzed the hydrolysis of triacylglycerols of chylomicrons and VLDL to produce 20acylglycerols and fatty acids. The enzyme, LPL, is localized on the surface of the capillary endothelium and is widely distributed in extrahepatic tissues including heart, skeletal muscle and adipose tissue. LPL has been isolated from boving milk by affinity chromatography on heparin-separose in 2 M NaCL, 5mM barbital buffer, pH 7.4. To elucidate the lipid-binding regin, LPL was digested with trypsin and then separated by gel filtration. Lipid binding region of LPL has been investigated by recombining LPL peptides with DMPC vesicles. Proteolytic LPL fragments with DMPC were reassembled and stabilized by cholate. Lipid-binding region of LPL was identified by a PTH-automated protein sequencer, as AQQHYPVSAGYTK. The analysis of the secondary structure of the lipid-binding peptides revealed a higher probability of $\alpha$-helix structure compared to the whole LPL protein. The prediction of hydrophobicity of lipid -binding region was highly hydrophobic (-1.1) compared to LPL polypetide(-0.4).

• Membrane Journal
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• v.6 no.1
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• pp.10-21
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• 1996

This study is undertaken to investigate the major factor which causes a fouling phenomenon in membrane separation system and effect of hydrophilic treatment on fouling repression of hydrophobic polymer (polysulfone, PSf). Chlorosulfonic acid (CSA) and sulfuric acid as a sulfonating agents are used to produce sulfonated PSf (SPSf). SPSf membrane is prepared under several conditions to investigate it's separation process. The extent of fouling-repression is measured by membrane filtration index (MFI) value. With increasing the ion exchange capacity (I.E.C), the flux of SPSf membrane is decreased but the rejection is increased and the flux is less reduced. According to the MFI value, the SPSf membrane has a fouling-retardant effect.

• Korean Journal of Microbiology
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• v.26 no.1
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• pp.52-59
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• 1988

A partially purified preparation of L-galactonolactone oxidase which catalyzes the last step of L-ascorbic acid biosynthesis was obtained from Saccharomyces cerevisiae ATCc 26787. The purification procedures included Triton X-100 treatment, protamine sulfate precipitation, ammonium sulfate precipitation, DEAE-Sepharose CL-6B ion exchange chromatography, Sephadex G-150 gel filtration chromatography, and Phenyl-Sepharose CL-4B hydrophobic interaction chromatography. The optimum temperature for the enzyme activity was about $34^{\circ}C$ and the optimum pH was 6.8-7.0. The substrate specificity was confined to L-aldonolactones, L-galactono-1,4-lactone and L-gulono-1,4-lactone. An apparent Km value of 0.294mM with L-galactono-1,4-lactone as a substrate was found. By comparing the substrate specificities of this enzyme with those of isofunctional enzymes of higher plants and animals, it becomes evident that the enzyme of S. cerevisiae ATCC 26787 is rather similar to the L-gulonolactone oxidase of animals than the galactonolactone dehydrogenase of higher plants.

• Journal of Microbiology and Biotechnology
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• v.7 no.6
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• pp.386-390
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• 1997

A xylanase from the Bacillus sp. strain DSNC 101, isolated from soil, was purified to homogeneity by anion-exchange and hydrophobic interaction chromatography followed by gel filtration chromatography. The enzyme cleaved xylan, but not carboxymethyl cellulose, Avicel, soluble starch, and pNPX. The main product of oat spelts xylan hydrolysates was xylobiose. The xylanase had a molecular weight of 25 kDa determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Optimum temperature and pH for the xylanase activity were $50^{\circ}C$ and 6.0, respectively. $K_{m}\;and\;V_{max}$ of the enzyme for oat spelts xylan were 12.5 mg of xylan/ml and 869.5 unit/mg of protein, respectively. Xylanase was completely inhibited by Hg, Cu, and N-bromosuccinimide, but was stimulated by Ca, Co, and Mg.

• Journal of Korean Society of Environmental Engineers
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• v.37 no.3
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• pp.152-158
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• 2015

This paper investigated the membrane fouling potential at the state of passive adsorption which is no permeation with the test modules on COD (Chemical oxygen demand) loading rates, examined the recovery rate and resistance on membrane fouling by three cleaning manners of hydrophobic membrane in a bioreactor. The results showed that high COD loading led to the increase of extra-cellular polymeric substances and filtration resistance. The permeability resistance from 1st day to 63rd day was getting increased, however, the value of permeability resistance after 63th day during the operation period was almost same level at three COD loading rates, it was due that the biomass adhesion on membrane surface at the state of passive adsorption reached to the critical state. Also, the final recovery rates after three cleaning manners were 78%, 72% and 69% at the COD loading concentrations of 250 mg/L, 500 mg/L and 750 mg/L respectively, and then recovery rate by physical cleaning at Run 2 and Run 3 was decreased after 40th day, it proved that biomass cake, which is not easily removed, was formed on the membrane surface because of high COD loading rate and EPS concentration.

• Journal of Korean Society of Environmental Engineers
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• v.36 no.7
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• pp.492-497
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• 2014

This study investigated removal characteristics of organic matters in pretreatment and reverse osmosis (RO) membrane processes for seawater desalination. Also, the influence of the changes in characteristics of organic matters on the membrane fouling was assessed. The pretreatment processes included dual media filtration (DMF), pressurized membrane filtration (MF), and submerged membrane filtration (SMF). Turbidity, UV absorption at 254 nm, dissolved organic carbon, size exclusion chromatography (SEC), fluorescence excitation emission matrix (FEEM), and transparent exopolymer particles (TEP) in raw and processed waters were analyzed. Ions and minerals were not removed by any pretreatment process tested, but were removed over 99% through the RO membrane process. Hydrophobic organics, which can play major role in organic membrane fouling, were relatively readily removed compared with hydrophilic ones. Membrane based pretreatment such as MF and SMF exhibited better removals of organics than conventional DMF. As the levels of organics in pretreated water decreased, the silt density index (SDI) decreased. MF treated water exhibited the lowest SDI value; this is possibly due to the lowest TEP ($0.1-0.4{\mu}m$) concentrations.

• Korean Chemical Engineering Research
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• v.46 no.3
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• pp.639-645
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• 2008

The objectives of this research are to (1) observe changes in particle size distribution due to formation of microflocs during coagulation process (2) identify the membrane fouling potential on cross flow system (3) investigate the mechanism of membrane fouling. The rate of flux decline for the hydrophobic membrane was significantly greater than for the hydrophilic membrane, regardless of pretreatment conditions. The pretreatment of the raw water significantly reduced the fouling of the UF membrane. Also, the rate of flux decline for the hydrophobic membrane was considerably greater than for the hydrophilic membrane. Applying coagulation process before membrane filtration showed not only reducing membrane fouling, but also improving the removal of dissolved organic materials that might otherwise not be removed by the membrane. That is, during the mixing period, substantial changes in particle size distribution occurred under rapid and slow mixing condition due to the simultaneous formation of microflocs and NOM precipitates. Therefore, combined pretreatment using coagulation not only improved dissolved organics removal efficiency but also flux recovery efficiency.

• Journal of Microbiology and Biotechnology
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• v.9 no.6
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• pp.832-838
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• 1999

Two different types of lipases (lipase I and lipase II) secreted into culture medium by Rhizopus sp. L-I were purified using a hydrophobic chromatography and were partially characterized. Both enzymes were monomeric as revealed by SDS-PAGE and gel filtration. The molecular masses of the enzymes were identified as 45 kDa (lipase I) and 69 kDa (lipase II). The isoelectric points were estimated to be 3.6 and 5.2 for lipase I and lipase II, respectively. pH and temperature activity optima for lipase I were as 7.5 and $50^{\circ}C$, respectively, whereas the corresponding parameters for lipase II were 6.0 and $45^{\circ}C$. The amino terminal sequences of lipase I and lipase II, determined by Edman degradation, were found to be Leu-Val-Met-Ile-Gln-Arg and Leu-Val-Met-Lys-Gln-Arg, respectively. By western blotting analysis, the two lipases were found to have a common antigenic determinant. Immuno-electron cytochemistry conducted with polyclonal anti-lipase I antibody indicated the enzyme located in both the periplasm and the adjacent vesicles of fungal hyphae. Fortunately, the sites on the cell envelope where lipase was exported into the culture medium was also identified.

• Korean Journal of Microbiology
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• v.44 no.2
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• pp.116-121
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• 2008

In my search of microbial source of novel enzymes, a marine actinomycetes, A1460, producing haloperoxidase was isolated from macroalgae from south sea, Korea and studied for physiological and biochemical properties. The haloperoxidation reaction was followed by the bromination of phenol red in the presence of hydrogen peroxide and potassium bromide. The haloperoxidase was partially purified from the cell extract with $35\sim75%$ ammonium sulfate precipitation, High-Q anion exchange chromatography, gel filtration chromatography, hydroxyapetite chromatography and hydrophobic interaction chromatography to a yield of 42% and purification fold of 70. This enzyme showed relatively high heat stability without losing 50% of activity after 1 hr incubation at $60^{\circ}C$. The highest activity was found at $45^{\circ}C$, and the optimal pH was about pH 7, but higher stability was observed at pH 8. Azide and cyanide ion showed strong inhibition at less than 1 $\mu M$ level suggesting that the enzyme was Fe ion dependent haloperoxidase.

• Preventive Nutrition and Food Science
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• v.1 no.1
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• pp.87-92
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• 1996

This study describes a stable and simple method for the measurement of cholesteryl ester transfer protein(CETP) activities using reconstituted HDL and LDL as substrates. Apolipoproteins (apo) A-I and -B were purified from hog plasma by a new strategy without ultracentrifugation and delipidation. a simple two-step column chromatography was administered. In the first step of phenyl-sepharose CL-4B column chro-matography, hydrophobic plasma proteins were isolated. The most hydrophobic proteins bound to the column appeared to be A-I and apo-B. Contaminat proteins were efficiently eliminated from the sample by washing the column with 0.3M NaCI containing buffer after loading the plasma on the column. Two pure proteins showing each single band on SDS-PSGE of apo A-I and apo-B were individually obtained by a subsequent gel filtration column chromatography(Sephadex G-200). This two-step purification was simple and inexpensive compared to the ultracentrifugation and/or delipidation method that are most commonly used. Reconstituted hight-density lipoproteins(HDL) and low-density lipoproteins(LDL) were prepared using the purified apo A-I and-B, respectively. When these artificially prepared HDL and LDL were used in the assays for CETP as the cholesteryl ester(CE) donor and acceptor respectively, the specific transfer of CE increased up to two fold compared to that used the native HSL and LDL.