• 한국생물공학회:학술대회논문집
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• 2003.04a
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• pp.334-338
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• 2003

In this study, We evaluated the removal efficiency of natural organic matters(NOM) in the Ultrafiltration(UF) and Nanofiltration(NF) membranes with molecular weight cutoff of 2500(GH), 8000(GM) and 250(HL), respectively. Filtration type was cross-flow filtration. The investigation result about raw water structure was hydrophobic 28%, hydrophilic 53% and transphilic 19%, in conjunction with XAD8/4 resin fractionation method. We were compared with UF(GM, GH) and NF(HL), in operation characteristic. In spite of poor MWCO, GM(8000Da) was superior than GH(2500Da), in the efficiency of total operation. It was showed the NF(HL) 80%, UF(GM) 50%, in the removing efficiency of HAAFP.

• Journal of Microbiology and Biotechnology
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• v.24 no.2
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• pp.245-253
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• 2014

A fibrinolytic enzyme was produced by an edible mushroom of Pleurotus ostreatus using submerged culture fermentation. The enzyme was purified from the culture supernatant by applying a combination of freeze-thaw treatment, ammonium sulfate precipitation, hydrophobic interaction, and gel filtration chromatographies. The enzyme was purified by a 147-fold, with a yield of 7.54%. The molecular masses of the enzyme an determined by gel filtration and SDS-PAGE were 13.6 and 18.2 kDa, respectively. The isoelectric point of the enzyme was 8.52. It hydrolyzed fibrinogen by cleaving the ${\alpha}$ and ${\beta}$ chains of fibrinogen followed by the ${\gamma}$ chains, and also activated plasminogen into plasmin. The enzyme was optimally active at $45^{\circ}C$ and pH 7.4. The enzyme activity was completely inhibited by EDTA, whereas protease inhibitors of TPCK, SBTI, PMSF, aprotinin and pepstatin showed no inhibition on its activity. The partial amino acid sequences of the enzyme as determined by Q-TOF2 were ATFVGCSATR, GGTLIHESSHFTR, and YTTWFGTFVTSR. These sequences showed a high degree of homology with those of metallo-endopeptidases from P. ostreatus and Armillaria mellea. The purified enzyme can also be applied as a natural agent for oral fibrinolytic therapy or prevention of thrombosis.

• Microbiology and Biotechnology Letters
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• v.32 no.1
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• pp.29-36
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• 2004

$\alpha$-Cyclodextrin glucanotransferase excreted from a newly isolated Geobacillus thermosacchalytycus was purified through the ultrafiltraion, hydrophobic Sepharose CD-4B affinity chromatography, and gel filtration on Sephadex G-75, respectively. The molecular weight of the purified CGTase was 69 kDa and its N-terminal amino acid sequence was determined to be Asn-Leu-Asn-Lys-Val-Asn-Phe-Val-Ser-Asp-Val-Val-Val-Gln-Ile. The optimum pH and temperature were pH 6.0 and$ 60^{\circ}C$, respectively, and stably at the pH range of 6.0-8.0 and $60^{\circ}C$ in the presence of $Ca^{++}$. The excreted CGTase from the thermophilic G. thermosacchalytycus was $\alpha$-type showing a high coupling activity for the transglycosylation on various glucosides. The coupling reaction was carried out according to the random ternary complex mechanism.m.

• Journal of Korean Society of Environmental Engineers
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• v.30 no.11
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• pp.1139-1145
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• 2008

The objectives of this research are to investigate the mechanism of coagulation affecting UF and find out the optimum conditions of the combined of coagulation with UF membrane filtration for NOM removal. 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 (both rapid mixing and slow mixing) improved dissolved removal efficiency. Also, for combined coagulation to membrane process, flux reduction rate showed lower than only UF process. 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.

• Food Science of Animal Resources
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• v.39 no.6
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• pp.966-979
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• 2019

Muscle-based by-products are often undervalued although commonly reported having a high amount of natural bioactive peptides. In this study, elastin was isolated from the protein of broiler hen skin while its hydrolysate was prepared using Elastase. Assessment of antioxidative properties of elastin-based hydrolysate (EBH) was based on three different assays; 2,2-diphenyl-1-picryl-hydrazyl-hydrate (DPPH) radical, 2,2'-azinobis (3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) radical and metal chelating ability. The EBH was purified further using ultrafiltration, gel filtration and Reverse- Phase High-Performance Liquid Chromatography (RP-HPLC). The IC₅₀ of ABTS radical activities for EBH were decreased as EBH further purified using ultrafiltration (EBH III; 0.66 mg/mL)>gel filtration (EB-II; 0.42 mg/mL)>RP-HPLC (EB-II4; 0.12 mg/mL). The sequential identification of the peptide was done by matrix-assisted laser desorption/ionization time-of-flight/time-of-flight mass spectrometry (MALDI-TOF/ TOF-MS) of the potent fractions obtained from RP-HPLC (EB-II4). The presence of hydrophobic amino acids (Val and Pro) in the peptide sequences could potentially contribute to the high antioxidant activity of EBH. The sequences GAHTGPRKPFKPR, GMPGFDVR and ADASVLPK were identified as antioxidant peptides. In conclusion, the antioxidative potential from poultry skin specifically from elastin is evident and can be explored to be used in many applications such as health and pharmaceutical purposes.

• Membrane and Water Treatment
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• v.2 no.3
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• pp.137-145
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• 2011

Membrane processes are major breakthrough for the removal of organic pollutants in water remediation. The separations of solutes depend on nature of the membranes and solutes. The separation performance depends on the nature of the solutes (i.e., molecular volume, polarity, and hydrophobicity) for the same membrane. As 4-chlorophenol is of more dipolemoment compared to 2-chlorophenol, the orientation of the molecule enables it pass through the pores of the membrane, which is of negatively charged and thus separation order follows: 2-chlorophenol > 4-chlorophenol. Hydrophobicity factor also supports the order. Addition of sodium dodecyl sulfate (SDS) to chlorophenol solution shows remarkable increase in separation performance of the membrane. The improvement in separation is 1.8 and 1.5 times for 4- and 2- chlorophenol consecutively in case of 0.0082 M SDS (1cmc = 0.0082 M) in the solution. 4-chlorophenol has better attachment tendency with SDS because of its relatively more hydrophobic nature and thus reflects in performance i.e. the separation performance of 4-chlorophenol with SDS through the membrane is better compared to 2-chlorophenol.

• BMB Reports
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• v.39 no.2
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• pp.150-157
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• 2006

Native grass carp (Ctenopharygodon idellus) growth hormone, has 5 cysteine amino acid residues, forms two disulphide bridges in its mature form. Recombinant grass carp growth hormone, when over-expressed in E. coli, forms inclusion bodies. In vitro oxidative renaturation of guanidine-hydrochloride dissolved recombinant grass carp growth hormone was achieved by sequential dilution and stepwise dialysis at pH 8.5. The redox potential of the refolding cocktail was maintained by glutathione disulphide/glutathione couple. The oxidative refolded protein is heterogeneous, and contains multimers, oligomers and monomers. The presence of non-disulphide-bond-forming cysteine in recombinant grass carp growth hormone enhances intermolecular disulphide bond formation and also non-native intramolecular disulphide bond formation during protein folding. The non-disulphide-bond-forming cysteine was converted to serine by PCR-mediated site-directed mutagenesis. The resulting 4-cysteine grass carp growth hormone has improved in vitro oxidative refolding properties when studied by gel filtration and reverse phase chromatography. The refolded 4-cysteine form has less hydrophobic aggregate and has only one monomeric isoform. Both refolded 4-cysteine and 5-cystiene forms are active in radioreceptor binding assay.

• Journal of Microbiology and Biotechnology
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• v.21 no.8
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• pp.838-845
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• 2011

The present work describes the identification, purification, and characterization of bile salt hydrolase (BSH) from Bifidobacterium animalis subsp. lactis. The enzyme was purified to electrophoretic homogeneity by hydrophobic chromatography, ion-exchange chromatography and ultrafiltration. SDS-PAGE analysis of putative BSH and gel filtration revealed that the analyzed protein is presumably a tetramer composed of four monomers each of about 35 kDa. The purified enzyme was analyzed by liquid chromatography coupled to LTQ FT ICR mass spectrometry and unambiguously identified as a bile salt hydrolase from B. animalis. The isoelectric point of the studied protein was estimated to be around pH 4.9. The pH optimum of the purified BSH is between 4.7 to 6.5, and the temperature optimum is around 50oC. The BSH of B. animalis could deconjugate all tested bile salts, with clear preference for glycine-conjugated bile salts over taurine-conjugated forms. Genetic analysis of the bsh showed high similarity to the previously sequenced bsh gene from B. animalis and confirmed the usefulness of bile salt hydrolase as a genetic marker for B. animalis identification.

• Journal of Microbiology and Biotechnology
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• v.8 no.4
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• pp.318-324
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• 1998

A ${\beta}$-galactosidase with high transgalactosylic activity was purified from a Bacillus species, registered as KFCC10855. The enzyme preparation showed a single protein band corresponding to a molecular mass of 150 kDa on SDS-PAGE and gave a single peak with the estimated molecular mass of 250 kDa on Sephacryl S-300 gel filtration, suggesting that the enzyme is a homodimeric protein. The amino acid and sugar analyses revealed that the enzyme is a glycoprotein, containing 19.2 weight percent of sugar moieties, and is much more abundant in hydrophilic amino acid residues than in hydrophobic residues, the mole ratio being about 2:1. The pI and optimum pH were determined to be 5.0 and 6.0, respectively. Having a temperature optimum at $70^{\circ}C$ for the hydrolysis of lactose, the enzyme showed good thermal stability. The activity of the enzyme preparation was markedly increased by the presence of exogenous Mg (II) and was decreased by the addition of EDTA. Among the metal ions examined, the most severely inhibitory effect was seen with Ag (I) and Hg (II). Further, results of protein modification by various chemical reagents implied that 1 cysteine, 1 histidine, and 2 methionine residues occur in certain critical sites of the enzyme, most likely including the active site. Enzyme kinetic parameters, measured for both hydrolysis and transgalactosylation of lactose, indicated that the enzyme has an excellent catalytic efficiency for formation of the transgalactosylic products in reaction mixtures containing high concentrations of the substrate.

• The Korean Journal of Physiology
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• v.24 no.1
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• pp.131-144
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• 1990

It is well known that the atrial natriuretic peptide (ANP) has a prepro-hormone of 151 amino-acids which loses their hydrophobic signal peptide to form 126 amino acid prohormone. The whole prohormone is released and then cleaved by proteases into more than one circulating forms. Recently, Winters et al. (1988a, b) reported that high concentrations of N-terminal fragments of prepro-ANP $(26{\sim}55),\;(56{\sim}92)\;and\;(104{\sim}123)$ were detected in human plasma. However, their physiological roles have not been established. The present study was conducted to determine whether the N-terminal fragments of pro-ANP have any effect on the renal function and to compare the effect with those of G-terminal fragments of pro-ANP The results indicate that intrarenal arterial infusions of prepro-ANP $(26{\sim}41),\;(26{\sim}55),\;(56{\sim}92)\;and\;(104{\sim}123)$ induced no significant changes in renal function. Whereas ${\alpha}-human$ ANP $(prepro-ANP,\;124{\sim}151)$ and pro-ANP caused a significant increase in urine volume, renal plasma flow, glomerular filtration rate, urinary excretions of sodium, chloride and potassium, and fractional excretion of sodium. These results suggest that the N-terminal fragments of pro-ANP are ineffective, while the C-terminal fragments retain the natriuretic and diuretic activities.