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

• Food Science and Preservation
• /
• v.22 no.3
• /
• pp.421-427
• /
• 2015

Oriental melon (Cucumis melo L. var. makuwa) has been widely consumed as various processed foods, such as dried products, jelly, wine, juice, and vinegar, in Asian countries. In fruit processing, blanching and pressure treatments affect its quality, such as antioxidant activities, sensory characteristics, and etc. This study was conducted to evaluate the effects of blanching and pressure pre-treatments on oriental melon wine-making (BP, blanching and pressure filtration; BNP, blanching and non-pressure filtration; NBP, non-blanching and pressure filtration; and NBNP, non-blanching and non-pressure filtration). Physicochemical properties and antioxidant capacities by ${\alpha}$, ${\alpha}$-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging activity, ferric ion reducing antioxidant power (FRAP) assay, and total phenolic and total flavonoid contents were measured for comparison of the different pre-treatment methods. After the aging process, the alcohol contents and pH values showed no statistical differences, whereas the amount of soluble solids, reducing sugar, and titratable acidity were slightly different among the pre-treatments (p<0.05). The samples with blanching pre-treatment showed higher antioxidant capacities than those of other pre-treatments. In the sensory evaluation, the BNP was the best in overall acceptability. Thus, this study showed that the blanching treatment enhanced the antioxidant capacities and sensory qualities of the oriental melon wine.

• Journal of Korean Society of Environmental Engineers
• /
• v.32 no.8
• /
• pp.754-760
• /
• 2010

Geosmin removal by biodegradation was investigated in lab-scale slow sand filtration column with different empty bed contact times (EBCTs) and water temperature. Schmutzdecke layer was built up after 30 days operation and biomass and activity were $4.5{\times}10^6\;CFU/g$ and $3.42\;mg{\cdot}C/m^3{\cdot}hr$, respectively. The attached bio-film microorganisms in schmutzdecke layer were isolated and identified. The dominant species was Pseudomonas sp. that had occupied 56%. Removal efficiencies of dissolved organic carbon (DOC) and geosmin were 27% and 95% after 30 days operation. In lab-scale slow sand filtration column, geosmin and DOC removal efficiencies were 62% and 10% at $5^{\circ}C$, respectively. And increasing water temperature ($15^{\circ}C$ and $25^{\circ}C$) increased the geosmin and DOC removal efficiencies (88~100% and 25~42%) in lab-scale slow sand filtration column. Geosmin and DOC biodegradation rates (k) in the schmutzdecke layer (in the upper 5 cm filter bed) were $1.842{\sim}15.965\;hr^{-1}$1 and $0.253{\sim}1.123\;hr^{-1}$, respectively. It were about 18~32 times and 20~51 times of the rates in the deeper filter bed (5~60 cm).

• Biomolecules & Therapeutics
• /
• v.5 no.1
• /
• pp.53-58
• /
• 1997

$[Lys^7$]dermorphin, abbreviated K7DA, which has structural features similar to a metabolically stable $\mu$-opioid peptide agonist $[D-Arg^2, Lys^4$]dermorphin analogue (DALDA), but is intrinsically more potent with respect to binding to the $\mu$-opioid peptide receptor. The present studies report on attempts to enhance brain uptake of systemically administered K7DA by conjugation to a complex of streptavidin (SA) and the OX26 murine monoclonal antibody to the rat transferrin receptor, which undergoes receptor-mediated transcytosis through the blood-brain barrier (BBB). SA-OX26 conjugate mediates BBB transport of biotinylated therapeutics. The K7DA is monobiotinylated at the $\varepsilon$-amino group of the $[Lys^7$] residue with cleavable linker using NHS-SS-biotin. The brain uptake of $^{125}I$ labeled biotinylated K7DA ($^{125}I$-bio-SSa-K7DA) was very small and rapidly metabolized after intravenous injection. The brain uptake, expressed as percent of injected dose delivered per gram of brain, of the $^{125}I$-bio-55-K7DA bound to the SA-OX26 conjugate $^{125}I$-bio-SS-K7DA/SA-OX26) was 0.14$\pm$0.01, a level that is 2-fold greater than the brain uptake of morphine. The cleavability of the disulfide linker in vivo in rat plasma and brain was assessed with gel filtration HPLC and intravenous injection of labeled opioid chimeric peptides. The disulfide linker is stable in plasma in vivo but is cleaved in rat brain in vivo. In conclusion, these studies show that delivery of these potential opioid peptides to the brain may be improved by coupling them to vector-mediated BBB drug delivery system.

• Korean Journal of Agricultural Science
• /
• v.39 no.2
• /
• pp.255-261
• /
• 2012

A bacterium AB-55, isolated from waste mushroom bed of Agaricus bisporus in Sukseong-myeon, Buyeo-gun, Chungcheongnam-do, Korea, was screened onto xylan agar congo-red plate by the xylanolysis method and was used to produce an xylanase in shaker buffle flask cultures containing oat spelt xylans. The phylogenetic analysis using 16S rRNA gene sequence data showed that the strain AB-55 had the highest homology (99.0%) with Bacillus subtilis and it was named as Bacillus subtilis AB-55. A xylanase was purified by ammonium sulfate precipitation (50~80%), gel filtration on sephacryl S-300, and ion exchange chromatography on DEAE sepharose FF. The molecular weight of the xylanase was estimated as 44 kDa by SDS-PAGE. Optimal pH and temperature for the xylanase activity was pH 7 and $50^{\circ}C$, respectively. N-terminal amino acid sequence of the enzyme was identified as Ser-Ala-Val-Lys-His-Gly-Ala-Ile-Val-Phe. The substrate specificity of the enzyme exhibited that it hydrolyzed efficiently oat spelt xylan as well as beechwood xylan, but showed no activity against Avicel and carboxymethyl clellulose (CMC). The enzyme activity was enhanced by $Fe^{2+}$ and $Mn^{2+}$ whereas was entirely inhibited by $Hg^+$.

• Journal of the Korea Organic Resources Recycling Association
• /
• v.21 no.4
• /
• pp.72-81
• /
• 2013

The objective of this study was to verify whether SCB(Slurry Composting & Bio-filtration) system can be applied for the treatment of anaerobic digestion(AD) wastewater and also, to identify the most effective set among three filtration compost beds tested. Results can be summarized as these; (a) When AD wastewater was sprayed on the top of beds which were mainly composed of sawdust and/or other media and, subsequently, filtrates collected and analyzed, there were large drop in the values of Electric Conductivity(EC), Total Suspended Solid(TSS), Biochemical Oxygen Demand(BOD), and Chemical Oxygen Demand(COD). In contrast, Total Nitrgen(T-N) and Total Phosphorus(T-P) were progressively elevated. We consider these changes as positive if the filtrate are to be utilized as liquid fertilizer. (b) When three sets of filtration beds (T1, T2, T3) were compared for their effectiveness, no significant difference was found among them. These indicate that expensive sawdust can be replaced in part with cheaper media such as woodchip, rice husks, or others. (c) At early stage of operation (within 20 days), BOD in filtrates were maintained at high level probably due to the lack of microbial activity. During the same stage, T-N, T-P was at low level but, were elevated to higher levels thereafter. These data, when combined, indicate that the filtration system needs at least a couple of weeks for the optimized microbial functioning. (d) The temperatures of the experimental beds were progressively dropped as the experiment continued through the fall season, although filtration effectiveness was not noticeably influenced.

• Journal of Microbiology and Biotechnology
• /
• v.29 no.7
• /
• pp.1043-1052
• /
• 2019

Active lipase-producing bacterium Burkholderia gladioli Bps-1 was rapidly isolated using a modified trypan blue and tetracycline, ampicillin plate. The electro-phoretically pure enzyme was obtained by purification using ethanol precipitation, ion-exchange chromatography, and gel filtration chromatography. The molecular weight was 34.6 kDa and the specific activity was determined to be 443.9 U/mg. The purified lipase showed the highest activity after hydrolysis with $p-NPC_{16}$ at a pH of 8.5 and $50^{\circ}C$, and the $K_m$, $k_{cat}$, and $k_{cat}/K_m$ values were 1.05 mM, $292.95s^{-1}$ and $279s^{-1}mM^{-1}$, respectively. The lipase was highly stable at $7.5{\leq}pH{\leq}10.0$. $K^+$ and $Na^+$ exerted activation effects on the lipase which had favorable tolerance to short-chain alcohols with its residual enzyme activity being 110% after being maintained in 30% ethanol for 1 h. The results demonstrated that the lipase produced by the strain B. gladioli Bps-1 has high enzyme activity and is an alkaline lipase. The lipase has promising chemical properties for a range of applications in the food-processing and detergent industries, and has particularly high potential for use in the manufacture of biodiesel.

• Journal of the Korea Safety Management & Science
• /
• v.11 no.4
• /
• pp.111-118
• /
• 2009

In this study the real situation of apartment house in seoul is reproduced with multi-zone modeling program CONTAM2.4. This model include disinfection system which is consist of dilution, filtration, UVGI(ultra violet germicidal irradiation). It's energy consumption was also analyzed through the linked model of CONTAM and TRNSYS according to the combination of components. The comparison of total energy consumption through energy analysis revealed that adjusting the air change rate of the UVGI air sterilizer to maintain the same indoor microbe removal capability was more advantageous in terms of energy consumption.

• Proceedings of the Korean Society of Applied Pharmacology
• /
• 1994.04a
• /
• pp.279-279
• /
• 1994

Fibrinolytic proteases, piscivorase I (PI) and piscivorase II (PII), were isolated from Agkistrodon piscivorus piscivorus (eastern cotonmouth moccasin) venom using gel filtration on Bio-Gel P100 and ion-exchange chromatography on CM-Sepharose. The molecular welghts of two proteases were approximately 23400 and 29000. Their isoelectric points 6.6 and 8.5, respectively. The partial amino acid sequences of PI were characterized by tryptic digestion. PI readily cleaves the A${\alpha}$-and B${\beta}$-chaln of fibronogen, but PII rapidly cleaves A${\alpha}$-chain and more slowly the B${\beta}$-chain, They were activated by Ca$\^$2+/, Mg$\^$2+/ and Ba$\^$2+/, but inhibited by Zn$\^$2+/, Cu$\^$2+/ and Mn$\^$2+/. Two enzymes were also inhibited by cysten, ${\beta}$-mercapto -ethanol, and by metal chelators such as EDTA and EGTA, but not by benzamidine, PMSF, soybean trypsin inhibitor and aprotinin. They did not act like thrombin, plasmin and kallikrein, using specific chromogenllc substrates. Two protease did not induce platelet aggregation. PI showed low hemorrhagic activity at dosage of 50 $\mu\textrm{g}$.

• Journal of Microbiology and Biotechnology
• /
• v.1 no.4
• /
• pp.232-239
• /
• 1991

Caboxymethyl cellulase (CMCase) I was purified from the induced culture filtrate of Penicllium verruculosum F-3 by ammonium sulfate precipitation, DEAE-Sephadex A-50 chromatography and Bio-gel P-150 filtration. The purified enzyme was assumed to be a glycoprotein consisting of 8.5% carbohydrate and having a molecular weight of 70.000 in SDS-polycrylamide gel electrophoresis (SDS-PAGE). The purified enzyme-specific anti-CMCase I IgG was obtained by rabbit immunization and protein A-sepharose CL-4B chromatography. The fungal poly($A^+$) RNA was isolated from the total RNA of the mycelium grown under cellulase induction conditions by oligo(dT)-cellulosse chromatography. The translation products in vitro were prepared by translating the isolated poly ($A^+$) RNA in rabbit reticulocyte lysate and analyzed by SDS-PAGE and fluorography. Of the translation products, CMCase I was identified by the immunoprecipitation against anti-CMCase I IgG.