• Bulletin of the Korean Chemical Society
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• 제15권9호
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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.

• 한국식품저장유통학회지
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• 제22권3호
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• pp.421-427
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• 2015

고품질 참외와인을 제조하기 위하여 브랜칭 및 착즙 처리를 하여 발효와 숙성에 따른 이화학적 특성 및 항산화능을 조사하였다. 발효 중 참외와인의 이화학적 특성은 모든 처리구가 유사한 추이를 보였으며, 브랜칭 및 착즙 처리가 알코올 발효에 영향을 미치지 않았다. 숙성 후 이화학적 특성을 측정한 결과는 알코올 함량, 가용성 고형분 함량, 환원당 함량, 적정 산도, pH가 각각 11.5~11.8%, 10.7~11.2%, 0.25~0.49 g/100 mL, 0.60~0.81%, 3.75~3.89 범위로 나타났으며, 숙성 전에 비하여 가용성 고형분, 환원당, 알코올 함량, 적정산도는 감소하고 pH는 증가하는 것으로 나타났다. 항산화능은 DPPH 라디칼 소거 활성, FRAP 활성이 각각 $563.00{\sim}785.00{\mu}M\;TE$, $504.60{\sim}811.93{\mu}M\;TE$ 범위로 나타났으며, 브랜칭 처리구의 항산화 활성이 높았다. 총페놀성 화합물 함량은 287.53~312.08 mg/L 범위로 전처리 방법에 따른 유의적인 차이가 나타나지 않았으며(p<0.05), 총플라보노이드 함량은 39.06~141.03 mg/L 범위로 브랜칭 처리구의 함량이 높았다. 또한 QDA profile 결과는 색, 맛, 풋내, 이취, 종합적 기호도 항목에서 모두 브랜칭 처리구가 더 높은 점수를 얻었다. 브랜칭 처리는 참외와인의 항산화능을 증가시키고 기호성을 좋게 하는 반면, 착즙 처리는 참외와인 제조 시 영향을 미치지 않는 것으로 나타났다.

• 대한환경공학회지
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• 제32권8호
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• pp.754-760
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• 2010

완속 모래여과 컬럼의 생물막(schmutzdecke)은 운전 시작 30일 정도에 정상상태에 도달하는 것으로 나타났으며, 생체량과 활성도는 각각 $4.5{\times}10^6\;CFU/g$과 $3.42\;mg{\cdot}C/m^3{\cdot}hr$로 나타났다. 정상상태에 도달한 생물 여과층의 박테리아 종 분포는 Pseudomonas sp.가 차지하는 비율이 56%였으며 그 중에서 Pseudomonas fluorescens가 전체비율의 22%를 차지하였다. 운전 시작 30일 후의 용존 유기탄소(dissolved organic carbon, DOC)와 geosmin의 제거율은 각각 27%와 95%로 나타나 최대의 제거율을 나타내었으며, 그 이후에는 DOC와 geosmin의 제거율에는 큰 변화가 없었다. 수온 변화에 따른 DOC와 geosmin의 제거율 변화에서 유입수의 수온이 $5^{\circ}C$일 경우 geosmin과 DOC의 평균 제거율은 각각 62%와 10%로 나타났으나 수온을 $15^{\circ}C$와 $25^{\circ}C$로 증가시켰을 경우에는 geosmin과 DOC의 평균 제거율이 각각 88%와 25% 및 100%와 42%로 나타났다. 수온 변화에 따른 완속 모래여과 컬럼의 상부 생물막 층에서의 geosmin과 DOC에 대한 생물분해 속도상수(k)는 $1.842{\sim}15.965\;hr^{-1}$와 $0.253{\cdot}1.123\;hr^{-1}$이였고, 상부의 생물막 층이 그 하부 보다 DOC와 geosmin에 대한 생물분해 속도상수가 각각 18~32배 및 20~51배 정도 큰 것으로 나타났다.

• Biomolecules & Therapeutics
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• 제5권1호
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• pp.53-58
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• 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.

• 농업과학연구
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• 제39권2호
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• pp.255-261
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• 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 $Hg^+$.

• 유기물자원화
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• 제21권4호
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• pp.72-81
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• 2013

본 실험에서는 돈분뇨의 혐기소화 과정에서 발생하는 소화폐액을 액비로 자원화하기 위해 기존의 SCB 기법(퇴비단 여과)을 적용하여 그 효과를 검토하였으며, 여과재의 선택과 여과단 구성방법이 여과작용에 어떠한 영향을 미치는 지를 평가하였다. 주요 결과를 요약하면 (a) 퇴비단 여과상을 이용하여 돈분뇨 슬러리 혐기소화폐액을 여과하였을 경우, EC, BOD, SS는 낮아지고 T-N, T-P는 상승하는 것을 확인하였으며, 이러한 변화는 여과액이 액비로서 지니는 가치를 상승시키는 효과라고 볼 수 있다. (b) 3가지의 퇴비단 조합들(T1, T2, T3)을 비교해 볼 때 대부분의 지표에서 별다른 차이를 보이지 않았다 따라서 값비싼 원료인 톱밥을 저가의 왕겨 또는 목편으로 일부 대체하였을때 퇴비단의 여과 능력에는 큰 변화가 없을 것으로 판단된다. (c) 초기 여과액에서는 BOD가 매우 높게 유지되었으나 여과상의 미생물이 충분히 증식함에 따라 하향 안정되었다. 반면 T-N, T-P의 경우 초기에는 낮은 수준을 유지하다가 15일 이후 원수와 비슷한 수준으로 유지되었다. 이 결과에서 퇴비단 운영 시작 후 20일 이내에 얻어진 여과액은 액비로 사용하기에는 적합하지 않으며 사용을 제한할 필요가 있다고 판단된다. (d) 계절적인 영향에 의한 외기온도의 저하로 퇴비단 내부 온도가 저하되었으나 여과효율에는 큰 영향을 미치지 않는 것으로 나타났다.

• Journal of Microbiology and Biotechnology
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• 제29권7호
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• pp.1043-1052
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• 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.

• 대한안전경영과학회지
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• 제11권4호
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• pp.111-118
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• 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.

• 한국응용약물학회:학술대회논문집
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• 한국응용약물학회 1994년도 춘계학술대회 and 제3회 신약개발 연구발표회
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• pp.279-279
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• 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
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• 제1권4호
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• pp.232-239
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• 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.