• Journal of Acupuncture Research
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• v.28 no.2
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• pp.125-131
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• 2011

목적 : 본 연구는 합환피약침액(合歡皮藥鍼液)이 사람 피부 섬유아세포의 콜라게나제 활성 및 프로콜라겐 합성에 미치는 영항과 티로시나제 활성에 미치는 효과를 측정하고자 실시하였다. 방법 : HS68 사람 정상 섬유아세포에 UVB 조사 후 합환피(合歡皮) 약침액(藥鍼液)가 type I procollagen 생성과 콜라게나제 효소활성에 미치는 효능과 티로시나제 효소활성에 미치는 효능을 평가하였다. 결과 : 합환피약침액(合歡皮藥鍼液)은 UVB 조사된 세포의 콜라게나제 효소활성을 통계적으로 유의하게 억제하였고, 티로시나제 활성을 통계적으로 유의하게 억제하였다. 그러나 티로시나제 억제활성의 정도는 미백효능으로 활용하기에 약간 약한 경향이 있었다. 결론 : 합환피약침액(合歡皮藥鍼液)의 콜라게나제 억제효능은 주름개선 약침치료에 활용이 가능할 것으로 생각된다.

• The Korean Journal of Mycology
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• v.11 no.3
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• pp.109-114
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• 1983

${\beta}-Galactosidase$ activity of Aspergillus phoenicis was studied using ONPG and lactose as substrate. It increased monotonically during the exponential growth phase and dropped rapidly at the beginning of the stationary one. It exhibited high tolerable temperature and acidic optimal pH which provides certain advantages from the industrial view point. Enzyme of ${\beta}-galactosidase$ had more subsrate affinity for ONPG than for lactose and its apparent maximum activity was also higher with the former as substrate. Activity of this enzyme depended upon the conditions of immobilization. Optimum crosslinking reaction was occurred at pH 7.2 and 0. 35 vol. % of glutaraldehyde concentration.

• The Korean Journal of Pesticide Science
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• v.11 no.3
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• pp.179-185
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• 2007

Esterase isozymes were investigated from digestive juice of M. saltuarius adults after pesticide treatment. Twelve esterase isozymes were separated on 12% native-PAGE gel and stained with three different substrates(${\alpha}$-naphthyl acetate, ${\beta}$-naphthyl acetate, and ${\alpha}$-naphthyl butyrate). Interestingly, the isozyme of Est1(${\alpha}$-naphthyl acetate) was strongly inhibited by the carbofuran and methomyl. The Est1 activity was completely inhibited by the chlorpyrifos and partially inhibited by methidation about 70 %. In addition, eserine suppressed esterase isozyme activities of Est1 about 70% and isozyme activities of Est2, Est3, and Est4 were weakly inhibited. ${\alpha}$-pinene did not suppressed esterase isozyme activities but activities of esterases were very weakly inhibited in camphor and bornyl acetate.

• Korean Journal of Microbiology
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• v.40 no.3
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• pp.230-231
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• 2004

The mycelia of Sparassis crispa DSMZ 5201 were cultivated at $24^{\circ}C$ for 15 days in yeast-malt extract-glucose broth (pH 4.0) and the filtrate was used as crude enzyme solution to determined the extracellular enzyme activity. The specific activity of $\alpha$-amylase was 44.27 unit/protein. The specific activities of protease, CMCase, $\beta$-glucosidase, chitinase, exo-$\beta$-l,4-glucanase were relatively high. However, a very little activity of xylanase was found.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1979.04a
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• pp.114.2-115
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• 1979

Horikoshi등이 호 alkali 성 미생물에 관한 연구에서 분리한 수종의 cellulolytic bacteria중에서 가장 강력한 균체의 효소를 생산하는 Aeromonas 속 세균의 cellulolytic 효소에 관한 연구 결과를 보고한다. 공업적으로 생산된 효소를 사용하여 효소작용의 최적조건을 측정하고 gel filtration, ion-exchange chromatography 및 affinity chromatography 로 cel-luplytic 효소를 분리정제하였다. 본 효소의 활성 최적 pH는 7.0~8.5로 alkaline 효소였으며 반응온도 5$0^{\circ}C$에서 가장 강한 활성을 보였다. 분리 정제과정에서 carboxymethyl cellulose (CMC)에 대하여 활성이 있는 단백질이 최소 8종이상 분리되었으며 이중 1개 효소는 CMC에 대해서는 극히 낮은 활성을 보였으나 결정성 기질인 Avicel 에는 강한 활성을 보였다. 본 연구의 결과를 Cellulomonas속 세균 및 Trichoderma속 곰팡이의 효소와 그 성질을 비교 검토하였다.

• Applied Biological Chemistry
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• v.36 no.1
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• pp.64-69
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• 1993

This study was performed to investigate detoxifying enzyme activities of carboxylesterase(CE), glutathione S-transferase(GST) and lactate dehydrogenase(LDH) at variable toxicity levels in fresh water fish, carp(Cyprinus carpio L.). The carp was exposed to single and combined pesticides of IBP, isoprothiolane and cartap for 48 hr at sublethal doses, $LC_{10}$ and $LC_{26}$. The detoxifying enzyme activities were assayed for the liver, head and gut of the carp. The enzyme activities we discovered were as follows: Both activities of CE and GST were increased at the sublethal doses but were declined by increasing doses. In the gut, we found that the CE activity had high levels in the treatment groups of isoprothiolane+IBP and isoprothiolane+cartap. In the head, the CE activity had high levels in the treatment groups of cartap, IBP and isoprothiolane. However, the GST activities were inconsistent in the head and gut of the fish. Also, the GST activity was declined by increasing protein contents. The highest LDH activity was shown in the isoprothiolane treated fish, while the lowest activity was observed in the isoprothiolane+cartap treatment.

• Proceedings of the Korean Society of Applied Pharmacology
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• 1997.04a
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• pp.84-84
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• 1997

장내세균은 음식물, 스트레스, 생활환경에 의해 영향을 받으며 그 결과 장내 세균이 생산하는 효소활성도 영향을 받는다. 장내미생물효소는 질병과 밀접한 관계를 갖고 있으며 장내의 pH와 효소저해제에 의해 영향을 받는 데 장내의 높은 pH에 의해 $\beta$-glucosidase, $\beta$-glucuronidase, tryptophanase 등의 장내유해효소활성이 유도되므로 장내의 pH를 낮춤으로써 효소활성을 저하시킬 수 있다. Bifidobacterium은 장내에서 lactic acid, acetic acid를 생산하여 장내의 pH를 낮추며 유해균의 증식을 억제하고 유해효소의 활성을 억제하는 역할을 할 것으로 기대된다. 특히 한국인으로부터 분리된 유산균일 경우 한국인의 장내에 가장 잘 정착되며 장내미생물의 유해효소를 효과적으로 억제할 것으로 생각된다.

• Korean Journal of Microbiology
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• v.39 no.4
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• pp.230-234
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• 2003

An extracellular protease of Bacillus amyloliquefaciens S94 was purified to apparent homogeneity. The enzyme activity was strongly inhibited by general inhibitor for serine protease, PMSF, suggesting that the enzyme is a serine protease. The purified enzyme activity was inhibited by leucine peptidase inhibitor, bestatin, suggesting that the enzyme is a leucine endopeptidase. When the enzyme was chemically modified with PMSF, which specifically reacted with serine residue on the enzyme, the activity was eliminated. The endopeptidase activity was inhibited by the modifier which chemically modified carboxyl group of aspartate and glutamate. PLP, which would modify lysine residue, did not affect the endopepetidase activity to a greater extent. This demonstrates that serine and aspartate (or glutamate) residues of enzyme would participate in a important function of the endopeptidase activity.

• Korean Journal of Microbiology
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• v.10 no.2
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• pp.87-92
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• 1972

In order to study on the pigment and protease of Serratia marcescens, the correlation between protease activity and pigment formation was investigated. The results are as follows ; 1) The protease activity exhibitied two pH optima 6.0 and 7.5, respectively. 2) The optimal temeprature of proteolytic activity was 45.deg.C. With these-results, it is suggested that the proteolytic enzymes of Serratia masrecescens is stable at neutral pH range and more active at the high temeprature than lthat of otehr proteolytic enzymes.

• Journal of Animal Science and Technology
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• v.51 no.2
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• pp.177-182
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• 2009

The glycosylated human MINPP (multiple inositol polyphosphate phosphatase), which was recombinantly over-expressed by using industrial host, Pichia pastoris, showed the phytase activity against phytate ($InsP_6$) and the enzyme activity of the unglycosylated counterpart was decreased to 30%. The optimal phytase activity occurred at pH 7.4. The human MINPP showed high substrate specificity for $InsP_6$ with little activity on other organic phosphate conjugates such as para-nitrophenylphosphate (pNPP), ATP, and ribose-1-phosphate (R-1-P). The phosphatase activity against 2,3-bisphosphoglycerate (2,3-BPG) by human MINPP was increased to 1.2-fold in the presence of stimulator, 1 mM 2-phosphoglycolate (2-PG) but the phytase activity against $InsP_6$ was not affected by addition of 1 mM 2-PG. The phosphatase activity against 2,3-BPG by human MINPP was not increased in the presence of 2 mM $Mg^{2+}$ or 100 mM $Cl^-$.