• Journal of Wetlands Research
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• v.14 no.1
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• pp.47-57
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• 2012

We have measured soil enzyme activities, which represent the rates of organic matter decomposition, in four riparian ecosystems in Korea. ${\beta}$-glucosidase, N-acetylglucosaminidase, phosphatase and arylsulfatase activities were determined in five occasions over a year period in soils of control plots and plots with invasive plants, namely Sicyos angulatus and Humulus japonicus. Significantly higher enzyme activities were found in soils with invasive plant in barren land, but the difference was season and enzyme-specific. Although it was not universal changes, the invasive plants appeared to accelerate organic matter decomposition in some disturbed riparian ecosystems.

• The Korean Journal of Mycology
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• v.51 no.4
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• pp.265-276
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• 2023

This study aimed to isolate and characterize fungi from freshwater environments in South Korea and evaluate their extracellular enzyme activities. Fungal strains were collected from various freshwater sources and identified using phylogenetic analysis. The isolated fungi included known aquatic hyphomycetes and previously unreported species. Extracellular enzyme, including those of protease, amylase, lipase, cellulase, laccase, and chitinase, activities were evaluated. Among the isolated strains, several showed high enzyme activity, suggesting their potential role in organic matter decomposition in freshwater ecosystems. This research expands our knowledge of the diversity and enzyme activities of the fungi in freshwater environments, contributing to our understanding of their ecological roles.

• Microbiology and Biotechnology Letters
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• v.17 no.1
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• pp.69-73
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• 1989

Cellular autolytic enzyme was isolated from the supernatant fluid of exponentially growing cuiture of Cl. butyricum ID-113. The autolysin was partially pruified by ammonium sulfate fractionation, chromatography on DEAE-Sephadex A-50 and gel filtration through Sephadex G-200. This autolytic enzyme lysed SDS-treated cell wall fractions of Cl. butyricum ID, but not whole cells at all. Its optimum pH and temperature were 5.0 and 37$^{\circ}C$, respectively. This enzyme was relatively stable at neutral pH, but sensitive to heat treatment. Enzyme activity was not influenced by the addition of various divalent cation, but inhibited by Cu$^{++}$.

• Korean Journal of Microbiology
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• v.27 no.3
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• pp.237-244
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• 1989

A soluble intracellular protease from cells of Pseudomonas carboxydovorans, a carboxydobacterium, grown on nutrient broth was purified 68-fold in five steps to better than 95% homogeneity with a yield of 2.4% using azocasein as a substrate. The enzyme activity was not detected from cells grown on pyruvate, succinate, acetate, or CO as a sole source of carbon and energy. The molecular weight of the native enzyme was determined to be 53,000. Sodium dodecyl sulfate-gel electrophoresis revealed the purified enzyme a monomer. The enzyme was found to be a serine-type protease. The enzyme activity was inhibited completely by several divalent cations such as $Cd^{2+}, Cu^{2+}, Hg^{2+}$, and $Fe^{2+}$. The enzyme was also inhibited by EGTA, but was stimulated by iodoacetamide. The optimal pH and temperature for the enzyme reaction were found to be 8.0 and $50^{\circ}C$, respectively. The enzyme was inactive on CO dehydrogenase.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1986.12a
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• pp.526.1-526
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• 1986

세균내 glutathione의 동태를 연구하기 위한 일환으로 P. mirabilis로부터 cysteinylglycine 분해효소를 정제 검토하였다. 본 균이 생산하는 cysteinylglycine 분해효소의 정제는 무세포추출액에 비해 비활성이 10배 증가하였고 0.68%의 낮은 수율을 나타내었다. 본 호소는 (NH$_4$)$_2$ SO$_4$ 침전과정에서 활성을 크게 손실하는 등 정제과정에서 불안정하였으며 투석 중에 형성하는 불용성 침전물은 4% Trition X-100 처리에 의해 효과적으로 용해되었다.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1986.12a
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• pp.518.2-519
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• 1986

토양으로부터 분리한 질소고정균인 Klebsiella pneumoniae NFB320의 chromosomal DNA를 BamHI으로 절단하여 동일한 제한효소로 절단한 pBR322에 ligation시켜 E. coli HB101에 형질전환을 행하여 pullulanase activity를 나타내는 clone을 얻어내었다. 이 형질 전환체로부터 분리한 pullulanase 유전자가 재조합된 plasmid DNA는 약 10kb의 DNA단편을 가지고 있었으며, 재조합된 plasmid로부터 생산되는 pullulanase의 특성은 최적 활성 pH가 6.0이며, 효소의 pH안정성은 5-10이었다. 또한 형질 전환체로부터 생산되는 pullulanase의 localization,효소활성에 영향을 미치는 온도안정성 둥을 조사하였다.

• Microbiology and Biotechnology Letters
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• v.44 no.3
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• pp.376-382
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• 2016

The amylolytic enzyme activities of nuruks collected or produced in this study were examined. A maximum α-amylase activity of 24,747.1 ± 777.7 units/mg protein was obtained for a nuruk incubated at a relative humidity of 40% at 30℃. A nuruk matured at a relative humidity of 50% at 25℃ showed the highest glucoamylase acitivity. Among the 98 fungal strains isolated from the nuruk exhibiting the highest amylolytic enzyme activities, 26 strains of Aspergillus oryzae and 18 strains of Rhizopus oryzae were identified. Rhizopus oryzae MBF345 showed an α-amylase activity of 36,724.9 ± 10.2 units/mg protein and a glucoamylase activity of 4,911.8 ± 48.1 SP. These values were 1.7-fold and 1.4-fold greater, respectively, than those of the control strain. Strain MBF345 was deposited as KCTC46312 in the Korean Culture Type Collection.

• Microbiology and Biotechnology Letters
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• v.17 no.2
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• pp.148-153
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• 1989

A strain of alkalophilic Bacillus sp. YC-335 has been isolated from soil. The strain was capable of producing large amount of cyclodextrin glycosyl transferase (CGTase) in the culture broth. The preferable medium composition has been determined to be as follows : 1.5% soluble starch, 5% corn steep liquor, 0.1% $K_2$HPO$_4$, 0.02%mgSO$_4$.7$H_2O$, 1% CaCO$_3$and 1% Na$_2$CO$_3$(pH 10.3). The highest enzyme production was observed after 48 hours of cultivation at 31$^{\circ}C$. The optimum pH and temperature for the activity of crude enzyme were 6.0 and 5$0^{\circ}C$, respectively. The enzyme was stable between pH 5 and 9, and upto 5$0^{\circ}C$. The enzyme converted starch into $\alpha$-, $\beta$- and ${\gamma}$-CD in the relative amounts of 1:10:1.5, respectively.

• Korean Journal of Microbiology
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• v.35 no.3
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• pp.231-236
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• 1999

The fuugus(Penicil1ium oralicum; HCLF-34) secreted the cyanobacteria lytic enzyme which had a molecular weight of about 22 kDa, a optimum temperature of $20^{\circ}C$, a optimum pH of 3.5, and a temperature-stable up to $50^{\circ}C$. The chemical ions such as sodium, potassium, barium, magnesium. and mangan ions appeared positive activity. but calcium, iron, copper ions, EDTA, and PMSF displayed negative activity: this results were the same as the characterilics of other cell wall lytic enzymes. This extracellular enzyme showed lytic aclivily against SDS-insoluble peptidoglycan of Anabaenrr cylinrlrica. The cell wall lylic enzyme of Penicilliurn oxalicum(HCLF-34) seemed to be glycosidase-like enzyme in the fact that ihe concentration of rcducing sugar was increased when the peptidoglycan of Anabaena qlinrlricn md Micrococcus luteus reacted with this enzyme

• Korean Journal of Microbiology
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• v.17 no.1
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• pp.42-48
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• 1979

Cellulases were isolated from both healthyl(PC) and virus0infected penicillum chrysogenum(PCV) in the wheat bean culture, and some properties of the enzymes were studied. 1) At $37^{\circ}C$, pH 6, 4 and 6day's culture the maximal enzyme yield was obtained in both PC and PCV. 2) The optimum temperature for the PC cellulase was at $50^{\circ}C$, and that for the PCV enzyme was the same. 3) The optimum pH for the PC enzyme was at 5.0, whereas the PCV enzyme was at 6.0, indicating that they are isozymes. 4) When Na-CMC was used as a substrate, PC enzyme was twice as high as the activity of PCV enzyme.