• Journal of the Korean Chemical Society
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• v.24 no.1
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• pp.25-33
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• 1980

Pyrocatechase as a phenolytic dioxygenase was extracted from the benzoate-induced cells of a soil bacterium, a member of Pseudomonadaceae, and purified partially by DEAE-cellulose ion-exchange chromatography and Sephadex G-75 gel filtration. Final preparation of the enzyme yielding 200 fold purification over the crude extracts showed a specific activity of about 40 ${\mu}moles$ per minute per mg protein based on catechol as the substrate. The enzyme showed a very limited substrate specificity towards catechol for its catalytic activity. Based on the inhibition study with the substrate analogues, it was assumed that ortho dihydroxy groups on the aromatic ring may participate in the enzyme-substrate binding. The $K_m$ value for catechol was obtained as $1.9{\times}10^{-6}M$, and the optimum activity of the enzyme was obtained at the pH range of 7∼10 and $35^{\circ}C$. With SH-group blocking agents the enzyme was inhibited seriously. The activity of enzyme was also inhibited by the addition of some heavy metals, $Ag^+$ and $Cu^{2+}$, but was not affected by EDTA. General property of the enzyme was characterized and the possible nature of the enzyme active center was also discussed.

• The Korean Journal of Mycology
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• v.1 no.1
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• pp.23-28
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• 1973

The soil of Kwangneung area(Kyeunggi-Do) was inoculated directly into wheat-bran-media and after $3{\sim}4$ days of incubation, a Penicillium species whose cellulase activity was 1011u/g was isolated. With the treatment of mutagenic agents an improved strain(cellulase activity: 1303u/g) was obtained. This strain was screened again by mono-spore isolation method. Finally a strain C8-14 (cellulase activity: 2351u/g) which had lesser spores than the wild strain was obtained.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1986.12a
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• pp.532.2-532
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• 1986

Alkaline protease which is an important enzyme used in detergents, leather tanning and food industry was produced by alkalophilic bacterium, Bacillus sp. KCTC 1723 isolated from soil. The maximum productivity of the enzyme in alkaline medium containing 1% sodium bicarbonate was obtained by incubating for 3 days at 37$^{\circ}C$. The optimum pH of the enzyme was 11.5 and calcium ion was effective on stabilization of the enzyme at high temperature. The enzyme was not inhibited by metal chelating agent such as El)TA but inhibited by diisopropyl fluorophosphate. Purification of the enzyme was carried out DEAE- and CM-cellulose column chromatographies and molecular weight of the purified enzyme was determined

• Journal of the Korean Society of Tobacco Science
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• v.27 no.1 s.53
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• pp.75-82
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• 2005

This work investigated biodegradability for the cellulose acetate, carbon dual, paper and web used to cigarette filter materials by soil test. Also, because of demanded a lot of the time and effort in case of soil test, the possibility of biodegradation by enzyme was studied. The evaluation of degradation for the filter materials by soil test was examined with the naked eye, electron microscopy and weight loss. The biodegradability according to the filter materials was represented in the order of paper > web > carbon dual > cellulose acetate without relating to the evaluation methods. Experiment of biodegradability by the cellulase(E C 3.2.1.4, Trichoderma viride) among the several biodegradability enzymes was demanded reaction time of the $5\~10$ hours and represented the same result with that of soil test.

• Journal of the Korean Society of Clothing and Textiles
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• v.20 no.4
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• pp.655-666
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• 1996

The effect of protease (subtilisin Carlsberg) on the removal of hemoglobin as protein soil was studied. The relation between the renloval and the hydrolysis of hemoglobin by subtilisin Carlsberg was discussed. The soiled babric was prepared by spotting of hemoglobin solution evenly on the cotton fabric and was denatured by steaming. The soiled fabric was washed by using Terg-0-Tometer at various conditions. The removal efficiency was evaluated by analysis of protein on the fabrics before and after washing by means of copper-Folin method. 1. The removal of hemoglobin was increased in proportion to increasing of the enzyme concentration up to a certain point, but it began to decrease above the point. 2. The hemoglobin was removed effectively by adding of subtilisin Carlsberg, and more effectively removed by adding of AOS in the enzyme solution. 3. The removal of hemoglobin deviated from the first order reaction in detergency. 4. The renloval of hemoglobin was highest at $50^{\circ}C$ in detergency, Even at low temperature the removal efficiency of enzyme was relatively higher compared with the hydrolysis of hemoglobin by the enzyme. However the removal of hemoglobin was apparently decreased with the increase of temperature over $60^{\circ}C$. 5. The removal of hemoglobin was relatively high at pH 7.0~8.0 and increased continuously with the increase of pH in detergency 6. In detergency, the removal mechanism of hemoglobin by subtilisin Carlsberg could be explained as follows: Fisrt of all, the enzyme hydrolyzed hemoglobin substrates partially by forming E-S complex at the surface of hemoglobin on the cotton fiber, and decomposed cooperative binding of hemoglobin. Subsequently, the fragments of hemoglobin were easily removed by washing. According as the enzyme penetrated to inner part of hemoglobin gradually, the hemoglobin on the cotton fiber was effectively removed by the repetition of these process. The removal of hemoglobin was more effectively increased by adding both the enzyme and AOS in the washing solution. Therefore, it was regarded that AOS molecules were adsorbed at the hydrophobic surface of denatured hemoglobin, subsequently, decomposed more effectively cooperative binding of hemoglobin, and the fragments of hemoglobin were removed more efficiently by means of the interfacial reaction of AOS.

• Journal of Applied Biological Chemistry
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• v.60 no.3
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• pp.257-263
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• 2017

A cellulolytic strain Y2 was isolated from soil obtained in the Canadian Alpine region. The isolate was identified as Paenibacillus sp. Y2 by 16S rRNA sequencing. When grown in LB medium supplemented with carboxymethyl-cellulose (CMC), CMCase production increased to 122.0% of that observed in LB without CMC. Culture supernatant was concentrated by ultrafiltration and 80% ammonium sulfate precipitates were separated by Hi-Trap Q and CHT-II chromatography. The purified enzyme (EG-PY2) showed a homogeneous single band and the molecular mass was estimated to be 38 kDa by SDS-PAGE. Optimum pH and temperature of the enzyme were 4.5 and $30^{\circ}C$, respectively. The half-life of enzyme activity at 50 was 140.7 min, but the enzyme was drastically inactivated within 5 min at $55^{\circ}C$. The enzyme was highly activated to 135.7 and 126.7% by 5.0 mM of $Cu^{2+}$ or $Mg^{2+}$ ions, respectively, and moderately activated by $Ba^{2+}$ and $Ca^{2+}$ ions, whereas it was inhibited to 76.8% by $Fe^{2+}$, and to ${\leq}50%$ by $Mn^{2+}$, $Co^{2+}$, $Zn^{2+}$, and EDTA. The enzyme was activated to 211.5% in the presence of 0.5 M of NaCl and greatly tolerant to 3.15M of NaCl. The enzyme showed 2.98 times higher ${\beta}$-glucanase activity than CMCase activity. Based on these results, it can be concluded that EG-PY2 is an acidophilic, cold-active, and halotolerant endoglucanase. The authors suggest it is considered to be useful for various industrial applications, such as, fruit juice clarification, acidic deinking processes, high-salt food processing, textile and pulp industries, and for biofuel production from seaweeds.

• Korean Journal of Soil Science and Fertilizer
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• v.38 no.5
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• pp.281-286
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• 2005

The effect of oyster shell meal, which is made of a simple crushing and alkaline calcium materials, on soil microbial properties, microbial biomass C, N and P contents, and enzyme activities were evaluated in silt loam soil. The oyster shell meal fertilizer was added at the rates of 0, 4, 8, 12 and $16Mg\;ha^{-1}$. Microbial biomass C, N and P contents were significantly increased with increasing application of oyster shell meal. Soil enzyme activities, such as urease, ${\beta}$-glucosidase and alkaline phosphomonesterase were increased significantly by shell meal application, due to increased soil pH towards neutral range and increased nutrient availability in soil. In particular, the increased microbial biomass P content and phosphomonoesterase activities were strongly correlated with available P content in soil. Conclusively, oyster shell meal fertilizer could be a good supplement to improve soil microbial activities.

• Ecology and Resilient Infrastructure
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• v.4 no.2
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• pp.93-96
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• 2017

Spatial variations of physicochemical and microbiological variables were examined to understand spatial heterogeneity of those variables in intertidal flat. Variograms were constructed for understanding spatial autocorrelations of variables by a geostatistical analysis and spatial correlations between two variables were evaluated by applications of a Cross-Mantel test with a Monte Carlo procedure (with 999 permutations). Water content, organic matter content, pH, nitrate, sulfate, chloride, dissolved organic carbon (DOC), four extracellular enzyme activities (${\beta}-glucosidase$, N-acetyl-glucosaminidase, phosphatase, arylsulfatase), and bacterial diversity in soil were measured along a transect perpendicular to shore line. Most variables showed strong spatial autocorrelation or no spatial structure except for DOC. It was suggested that complex interactions between physicochemical and microbiological properties in sediment might controls DOC. Intertidal flat sediment appeared to be spatially heterogeneous. Bacterial diversity was found to be spatially correlated with enzyme activities. Chloride and sulfate were spatially correlated with microbial properties indicating that salinity in coastal environment would influence spatial distributions of decomposition capacities mediated by microorganisms. Overall, it was suggested that considerations on the spatial distributions of physicochemical and microbiological properties in intertidal flat sediment should be included when sampling scheme is designed for decomposition processes in intertidal flat sediment.

• Journal of Microbiology and Biotechnology
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• v.15 no.5
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• pp.1067-1072
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• 2005

A metagenomic library was constructed using a fosmid vector, and total genomic DNA was extracted directly from soil at Cisolok (hot spring area, Indonesia). This library was composed of 10,214 clones and screened for lipolytic enzyme on tributyrin agar plates. An esterase gene (estMa) was subcloned and sequenced from a positive lipolytic active clone. Esterase EstMa was encoded by a 954-bp open reading frame and showed low ($11-33\%$) amino acid similarity to known esterases. The amino acid sequence analysis demonstrated that the enzyme is a new member of lipolytic enzyme family VI. The estMa gene encodes a preprotein of 317 amino acids with a predicted molecular mass of 34,799 Da. The purified enzyme exhibited optimal activity at $50^{\circ}C$ and pH 6.5. The $K_m,\;and\;V_{max}$ values of EstMa for the hydrolysis of p-nitrophenyl valerate were $45.3\;{\mu}M$ and 4.45 U/mg, respectively.

• The Korean Journal of Food And Nutrition
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• v.5 no.2
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• pp.132-136
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• 1992

Streptomyces sp. YB-88-20 was Isolated from soil and the properties of chitobiase were investigated. The optimal reaction condition for the enzyme was pH 5.5 and 4$0^{\circ}C$ , and was stable in the range of pH 4. 0 to 5.5 and temperature at 4$0^{\circ}C$, and 40 min, respectively The enzyme was inactivated by heating at 45$^{\circ}C$ for 1 hr. The enzyme was slightly activated by Mna+. Mg2+, but inhibited by Fea+. Km and activation energy was 1.5072 M and 8.314 kcal/mol.