• Microbiology and Biotechnology Letters
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• v.10 no.4
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• pp.283-288
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• 1982

Trypsin inhibitor produced by Streptomyces sp. was investigated its reactive characteristics against trypsin. The mode of inhibition against trypsin was mixed type of non-competitive and competitive with casein, and enzyme-inhibitor complex was formed rapidly. The inhibitory activity was increased by the addition of isoleucine and depressed by silver, mercuric or cupric ion. And when egg albumin or hemoglobin was used as substrate for trypsin, the inhibition ratio was changed. The inhibitor inhibited coagulation of blood of bovine.

• Journal of Microbiology
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• v.40 no.1
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• pp.20-25
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• 2002

An extracellular PHB depolymerase was purified from P. simplicissimum LAR13 cultural medium by Sepharose CL-6B chromatography. When the fungus was grown in a basal salt medium with poly(3-hydroxybutyrate) (PHB) as the sole carbon source, PHB depolymerase production reached maximum at its stationary phase. The mycelial growth rate was higher at 37$^{\circ}C$ than at 30$^{\circ}C$ and even higher than at 25$^{\circ}C$, However, the enzyme production was lower at 37$^{\circ}C$ than 30$^{\circ}C$ or 25$^{\circ}C$. The isolated enzyme is composed of a single polypeptide chain with a molecular mass of about 36 kDa as determined by SDS-PAGE. The optimum conditions for the enzyme activity are pH 5.0 and 45$^{\circ}C$. The enzyme was stable for 30 min at a temperature lower than 50$^{\circ}C$, and stable at pH higher than 2.0 but it was unstable at pH 1.0.1 mM Fe$\^$2+/ reduced the enzyme activity by 56% and the enzyme was inhibited almost completely by 4 mM Fe$\^$2+/ . The enzyme was partially inhibited by phenylmethylsulfonyl fluoride and was very sensitive to diazo-DL-norleucine methyl esters dithiothreitol and mercuric ion. However, N-p - tosyl - L - Iysinechloromethyl ketone, p -hydroxymercuricbenzoate and N- acetylimidazole had no influence upon its activity.

• Journal of Microbiology and Biotechnology
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• v.5 no.4
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• pp.206-212
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• 1995

A strain BL-29, which produces a extracellular lytic enzyme on E. coli was isolated from the soil. The strain was identified as belonging to the genus Bacillus sp. The lytic enzyme was purified to homogeneity by ion exchange chromatography and gel filtration. Specific activity of the purified enzyme was 28, 850 U/mg protein and yield of the enzyme was 5$%$. The purified enzyme showed a single band on SDS-PAGE and its molecular weight was estimated to be 31, 000 by SDS-polyacrylamide gel electrophoresis and gel filtration column chromatography. The optimum temperature and pH were $55^{\circ}C$ and pH 10.0, respectively. The enzyme was stable at $45^{\circ}C$ but enzyme activity was reduced by up to 50$%$ when the temperature was raised to $55^{\circ}C$ for 15 min. Stable range of pH was from 5.0 to 11.0. but Enzyme activity was inhibited by lead-acetate, mercuric chloride, ethylene glycol-bis-[$\beta$-aminoethyl ether]-N, N, $N^1, $N^1$-tetraacetic acid (EGTA), and ethylenediamine tetraacetic acid (EDTA), but not affected considerably by treatment with other chemical reagents.

• Journal of the Korean Chemical Society
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• v.19 no.6
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• pp.428-433
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• 1975

500 ml of a sample water was extracted with 10 ml of 0.01 % dithizone-$CHCl_3$three times. When $CHCl_3$ layer was back extracted with 10 ml of 0.1 N HCl containing mercuric ion, the free metal ions come into aqueous layer. The aqueous layer was added with 2 ml of 2 N KCl and was washed with 10 ㎖ of $CHCl_3$two times in order to remove the trace dithizone, and then was recorded square wave polarogram. The concentration of copper, lead and cadmium can be determined up to 3 ppb and that of zinc up to 14 ppb with an error of 10 %.

• Journal of Life Science
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• v.20 no.6
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• pp.838-844
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• 2010

A fibrinolytic enzyme of Streptomyces corcohrussi from soil sediment was purified by chromatography using DEAE-Sephadex A-50 and Sephadex G-50. The analysis of SDS-polyacrylamide gel suggested that the purified enzyme is a homogeneous protein and the molecular mass is approximately 34 kDa. The purified enzyme showed activity of 0.8 U/ml in a plasminogen-rich fibrin plate, while its activity in a plasminogen-free fibrin plate was only 0.36 U/ml. These results suggested that the purified enzyme acts as a plasminogen activator. The fibrinolytic activity of the enzyme under the supplementation of protease inhibitors, $\varepsilon$-ACA, t-AMCHA and mercuric chloride in the enzyme reaction was less than 24%, indicating that it could be modulated by the plasmin and/or fibrinogen inhibitors involved in the fibrinogen-to-fibrin converting process. As time passed, $Zn^{2+}$, a heavy metal ion, inhibited the activity to 34.1%. The optimum temperature of the purified enzyme was approximately $50^{\circ}C$ and over 92% of the enzyme activity was maintained between pH 5.0 and 8.0. Therefore, our results provide a potential fibrinolytic enzyme as a noble thrombolytic agent from S. corcohrussi.

• Journal of Environmental Science International
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• v.22 no.6
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• pp.705-715
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• 2013

The response of the freshwater microalga Chlorella vulgaris to mercuric ion ($Hg^{2+}$) stress was examined using chlorophyll a fluorescence image analysis and O-J-I-P analysis as a way to monitor the toxic effects of mercury on water ecosystems. The levels of photosynthetic pigments, such as chlorophyll a and b and carotenoids, decreased with increasing $Hg^{2+}$ concentration. The maximum photochemical efficiency of photosystem II(Fv/Fm) changed remarkably with increasing $Hg^{2+}$ concentration and treatment time. In particular, above $200{\mu}M\;Hg^{2+}$, considerable mercury toxicity was seen within 2 h. The chlorophyll a fluorescence transient O-J-I-P was also remarkably affected by $Hg^{2+}$; the fluorescence emission decreased considerably in steps J, I, and P with an increase in $Hg^{2+}$ concentration when treated for 4 h. Subsequently, the JIP-test parameters (Fm, Fv/Fo, RC/CS, TRo/CS, ETo/CS, ${\Phi}_{PO}$, ${\Psi}_O$ and ${\Phi}_{EO}$) decreased with increasing $Hg^{2+}$ concentration, while N, Sm, ABS/RC, DIo/RC and DIo/CS increased. Therefore, a useful biomarker for investigating mercury stress in water ecosystems, and the parameters Fm, ${\Phi}_{PO}$, ${\Psi}_O$, and RC/CS can be used to monitor the environmental stress in water ecosystems quantitatively.

• Applied Biological Chemistry
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• v.12
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• pp.25-31
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• 1969

The characteristics of crude enzyme produced from Trichoderma viride($O_2-1$) which isolated from half spoiled Locust acacia wood (Robinia Pseudacacia Linne) were examined in this paper. The results obtained were summarized as follows: 1) As a results of enzymatic action on several cellulose substrate it was found that there were some sorts of cellulase in crude enzyme. 2) The activity of C.M.C. ase and ${\beta}-glucosidase$ were decreased in accordance with increasing concentration of substrate, and filter paper saccharifying enzyme relatively increased in accordance with increasing concentration of substrate and enzyme in couse of time. 3) The optimal pH of each enzyme was 5.0 and the range of stability on pH generally from 3 to 6. 4) In disintegrating activity on filter paper, in decomposing activity on C.M.C. and $p-nitrophenyl-{\beta}-D-glucoside$, and in saccharifying activity on filter paper, the optimal temperatures were $50^{\circ}C.,\;60^{\circ}C,\;and\;65^{\circ}C$. 5) The order of stability on temperature was as follow; saccharifying activity on filter paper decomposing activity on C.M.C. disintegrating activity on filter paper>decomposing activity on $p-nitrophenyl-{\beta}-D-glucoside$. 6) The activity of the enzymes was inhibited with mercuric and silver ion, and activated with potassium.