• Korean Journal of Microbiology
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• v.30 no.6
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• pp.528-532
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• 1992

The ATP-dependent protease. Clp P from Esehaichia coli has been increase the stahility with or without detergent as Triton X-100 and NP-40 in the Clp P. The C]p P proteolytic activity was remained to 0.1 M salt by $Na^{-1}$, $K^{+}$, $Li^{+}$ but was inhihited by $SO_4^{2}$. An active ATPase site in Clp A is required for A TP-dependent proteolysis by Clp protease as

• Korean Journal of Microbiology
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• v.37 no.1
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• pp.15-20
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• 2001

In this study, we have isolated bacterial cell wall lytic enzyme in the culture supernatant of Aspergillus sp. HCLF-4. This hydrolase showed cell wall lytic activity against Anabaena cylindrica. The extracellular enzyme was produced by Aspergillus sp. HCLF-4 when it was grown in a PDB media containing 0.05% heat killed Micrococcus luteus cells. The molecular weight of lytic enzyme was about 14.3 kDa. The optimal pH and temperature for the activity of this enzyme were 3.0~4.0 and $30^{\circ}C$, respectively. This hydrolase activity was reduced by $Na^{+}$, $Li^{+}$, $Ca^{2+}$, $Cu^{2+}$, $Fe^{3+}$, EDTA, and PMSF, whereas it was increased by $Mg^{2+}$, $Mn^{2+}$>. The enzyme has N-acetylmuramyl-L-amidase or endopeptidase activity.

• Korean Journal of Microbiology
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• v.52 no.2
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• pp.236-241
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• 2016

The Schizosaccharomyces pombe $sdu1^+$ gene, belonging to the PPPDE superfamily of deubiquitinating enzyme (DUB) genes, was previously shown to encode a protein with ubiquitin C-terminal hydrolase (UCH) activity and to participate in the response against oxidative and nitrosative stresses. This work focused on the reactive oxygen species (ROS)-dependent regulation of the S. pombe $sdu1^+$ gene. UCH activities, encoded by the $sdu1^+$ gene, were attenuated in the S. pombe cells exposed to $H_2O_2$, superoxide radical-generating menadione (MD), and nitric oxide (NO)-generating sodium nitroprusside (SNP). Reduced glutathione (GSH) and its precursor N-acetylcysteine (NAC) were able to significantly enhance the UCH activities in the absence or presence of $H_2O_2$. However, the influences of both GSH and NAC on the ROS levels in the absence or presence of $H_2O_2$ were opposite to their effects on the UCH activities under the same conditions. The UCH activities in the Sdu1-overexpressing S. pombe cells were also diminished under exposure to $H_2O_2$, MD and SNP, but still remained to be higher than those in the vector control cells. In brief, it is proposed that the S. pombe $sdu1^+$ gene is regulated by ROS in a negative manner, the meaning of which largely remains elusive.

• Microbiology and Biotechnology Letters
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• v.14 no.6
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• pp.441-446
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• 1986

Some properties of extracellular guanine deaminase produced by Pseudomonas synxantha A3 were studied. The enzyme was stable at pH 6.5-7.5 and generally stable when it was incubated at 4$0^{\circ}C$ for 10 minutes but inactivated gradually above 4$0^{\circ}C$. When the enzyme in 0.2M potassium phosphate (pH 8.0) was stored at room temperature, it was stable for thirty days. Alcohols and acetone were not effective for the eyzyme stability. The optimum pH and temperature for the enzyme activity were around pH 7.0-8.0 and 5$0^{\circ}C$, respectively. The enzyme was inhibited by 1mM of Hg$^{++}$, Ag$^+$ and Li$^+$ and by 0.1mM of Ag$^+$ with about 50% loss of activity. The enzyme inhibited by Li$^+$ was reactivated by EDTA. 1 mM of pentachlorophenol and p-CMB inactivated the enzyme with 50% and 40% loss of activity, respectively. The enzyme inactivated by p-CMB was reactivated by glutathione.

• Korean Journal of Microbiology
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• v.27 no.3
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• pp.304-309
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• 1989

The effects of simazine [2-chloro-4, 6-bis(methylamino)-s-triazine] on in vivo nitrogenase, glutamine synthetase, glutamate synthase, and glutamate dehydrogenase which are important in nitrogen assimilation of Rhodopseudomonas sphaeroides were investigated. Simazine inhibited the synthesis of nitrogenase and glutamine synthetase. The activity of glutamine synthetase in crude extracts of Rhodopseudomonas sphaeroides is less inhibited by simazine than that of glutamate synthase and glutamate dehydrogenase. These results suggest the possibility that simazine inhibits photosynthetic activity and so inhibits the synthesis of nitrogenase and glutamine synthetase in Rhodopseudomonas sphaeroides.

• Microbiology and Biotechnology Letters
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• v.45 no.1
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• pp.81-86
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• 2017

Alignment of 967 reference sequences of the typical 2-Cys peroxiredoxin family of proteins revealed that 10 amino acids were conserved, with over 99% identity. To investigate whether the conserved aspartic acid residues and serine residue affect the peroxidase and chaperone activity of the protein, we prepared yeast TSA1 mutant proteins in which aspartic acids at positions 75 and 103 were replaced by valine or asparagine, and serine at position 73 was replaced by alanine. By non-reducing SDS-PAGE, TSA1 and the S73A, D75V and D75N mutants were detected in dimeric form, whereas the D103V and D103N mutants were detected in various forms, ranging from high molecular-weight to monomeric. Compared with wild type TSA1, the D75N mutant exhibited 50% thioredoxin peroxidase activity, and the S73A and D75V mutants showed 25% activity. However, the D103V and D103N mutants showed no peroxidase activity. All proteins, except for the D103V and D103N mutants, exhibited chaperone activity at $43^{\circ}C$. Our results suggest that the two conserved aspartic acid residues and serine residue of TSA1 play important roles in its thioredoxin peroxidase activity, and D103 plays a critical role in its chaperone activity.

• Microbiology and Biotechnology Letters
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• v.33 no.1
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• pp.24-28
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• 2005

A bacterial strain D­1 found to have potent fibrinolytic activity was isolated from Korean traditional Doenjang. It was identified as Bacillus sp. based on its 16S rRNA sequence analysis, morphological and physiological characteristics.

• Microbiology and Biotechnology Letters
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• v.31 no.2
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• pp.157-164
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• 2003

An alkali-tolerant bacterium producing the xylanase was isolated from soil and identified as Bacillus alcaiophilus. This strain, named B. alcalophilus AX2000, was able to grow and produce xylanase optimally at pH 10.5 and $37^{\circ}C$. The maximum xylanase production was obtained when 0.5%(w/v) birchwood xylan and 0.5%(w/v) polypeptone and yeast extract were used as carbon source and nitrogen source, respectively. The biosynthesis of xylanase was under the catabolite repression by glucose in the culture medium, and inhibited in the presence of high concentration of xylose. The maximum activity of xylanase was observed at pH 10.0 and $50^{\circ}C$ and the enzyme activity remained was over 80% at $60^{\circ}C$ and from pH 5.0 to 11.0.

• Microbiology and Biotechnology Letters
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• v.4 no.4
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• pp.138-144
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• 1976

five strains of Streptomyces spp. with high Productivity of glucose isomerase (15-30 units/ml) were obtained among 280 microbial strains isolated from 150 soil samples. These strains produced glucose isomerase with xylose as an inducer. These 5 strains were also identified to be different strains of Streptomyces spp.：streptomyces sp. K-14, K-53, K-71, K-77 and K-733. It was found that Streptomyces sp. K-14 produced the highest enzyme activity. The spore chains of these strains were rectiflexible and spore surface was smooth except Steptomyces sp. K-77 and K-733, with spiny surface.

• Korean Journal of Microbiology
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• v.28 no.3
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• pp.229-235
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• 1990

A rapid and sensitive method to detect the extracellular enzymatic activity of bacteria colonies grown on agar plates is described. Selective agar media supplemented with protein, starch, chitin, Tween-80, etc. are conventionally used to detect biochemical properties of bacteria. It has been experimentally demonstrated with bacteria pure cultures that fluorogenic Methylumbelliferyl (MUF)-substrates are excellent substrate analogues for normally occurring polymers. Based on MUF-substrate hydrolysis the new method provides reliable qualitative estimates of extracellular enzymatic properties of bacteria within minutes using pure cultures as well as agar p;ates prepared for colony counts. Extracellular enzyme activities of heterotrophic bacteria from freshwater ecosystems and marine sediment using this method are discussed.