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REFERENCE LINKING PLATFORM OF KOREA S&T JOURNALS
> Journal Vol & Issue
The Korean Journal of Microbiology
Journal Basic Information
Journal DOI :
The Microbiological Society of Korea
Editor in Chief :
Volume & Issues
Volume 30, Issue 6 - Dec 1992
Volume 30, Issue 5 - Oct 1992
Volume 30, Issue 4 - Aug 1992
Volume 30, Issue 3 - Jun 1992
Volume 30, Issue 2 - Apr 1992
Volume 30, Issue 1 - Feb 1992
Selecting the target year
Bacillus licheniformis SSA3-2M1 이 생산하는 Proteinases
The Korean Journal of Microbiology, volume 30, issue 4, 1992, Pages 239~245
Buci1llr.s 11c~h~n~1rnSiSi.As 3-2MI which is responsible for the special taste of traditionalKorean soy sause produced two kinds of proteinase. The activity of the proteinasc I washigher about two fold than that of proteinase 11. The optimai, reaction pH of proteinaseI and I1 wcre found to be 7-1 1.5 and 7-9. respectively. Proteinase I1 was more stable andactive than proteinase I at pH ranges around 3 to 5. The optimal te~tlperature of proteinaseI and I1 were 502. The temperature stabilitl of proteinase I1 was Inore stable thanproteinase 1 at temperature range around 30-quot;~A. ctivities of proteinase I and I1 graduallydeclined above
C and 45C. respectively. Proteinasc 1 was more active than proteinaseI1 at salt concentration range around 25-3500. The K,,, values of casein and soy proteinfor proteinase I were 6.89 mglml and 3.98 mglml. In case of proteinase 11. they were 9.00mgiml anti 11.44 111g/ml. respectively. The activity of the crudc enzyme was increased by1 rnM Pb(CH3COO). but was decreased by 5 n1M and 10 rnM of HgS04 and ZnS04. Thetwo proteinases produced amino acids and peptides from the soybean protein. The peptideswere digested into amino acids. Both protcinases were found to be the main enzymes thatproduced amino acids which make the main taste of traditional Korean soy sauce.al Korean soy sauce.
Molecular Cloning of nod Genes from Bradyrhizobium sp. SNU001
The Korean Journal of Microbiology, volume 30, issue 4, 1992, Pages 246~251
Molccular cloning of nod genes from Bradvrhizobium sp. SNU001, a nitrogen-fixing symbiont isolated from thc root nodules of soybean (Clycine trim) . was carried out. nod genes were found to be located on thc genome of the symbiont by gcnomic hybridization with 4.5 kb EcoRI/HndIII fragment (nod DABC) of Rhizohium meliloti as probe. Genomic library of this symbiont was constructed using h phage EMBL3-BanlHI vector. from which five nod positive clones were sclectcd by primary and secondary screening methods. The partial restriction map of inserted genomic DNA of h CNS-l(c1one 2) was constructed. and 3.9 kh Bun7HI fragment. which showed strong hybridization signal to the probe, was subcloned into pBS KS(+) plasmid vector. Partial restriction inap ot' a selected subclone (pBjCNS-I) was constructed and nod DABC was found to be located on the 1.8 kb KpnI/Sacl fragment of this subclone.
Characterization of Laccase Excreted from Lentinus edodes
The Korean Journal of Microbiology, volume 30, issue 4, 1992, Pages 252~259
Extracellular laccase excreted from Lentinus edodes ATCC 48085 was purified through a series of DEAF, Sephadex A-50. Con A-Sepharosc and Sephadex G-150 chromatography. Extracellular enzyme. which consists of a single polypeptide, has a n~olecular mass of 87.000 daltons and contains 12.0'%, carbohydrate. The N-terminal amino acid sequence (I5 residues) of the puritied enzyme was similar to that of laccases of PIeurotus ostreatus and Coriolus hirsutus. The enzyme showed optimal activity at near pH 4.8 and
. The enzyme was stable at pH 7-9 and below
values for syringaldazine were estimated to be
and 77 sec, respectively. The developed patterns of reaction products of thevenzyme on thin layer chromatography were similar to those of laccase of Pleurotus ostreatus
2, 4, 5-Trichlorophenoxyacetic Acid 분해균의 유전적 특성에 관한 연구
The Korean Journal of Microbiology, volume 30, issue 4, 1992, Pages 260~264
Pseudotnorju.c sp. EL-071P degrading 2.4.5-trichlorophe~~oxyi~cetaicci d (2.3.5-T) was resistantto antibiotics: rifampicin. ampicillin. kanamycin and metal ions : Zn" and Cu".The plasmitl related to the degradation of 2.4.5-'r and rifa~npicin resistance was isolatecifrom the strain. Its size was about 40 Kb. As result of transforming the plasmid intoEsch~rirhiti coli MClOhl, it was confirmed that the plasmid ura.; related to 2.4.5-T degradation.The strain coulil grow in the various chlorinated aromatic analogs as the solc carbon source.In the case of chlorophcnols. the chlorinated mono-substituteti phenols were easily dcgradetlin the order ol' ortho-. ~ ~ a r um- ,c ~tu-position.T he 2.3.5-T mctaholism was inhibited by 4-chlorophenol of 2.4.5-7' analog. In non-chlorinateci aromatics. ~ C I I L O ~ I ~ Csa.l icylilte i~ndtoluene were uscd ax the carbon source by the strain and typestrain Acudonlotrtr.\ plrtirltrKCTC 1643 having clegrad;~bility of various aromatics. But naphtalene was usecl only bythe A~urlomonri.\ sp. EL-07 1 P.the A~urlomonri.\ sp. EL-07 1 P.
Bacteriocins in Purple Nonsulfur Bacteria
Lee, Sang Seob ; Oh, Tae Jeong ; Lee, Hyun Soon ;
The Korean Journal of Microbiology, volume 30, issue 4, 1992, Pages 265~268
In this study, we want to detect bacteriocin production in purple nonsulfur bacteria. As a results, it was showed that bacteriocin produced between some strains of Rhodobacter capsulatus, Rhodobacter sphaeroides and Rhodocyclus gelatinosus. In particular, it was appeared that cell membrane-bound bacteriocin was also produced by Rhodobacter capsulatus ATCC 17016
Evidence for two
Antiport Systems in Escherichia coli
Seo, Sung-Yum ;
The Korean Journal of Microbiology, volume 30, issue 4, 1992, Pages 269~277
Several insertion mutants of Escherichia coli in the ant gene, coding for
antiport activity, showed littel, if any, reduction in the antiport activity.
dependent transport activity also remained at wild type level. These facts led to the idea that E. coli has evolved at least two distinct systems for extrusion of
The antiport activities were studied under various conditions to reveal different properties of these systems. For convenience these activities are referred to as major and minor activities. The distinguishing properties of the two systems include : kinetics (Km, Vm) at pH 7.8, competition pattern between
, pH profiles, pattern of the change in kinetic parameters as a function of pH, and sensitivity to protease, chemicals and heat.
Numerical Identification of a Streptomyces Strain Producing Spores in Submerged Culture
Rho, Yong-Taik ; Kim, Hyoung-Tae ; Oh, Kyoung-Hee ; Kang, Heui-Il ; Alan C. Ward ; Michael Goodfellow ; Hah, Yung-Chil ; Lee, Kye-Joon ;
The Korean Journal of Microbiology, volume 30, issue 4, 1992, Pages 278~285
Chemotaxonomic and numerical identification were carried out for a isolate of Streptomyces strain SMF301 producing spores in submerged culture. Fifty taxonomic unit characters were tested and the data were analyzed numerically using the TAXON program. The isolate SMF301 was identified to cluster 1A of Streptomyces and best matched to Streptomyces limosus which is a synonym of Streptomyces albidoflavus. Therefore, it was concluded that the isolate was identified to be a member of Streptomyces alidoflavus.
Identification of Fluorescent Pseudomonads Producing Siderophore and Construction of Siderophore Biosynthesis Defective Mutant
Park, Yeal ; Kim, Hyun Hee ; Myeong-gu Yeo ; Young-woo Seo ; Han-cheol Koh ; Young-gi Yang ; Hyeon-Sook Cheong ; Sung-jun Kim ;
The Korean Journal of Microbiology, volume 30, issue 4, 1992, Pages 286~290
The present study was performed to isolate the fluorescent pseudomonads from Kwang-Ju soil and to construct a mutant strain defective in siderophore biosynthesis. The siderophore-secreting pseudomonads were screened on Blue agar (Chrome Azuol S agar) plates and one strain of them was designated to Pseudominas fluorescens (P. fluorescens) PY002. To construct a mutant defective in siderophore biosynthesis, P. fluorescens PY002 was randomly mutagenized with a transposon Tn5. The location of Tn5 integrated into chromosomal of the mutants strain was determined by Southern blot analysis. The mutagenized strain showed non-fluorescent on a King's B agar plate and were defective in iron (III) acquisition ability.
Streptomyces coelicolor 의 Catalase 들의 분석
The Korean Journal of Microbiology, volume 30, issue 4, 1992, Pages 291~298
Srrepromycec. corlirolar produces at least 4 catalase activity bands with different electrophoretic mobilities on polyacrylamide gel which vary during development. Spores and mycelia at stationary phase produced all the activity bands(Cat1. 760 kr); Cat3-I, 170 kD: Cat3-2, 140 kD: Cat3-3. 130 kD; Cat4, 70 kD) except for Cat2 (300 kD). Mycelia at mid-logarithmic phase produced only Cat2 and Cat3-2 bands, and mycelia at late-logarithmic phase produced bands except Catl and Cat\ulcorner. Catalase-deficient mutants were screened in S. coelicalur by H201 bubbling test following NTG mutagenesis. Wc tested sevcral non-bubbling or slow-bubbling mutants for their catalase activities. The overall activities in cell extracts decreased more than 5 fold. Activity bands in native gel selectively decreased in intensity or disappeared. In all the non-bubbling mutants testcd, Cat3-2 band decreased significantly or disappeared. suggesting that Cat3-2 is the major catalase. The selective disappearance of bands in mutants suggest that each band is governed by different genes. We purified catalase activity from -:ell extracts obtained at late-logarithmic phase. Following chromatographies on Sepharose CL-4B. DEAE Sepharose CL-6B. Phcnyl Sepharose CL-4B. and hydroxylapatite columns. only the Cat3-2 activity was obtained. The native form of Cat3-2 has molecular weight of approximately 140 kD, judged by gel electrophoresis. Thc electrophoretic mobility on SDS-polyactylamide gel suggests that this enzyme contains 2 identical subunits of 67 kD.
Purification and Characterization of an Intracellular Protease form Pseudomonas carboxydovorans DSM 1227 Grown on Carbon Monoxide
Ho, Bae-Ki ; Kim, Young-Min ;
The Korean Journal of Microbiology, volume 30, issue 4, 1992, Pages 299~304
An intracellular protease form cells of Pseudomonas carboxydovorans DSM 1227 grown on carbon monoxide was purified 57-fold in six steps to homogeneity with a yield of 4.3% using azocoll as a substrate. The molecular weight of the enzyme was determined to be 150,000. Sodium dodecyl sulfate-gel electrophoresis revealed the purified enzyme to be a dimer with two identical subunits of molecular weight 72,000. The enzyme was stimulated by
but was inhibited completely by
The enzyme activity was also inhibited by EDTA, EGTA, phenylmethylsulfonyl fluoride, and phenyl glyoxal, but was increased by 1-ethyl-3(dimethyl aminopropyl fluoride, and phenyl glyoxal, but was increased by 1-ethyl-3(dimethyl aminopropyl)carbodiimide, iodoacetamide and dithiothereitol. The optimal pH and temperature for the enzyme reaction were found to be 7-8 and 50.deg.C, respectively. Casein and bovine serum albumin were hydrolyzed by the enzyme, but carbon monoxide dehydrogenase was not.
Bacillus stearothermophilus 에서 부분 정제한 Cytosine Deaminase 의 특성
The Korean Journal of Microbiology, volume 30, issue 4, 1992, Pages 305~309
Cytosine deaminase (EC 184.108.40.206) from BaciNus stc~urorhermophilus was partially purified 7.2-fold with an overall yield of 52.7%. The partially purified enzyme deiiminated cytosine only.but not 5-methylcytosine and 5-fluorocytosine. The apparent Michaclis constant. Km valuefor cytosine was 5.9 mM. The enzyme was relatively stable in the range of pH 4.0 to 7.0.furthermore extremely thermo-stable : more than 75'X) of the activity was remained afterheating at 80
C for I0 min at pH 6.5. The enzyme had a pH optimum at around pH7.0 to 7.5. and temperature optimum at 35 to 31
C. And the activation energ (En value)determined from an Arrhenius plot was 26 Kcal/mol. The enzyme activity was stronglyinhibited by heavy metal ions such as Cd", Hg". Cut' at 1 mM, anJ by o-phenanthroline,and p-chloromcrcuribcnzoate at I mM. But the enrymc activity was activatetl increased byGMP, and CMP at 1 mM.ased by GMP, and CMP at 1 mM.
The Uptake of Lead Ion with Staphylococcus epidermidis
The Korean Journal of Microbiology, volume 30, issue 4, 1992, Pages 310~315
from aqueous solution was studied using Staphylococcus epidermidis. Cells of exponential phase were employed as absorbents. Uptake ratio defined as the ratio of amount of
absorbed to that of initial
. Absorption of
increased with increase in cell concentration. while amount of
per unit cell mass decreased. Uptake ratio of
augmented and then diminished after exhibiting a maximum as the pH of the solution increased. Equilibrium absorption of
deviated from Freundlich isotherm especially at higher concentration of
due to the precipitation phenomena. HCI and EDTA were founded to desorb
more effectively than
. After 10 cycles of absorption and desorption.
absorption capability remained almost unchanged and the biomass had leaked out 30-40 wt/%. Uptake ratio of Pb2+ decreased in the presence of other heavy metal ions due to the competitive absorption The inhibition of
absorption appeared to have a strong correlation with ionic radius of the competing ions. Especially
having smaller ionic radius depressed more significantly the uptake of
than any other metal ions tested.
Molecular Cloning and Characterization of Catechol 2, 3-Dioxygenase Gene from Aniline-Degrading Psseudomonas acidovorans
Lee, Ji-Hyun ; Bang, Sung-Ho ; Park, Youn-Keun ; Lee, Yung-Nok ;
The Korean Journal of Microbiology, volume 30, issue 4, 1992, Pages 316~321
Catechol 2, 3-dioxygenase (C230) catalyses the oxidative ring cleavage of catechol to 2-hydroxymuconic semialdehyde. This is one of the key reactions in the metabolism of the widespresd pollutant aniline. We have cloned a gene encoding C230 from cells of the aniline degrading bacteria, Pseudomonas acidovorance KCTC2494 strain and expressed in E. coli, A 11.3-kilobase Sau3A partial digested DNA fragment from KCTC2494 was cloned into phagemid vector pBluescript and designated as pLP201. The C230 gene was mapped to a 2.8-kb region, and the derection of transcription was determined. The cloned C230 gene contains its own promoter which can be recognized and employed by E. coli transcriptional apparatus. C230 activities of subclones were identified by enzyme assay and activity staining. The T7 RNA promoter/polymerase system and maxicell analysis showed that a polypeptide with Mw of 35 kDa is the C230 gene product.
유전공학기법으로 변형시킨 내성유전자네 대한 수질환경에서의 전이동태
The Korean Journal of Microbiology, volume 30, issue 4, 1992, Pages 322~331
In order to understand the transfer and behavior of R gene in water environments. the Kmr gene in the genetically modified microorganisms(GMMs) w,is studied by conjugation. The plasmid variously rearranged in the conjugants were comparatively analyzied by agarosc gel electrophoresis and the specific Km' genes in the gel were tletected with DNA probe. The Kmr genes of the GMM strains(DKC600 and DKC601) were transferred at higher rate than those of natural isola~e(DKI)b, ut the ratc was a little diflurent depending upon the recipient strains. Rearrangement of the plasmids appeared morc drastic in GMM strains than in IIKI as donor. The transfer frequencies of the Km' genes in LR broth were remarkably higher than in the water of AW and FW without regards to the strains. In LA breth. the frequencies of Kmr genes were higher at 25'C-30
C than at 10
C and at pH - 7 than pH 9, but temperature and pH of the FW did n,,t affect to the frequency. And the conjugants from GMM strains in FW did not showed any plasmids. except tor 43 kb plasmiil. As results of Southern analysis of the plasmid, variously rearranged in eonjugant cells obtained in LB broth, the Kmr genes were detected at the same position of Km' plasrnids of the donor cell(DK1 and GMM strains). But Km' plasmid disappeared in the conjugants obtained in F'W and their chronlosomes showed strong signal of hybridization. The Kmr plasmid of DKl in the conjugants obtained in FW water was transferred and maintained its size, but the Kmr plasinids of the GMM strains were all integrated into chromosome. Therefore, the Kmr plasmids of DKI anit GMM strains in LH were intactly transferred and other plasmitls were variously rearranged. but Km' gene of DKC600 in FW water was integrated into the chromosorn: without regards to the temperature and pH of the water.