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REFERENCE LINKING PLATFORM OF KOREA S&T JOURNALS
> Journal Vol & Issue
Journal of Microbiology and Biotechnology
Journal Basic Information
Journal DOI :
The Korean Society for Applied Microbiology and Biotechnology
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Volume & Issues
Volume 5, Issue 6 - Dec 1995
Volume 5, Issue 5 - Oct 1995
Volume 5, Issue 4 - Aug 1995
Volume 5, Issue 3 - Jun 1995
Volume 5, Issue 2 - Apr 1995
Volume 5, Issue 1 - Mar 1995
Selecting the target year
Effects of Mutations in the Regulatory Region on Transcriptional Regulation of glpD Gene
Jeong, Hee-Tae ; Choi, Yong-Lark ; Chung, Soo-Yeol ; Chung, Chung-Han ;
Journal of Microbiology and Biotechnology, volume 5, issue 5, 1995, Pages 245~249
Expression of the adjacent but divergently transcribed glpD and glpE gene is positively regulated by cAMP-CRP. In this study, we constructed several mutants in which a CRP-binding site is placed at different distances upstream of the glpD promoter. The effect of the spacer length on transcription activation by cAMP-CRP was tested in vivo by
-galactosidase. The cAMP-CRP complex activated transcription from glpD when bound at a number of positions, all of which lay on the same face of the DNA helix, although the degree of activation varied with the length of the spacer. By contrast, the insertion of spacer length with non-integral turns of the DNA helix extremely inhibited the activation of transcription. The observed transcription activation by cAMP of the glpD promoter was influenced by the distance between the CRP binding site and the transcription start point.
Cloning and Sequencing of the ddh Gene involved in the Novel Pathway of Lysine Biosynthesis from Brevibacterium lactofermentum
Kim, Ok-Mi ; Kim, Hyun-Jeong ; Kim, Dal-Sang ; Park, Dong-Chul ; Lee, Kap-Rang ;
Journal of Microbiology and Biotechnology, volume 5, issue 5, 1995, Pages 250~256
The ddh gene encoding meso-diaminopimelate (meso-DAP)-dehydrogenase (DDH) in Brevibacterium lactofermentum was isolated by complementation of the Escherichia coli dapD mutation. It was supposed from subcloning experiments and complementation tests that the evidence for DDH activity appeared in about 2.5 kb Xhol fragmented genome. The 2.5 kb Xhol fragment containing the ddh gene was sequenced, and an open reading frame of 960 bp encoding a polypeptide comprising 320 amino acids was found. Computer analysis indicated that the deduced amino acid of the B. lactofermentum ddh gene showed a high homology with that of the Corynebacterium glutamicum ddh gene.
Expression of Bacillus licheniformis
-amylase Gene in Lactobacillus casei Strains
Kim, Jeong Hwan ; Sung Hee Woo ;
Journal of Microbiology and Biotechnology, volume 5, issue 5, 1995, Pages 257~263
As a first step for developing Lactobacillus strains capable of fermenting starch directly, the
-amylase gene (amyL) from Bacillus licheniformis (Kim et al., 1988. Kor. J. Appl. Microbiol. Bioeng. 16: 369-373) was introduced into Lactobacillus casei strains and the level of
-amylase expression in transformants was examined. 3 kb EcoRI fragments encompassing amyL were subcloned into the suitable lactococcal cloning vectors (pSA3, pMG36e, and p1L2530) and then recombinant plasmids were introduced into E. coli and L. casei strains by electroporation. Only one recombinant plasmid,
was able to transform few L. casei strains tested at low efficiencies. The transformation efficiencies with the plasmid into L. casei YIT 9018 and L. casei A Tee 4646 were less than
g pIL2530\alpha$. The level of amylase activities in L. casei was five to ten-fold lower than that in E. coli cells.
was stably maintained in Lactobacillus strains in the presence of Em (5
g/ml) but without antibiotic selection, it was unstable so more than 95
of cells lost plasmids after a week of daily subculturing.
Screening for Inhibitor of c-myc Expression and Identification of Isolate No.2303
Chung, Ji-Hyung ; Yeo, Ick-Hyun ; Oh, Doo-Whan ; Moon, Soon-Ok ;
Journal of Microbiology and Biotechnology, volume 5, issue 5, 1995, Pages 264~268
Sulforhodamine B(SRB) assay was performed on the human lung carcinoma, A549 cell line to screen soil microorganisms for production of anti-cancer agent. Among 4, 265 microorganisms, 45 isolates were selected for their cytotoxicity and tested for their effects on the expression of c-myc by RNA slot blot and Northern blot analysis resulting in selection of No.2303 isolate. This No.2303 was identified as Streptomyces sp. by ISP classification and the chemotaxonomic analysis method. NO.2303 inhibited the expression of cmyc in Col0320 DM and A549 cell lines. The culture extract of No. 2303 also inhibited the progression of the cell cycle of Go in NIH 313 cells, implying that the extract also inhibited the expression of c-myc in NIH 313 cell.
Purification and Characterization of A Thermotolerable Restriction Endonuclease from Streptomyces violochromogenes D2-5
Yun, Mi-Sub ; Hwang, Hye-Yeon ; Bae, Moo ;
Journal of Microbiology and Biotechnology, volume 5, issue 5, 1995, Pages 269~273
A thermotolerable restriction endonuclease. Svil, found in Streptomyces violochromogenes D2-5 was purified. For the purification, streptomycin sulfate and ammonium sulfate precipitation was used. Ph osphocellulose P-ll, DEAE-Cellulose and Sephacryl-S200 HR colum chromatography were also performed. The purified enzyme was found to be homogeneous and the molecular weight of the enzyme estimated by polyacrylamide gel electrophoresis containing 0.1
SDS was about 32, 000 daltons. The recognition sequence and cleavage site of the enzyme were determined to be
which is the same sequence as that of Asull. Unlike Asull, however, the Svil shows high thermal stability.
Purification and Properties of Extracellular Esterases of Aspergillus oryzae which synthesize Ethyl Caproate
Lee, Jong-Hoon ; Sato, Toshitsugu ; Kawai, Yuri ; Enei, Hitoshi ;
Journal of Microbiology and Biotechnology, volume 5, issue 5, 1995, Pages 274~279
Ethyl caproate, one of the major flavor compounds deciding the quality of sake (Japanese wine), is produced during the brewing by the action of alcohol acyltransferase and esterases of sake yeast and koji mold. Extracellular esterases of Aspergillus oryzae required for ethyl caproate synthesis were purified partially. The enzymes had different optimum pH and affinity toward substrates. Substrate preferences and inhibition features showed the three enzymes to be B-type esterases or carboxylesterases (EC 18.104.22.168).
Occurrence of OF494911 in the Fungal Mat formed by Surface Culture of Aspergillus niger F-580
Chun, Hyo-Kon ; Chung, Myung-Chul ; Ko, Hack-Ryong ; Lee, Ho-Jae ; Kho, Yung-Hee ;
Journal of Microbiology and Biotechnology, volume 5, issue 5, 1995, Pages 280~284
Aspergi11us niger F-580, a potent producer of aminopeptidase M inhibitor, was isolated from the brown spots of plant leaves with a pathological trait. The inhibitory activity was found only in the fungal mat formed by surface culture of Aspergi11us niger F-580, but not in the culture supernatant or cell pellet. The inhibitor was purified from the hot water extract of this fungal mat by using chromatographies on Diaion HP-20, DEAE-cellulose, Sephadex G-l0 and YMC-ODS-AQ columns. The purified inhibitor was analyzed by UV, mass, and NMR spectroscopies, and identified as OF494911, which had been isolated as an aminopeptidase B inhibitor from Penicillium rugulosum OF4949
Fermentation Conditions for the Production of Cell Mass and Comparison of Saccharide Utilization in Bifidobacterium longum and B. breve
Hyun Hyung Hwan ; Hyune Hwan Lee ; Kwan Park ; Joo Hee Lee ; Ick Hyun Yeo ; Tae Seok Kim ;
Journal of Microbiology and Biotechnology, volume 5, issue 5, 1995, Pages 285~291
Saccharide utilizations for the growth by Bifidobacterium longum and Bifidobacterium breve were compared. B. longum fermented glucose more rapidly than lactose as a carbon source whereas B. breve fermented lactose at a rate higher than that of glucose. The highest cell concentration, in the case of B. longum, was obtained when cultivated in a jar fermentor that contained modified MRS medium that half the beef extract was replaced by the same amount of tuna extract, and that pH was controlled at 6.0. B. breve showed the best growth when grown in a jar fermentor containing the MRS medium with lactose instead of glucose, controlled at pH 6.0. The optimal concentration of peptone in MRS medium for the growth of B. breve was 5 g/l.
Production of Poly(
-hydroxyvalerate) by Two-stage Fed-batch Fermentation of Alcaligenes eutrophus
Lee, In-Young ; Kim, Guk-Jin ; Shin, Yong-Cheol ; Chang, Ho-Nam ; Park, Young-Hoon ;
Journal of Microbiology and Biotechnology, volume 5, issue 5, 1995, Pages 292~296
Production of poly(
-hydroxyvalerate)[poly(HB-co-HV) from glucose and propionic acid was studied in a two-stage fed-batch fermentation using Alcaligenes eutrophus NCIMB 11599. When either glucose became sufficient or the feeding rate of propionic acid decreased, production of poly(HB-co-HV) increased but concomitantly resulted in a reduced fraction of HV. During the copolymer accumulation stage, the specific production rate of hydroxyvalerate (HV) increased up to 0.013 (g-HV/g-RCM/h) but it decreased as propionic acid was accumulated. Control of the propionic acid concentration in the medium, therefore, is considered to be one of the most important operating parameters for production of poly(HB-co-HV) with a higher HV fraction. A high titre of poly(HB-co-HV) (85.6 g/I) with HV fraction of 11.4 mol
could be obtained in 50 h by controlling the propionic acid concentration at 1 to 4 g/I.
Improved Production, and Purification of Aclacinomycin A from Streptomyces lavendofoliae DKRS
Kim, Wan-Seop ; Youn, Deok-Joong ; Cho, Won-Tae ; Kim, Myung-Kuk ; Kim, Hak-Ryul ; Rhee, Sang-Ki ; Choi, Eui-Sung ;
Journal of Microbiology and Biotechnology, volume 5, issue 5, 1995, Pages 297~301
An anthracycline antibiotic, aclacinomycin A (aclarubicin), was produced from a mutant strain of Streptomyces lavendofoliae. The mutant strain which showed a 4-fold higher productivity of aclacinomycin A compared with the parent strain was also found to produce a significantly higher amount of aclacinomycin A than the reported production strain, Streptomyces galilaeus. The aclacinomycin A was produced up to 125 mg/l using potato starch and soybean meal as carbon and nitrogen sources, respectively, on a 3 liter scale fermentation in a 5 liter jar fermentor. The mutant strain also produced significant amount of aclacinomycins Band Y. Aclacinomycin A was isolated from the culture broth by solvent extractions and further purified by silica gel column chromatography. The yield of aclacinomycin A with over 99
purity was found to be over 60
starting from 3 liters of culture broth.
A New HPLC Condition for the Analysis of Aclacinomycins A and Y in the Mixtures of Aclacinomycins
Kim, Wan Seop ; Won Tae Cho ; Myung Kook Kim ; Sang Ki Rhee ; Hak Ryul Kim ; Eul Sung Choi ;
Journal of Microbiology and Biotechnology, volume 5, issue 5, 1995, Pages 302~304
As the previous HPLC method (Ogasawara et al., 1983) was described for the analysis of aclacinomycin A and some of its analogue compounds but not for aclacinomycin Y, we developed novel HPLC condition by optimizing solvent system. The newly developed solvent system allowed a complete separation of aclacinomycins Y and A, as opposed to the incomplete resolution of these two compounds in conventional method. The amounts of aclacinomycins Y and A could be accurately determined when the fermentation broth of Streptomyces lavendofoliae DKRS was analyzed by the newly developed method.
Isolation of the Threonine Dehydratase Gene from a Tylosin-Producing Strain of Streptomyces fradiae
Lee, Sang Hee ; Kye Joon Lee ;
Journal of Microbiology and Biotechnology, volume 5, issue 5, 1995, Pages 305~308
From the plasmid library made from Sstl and San-digested genomic DNA of Streptomyces fradiae NRRL 2702, four positive clones were selected using an oligodeoxynucleotide probe from the N-terminal amino acid sequence of purified threonine dehydratase. The cloned gene for threonine dehydratase was a 2.0 kilo-base pair DNA fragment. The deduced amino acid sequence of PCR product (PCR245) was matched to that of the N-terminal part of threonine dehydratase from S. fradiae and this showed a high similarity to the threonine dehydratases of other organisms. This indicated that amino acid sequences of threonine dehydratases were highly conserved and the polypeptide product of the PCR245 was likely to be involved in the deamination of threonine.