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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
Editor in Chief :
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
Selection of the Constitutive Mutant of Bacillus firmus var. alkalophilus and its Characteristics of Cydodextrin Glucanotransferase Production
Lee, Yong-Hyun ; Kim, Chan ; Lee, Yong-Hyun ;
Journal of Microbiology and Biotechnology, volume 5, issue 2, 1995, Pages 61~67
To investigate the role of induction on CGTase production for alkalophilic Bacillus firm us var. alkalophilus H609, the constitutive mutants that form a halo around its colonies at non-inducible AG agar media containing amylose and glucose were selected. The selected constitutive mutants could produce CGTase in the range of 18.9 to 28.8 units/ml
in the alkaline basal medium, and finally a constitutive mutant Bacillus firmus var. alkalophilus CM46 was selected. The constitutive nature of CM46 was also confirmed in protein level using SDS-PAGE. The effects of induction and catabolite repression for both parent strain Bacillus firmus var. alkalophilus H609 and constitutive mutant CM46 were also compared by adding soluble starch and glucose during cultivation. The selected mutant CM46 was a non-inducible but a catabolite regulated type mutant. Even though inductive regulation was released, the specific CGTase activity defined as CGTase activity per cell concentration was not increased compared with that of parent strain. The cell growth and CGTase production patterns of constitutive mutant Bacillus firmus var. alkalophilus CM46 were compared with the parent strain to identify CGTase production characteristics.
Cloning and Expression of pcbC and pcbD Genes Responsible for 2,3-Dihydroxybiphenyl Degradation from Pseudomonas sp. P20
Nam, Jung-Hyun ; Oh, Hee-Mock ; Kim, Chi-Kyung ;
Journal of Microbiology and Biotechnology, volume 5, issue 2, 1995, Pages 68~73
Pseudomonas sp. P20 was shown to be capable of degrading biphenyl and 4-chlorobiphenyl (4CB) to produce the corresponding benzoic acids wnich were not further degraded. But the potential of the strain for biodegradation of 4CB was shown to be excellent. The pcbA, B, C and D genes responsible for the aromatic ring-cleavage of biphenyl and 4CB degradation were cloned from the chromosomal DNA of the strain. In this study, the pebC and D genes specifying degradation of 2, 3-dihydroxybiphenyl (2, 3-DHBP) produced from biphenyl by the pebAB-encoded enzymes were cloned by using pBluescript SK(＋) as a vector. From the pCK102 (9.3 kb) containing pebC and D genes, pCK1022 inserted with a EcoRI-HindIII DNA fragment (4.1 kb) carrying pebC and D and a pCK1092 inserted with EcoRI-XbaI fragment (1.95 kb) carrying pebC were constructed. The expression of pcbC and D' in E. coli CK102 and pebC in E. coli CK1092 was examined by gas chromatography and UV-vis spectrophotometry. 2.3-dihydroxybiphenyl was readily degraded to produce meta-cleavage product (MCP) by E. coli CK102 after incubation for 10 min, and then only benzoic acid(BA) was detected in the 24-h old culture. The MCP was detected in E. coli CK1022 containing pebC and 0 genes (by the resting cells assay) for up to 3 h after incubation and then diminished completely in 8 h, whereas the MCP accumulated in the E. coli CK1092 culture even after 6 h of incubation. The 2, 3-DHBP dioxygenases (product of pebC gene) produced by E. coli CK1, CK102, CK1023, and CK1092 strains were measured by native PAGE analysis to be about 250 kDa in molecular weight, which were about same as those of Pseudomonas sp. DJ-12, P. pseudoa1caligenes KF707, and P. putida OU83.
Genetic analysis of polyketide biosynthetic genes isolated from Streptomyces albus, a salinomycin producer.
JOO-WON SUH ; KWON, HYOUNG-JIN ; C.R. HUTCHINSON ; HYUNG-JONG JIN ; SOO-UN KIM ; KYE-JOON LEE ;
Journal of Microbiology and Biotechnology, volume 5, issue 2, 1995, Pages 74~79
Sequence analysis of a DNA region encompassing the site of hybridization to actl, the gene for type II minimal polyketide synthase (PKS) for actinorhodin biosynthesis, from Streptomyces ablus revealed three more complete open reading frames additional to the already found two genes, plausibly encoding
synthase/acyl transferase (KS/AT) and chain length determining factor (ClF). The open reading frames (ORFs) were named salA, salD, and salE, from the upstream. In the homology analysis of the deduced amino acid sequences, SalA resembles the Streptomyces glaucescens Tcml, decaketide cyclase, SalD resembles acyl carrier protein in type II PKS, and SalE resembles the Actlll ketoreductase, The whole 4.4 kb of DNA sequence obeys the same conservation pattern as other type II PKSs. Therefore, we suggest that the 4.4 kb DNA from Streptomyces albus encompasses genes encoding enzymes for polyketide biogenesis in the organism and its organization is type II. The exsitence of SaIA, an analogue of the aromatic cyclase, revealed a relatedness of the 4.4 kb DNA with the aromatic PKS.
Isolation and Characterization of Acinetobacter sp. WC-17 Producing Chitinase
SOON-DUCK HONG ; SHIN, WOO-CHANG ; DONG-SUN LEE ; TAE-HO KIM ; JU-HYUNG WOO ; JIN-MAN LEE ; JONG-GUK KIM ;
Journal of Microbiology and Biotechnology, volume 5, issue 2, 1995, Pages 80~86
The bacterial strain WC-17 able to produce chitinase was isolated from soil using an enrichment technique. The isolated strain was identified as Acinetobacter sp. judging by their morphological and physiological characterisitics. The optimal culture conditions for the production of chitinase of Acinetobacter sp. WC -17 are 1.5% colloidal chitin and 1 % tryptone at
with pH 6.5. Since the enzyme was rapidly produced in a culture supplied with chitin, glucose, or N-acetylglucosamine but not with other polymers and monosaccharide, the enzyme was considered to be an inducible enzyme. Notably N- acetylglucosamine and glucose were found to be effective inducers at low concentrations but repressors at excessive concentrations. The cultural supernatant of Acinetobacter sp. WC-17 inhibited the growth of phytopathogenic fungi such as P.oryzae, R.solani, and F.solani. Among the phytopathogenic fungi tested, P.oryzae was the most sensitive. The conventional agar plate (PDA containing 1 % colloidal chitin) method also produced the same result.
Molecular Cloning of Acinetobacter sp. WC-17 Gene Encoding Chitinase
SOON-DUCK HONG ; SHIN, WOO-CHANG ; DONG-SUN LEE ; JONG-GUK KIM ;
Journal of Microbiology and Biotechnology, volume 5, issue 2, 1995, Pages 87~91
The chitinase gene was cloned from Acinetobacter sp. WC-17 for investigating the genetic control and enzymatic properties of bacterial chitinase. A genomic library of Acinetobacter sp. WC-17 was prepared in E.coli JM109 by using pUC18 as a vector. The chitinase-positive clone containing 3.2kb insert fragment was obtained from 5, 000 insert-bearing transformants. The optimum pH and temperature of cloned enzyme were 6.0 and
, respectively. Almost all the chitinase activity of E.coli recombinant was localized in the periplasmic fraction, while most of the enzyme activity of Acinetobacter sp. WC-17 was found in the extracellular fraction.
Alginate Lyase Production of Halophilic Pseudomonas sp. by Recombinant Escherichia coli
Kong, In-Soo ; Kim, Young-Ok ; Kim, Jin-Man ; Kim, Sung-Koo ; Oh, Doo-Hwan ; Yu, Ju-Hyun ; Kong, Jal-Yul ;
Journal of Microbiology and Biotechnology, volume 5, issue 2, 1995, Pages 92~95
Halophilic Pseudomonas sp.W7 isolated from laver in the southem sea of Korea showed alginate lyase activity. Gene (aly) encoding alginate lyase was cloned in E.coli JM83 and the N-terminal amino acid sequence of the enzyme was determined after purificaion. The recombinant enzyme has been shown to have a molecular weight of about 40kDa after 12% SDS-polyacrylamide gel electrophoresis.
Effect of Magnesium Sulfate on Product Inhibition of Sisomicin Production
Shin, Chul-Soo ; Han, Sang-Hun ;
Journal of Microbiology and Biotechnology, volume 5, issue 2, 1995, Pages 96~99
Addition of l00mM
to a cell culture after 54 hours resulted in a 2.4-fold increase in the sisomicin titre compared to a control to which no
was added, and a considerable amount of intracellular sisomicin was liberated outside the cells. The occurrence of product inhibition in fermentation was confirmed by a reduction in net sisomicin production with increasing amounts of added sisomicin without addition of
. All added sisomicin was bound to sisomicin-free cells in the absence of
, whereas approximately 40% of added sisomicin was bound with the addition of l00mM
. Under conditions of no enzmye synthesis, maintained by adding chloramphenicol to exclude product repression, sisomicin was produced in the presence of 100 mM
but little sisomicin was produced in the absence of
Effects of Nitrogen and Oxygen Supply on Production of
in Azotobacter chroococcum
Lee, In-Young ; Stegantseva, Ellen-M. ; Savenkova, Ludmila ; Park, Young-Hoon ;
Journal of Microbiology and Biotechnology, volume 5, issue 2, 1995, Pages 100~104
(PHB) in a strain of Azotobacter chroococcum, a nitrogen-fixing bacteria, was investigated at various levels of nitrogen and oxygen. Feeding nitrogen source increased both cell growth and PHB accumulation. Oxygen supply appeared to be one of the most important operating parameters for PHB production. Both cell growth and PHB accumulation increased with the sufficient supply of air in the fed-batch fermentation of the strain. However, it was also noted that keeping the oxygen level under limited condition was critical to achieve high PHB productivity. A high titer of PHB (52 g/l) with a high cellular content (60%) was obtained after 48 hr of fed-batch operation by controlling the oxygen supply. Dual limitation of nitrogen and oxygen did not further increase the PHB accumulation probably due to the greater demand for reducing power and ATP for nitrogen fixation.
Detection of Anticancer Activity from the Root of Angelica gigas In Vitro
Ahn, Kyung-Seop ; Sim, Woong-Seop ; Kim, Ik-Hwan ;
Journal of Microbiology and Biotechnology, volume 5, issue 2, 1995, Pages 105~109
Anticancer activity of a fraction of the ethanol extract from the root of Korean angelica (Angelica gigas Nakai) was recognized in human cancer cell lines HeLa
, K-562, and Hep
. The extract blocked the phorbol ester-inducing megakaryocytic differentiation of K-562 cells, which indicated the modification of protein kinase C (PKC) activity. In vitro assay showed the activation of PKC by the extract. An effective fraction of the Angelica gigas extract, of which
value was 0.64 in a thin layer chromatography, was a different component from those of European angelicas. The
value of the fraction was 8, 9, and
, and K-562 cells, respectively, while the fraction showed higher
values against normal cell lines.
Transposon Tn5 Mutagenesis of Bradyrhizobium japonicum: A Histidine Auxotrophic Mutant of B. japonicum Shows Defective Nodulation Phenotype on Soybean
So, Jae-Seong ;
Journal of Microbiology and Biotechnology, volume 5, issue 2, 1995, Pages 110~113
Transposon Tn5 was used to induce random insertional mutations in Bradyrhizobium japonicum, a soybean endosymbiont. By genomic Southern blot analysis, transposition events were found to have occurred randomly throughout the B. japonicum genome. After screening 3, 626 mutants by auxotrophy test, a histidine auxotroph was isolated. Upon plant infection test, the His mutant showed a 3~4 day delay in nodule formation.
Yeast Biomass Production from Concentrated Sugar Cane Stillage Using a Thermotolerant Candida rugosa
Lee, Ki-Young ; Lee, Sung-Taek ;
Journal of Microbiology and Biotechnology, volume 5, issue 2, 1995, Pages 114~116
Concentrated Brazillian sugar cane stillage was used as a substrate for the yeast biomass production using Candida rugosa isolated from East Africa. At the optimum stillage concentration of 10% dry matter, biomass production was 20.4 g/l and COD reduction rate was 41%. The specific growth rate of the yeast was 0.17
and the corresponding productivity 0.91 g
in the batch fermentation was observed at