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REFERENCE LINKING PLATFORM OF KOREA S&T JOURNALS
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Journal of Microbiology and Biotechnology
Journal Basic Information
Journal DOI :
The Korean Society for Applied Microbiology and Biotechnology
Editor in Chief :
Volume & Issues
Volume 8, Issue 6 - Dec 1998
Volume 8, Issue 5 - Oct 1998
Volume 8, Issue 4 - Aug 1998
Volume 8, Issue 3 - Jun 1998
Volume 8, Issue 2 - Apr 1998
Volume 8, Issue 1 - Feb 1998
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Water Activity Control in Lipase-catalyzed Reaction System
Rhee, Joon-Shick ; Kwon, Seok-Joon ;
Journal of Microbiology and Biotechnology, volume 8, issue 3, 1998, Pages 191~196
This mini review describes the effects of water activity (
) on the kinetics, regio- and enantioselectivities of lipases, and various methods for measuring and controlling
in lipase catalyzed reaction in organic solvent.
Antifungal Activity of Medium-Chain (
) Alkenals against, and Their Inhibitory Effect on the Plasma Membrane
-ATPase of Saccharomyces cerevisiae
Lee, Jae-Ran ; Lee, Sang-Hwa ; Kubo, Isao ; Hong, Soon-Duck ;
Journal of Microbiology and Biotechnology, volume 8, issue 3, 1998, Pages 197~202
Aliphatic alkenals having 6 to 13 carbons were evaluated for antifungal activity against Saccharomyces cerevisiae. The activity was gradually increased with chain length, e.g., (E)-2-decenal and (E)-2-undecenal exhibited maximum potency, while (E)-2-dodecenal and (E)-2-tridecenal were completely inactive. Alkenals showed increasing inhibitory activity with chain length, as in the case of antifungal activity, towards glucose-induced medium acidification by the plasma membrane
-ATPase of S. cerevisiae. The group including (E)-2-nonenal, (E)-2-decenal, and (E)-2-undecenal exhibited maximum potency, but the potency of (E)-2-dodecenal and (E)-2-tridecenal demonstrated a sudden drop with respect to the former group. (E)-2-Nonenal revealed dose-responsive inhibition to the medium acidification and inhibited over 90% at a concentration of 1.25 mM (
/ml). In contrast to (E)-2-undecenal whose inhibitory efficiency increased with incubation time, inhibition by (E)-2-dodecenal was reversed with time. Of the tested alkenals, (E)-2-heptenal and (E)-2-octenal most highly inhibited ATP hydrolytic activity by the plasma membrane
ATPase, while (E)-2-heptenal at 10 mM (
/ml) showed an inhibitory efficacy of 93.2%.
Invertase Production by Fed-batch Fermentations of Recombinant Saccharomyces cerevisiae
Koo, Ja-Hyup ; Kim, Sang-Yong ; Park, Yong-Cheol ; Han, Nam-Soo ; Seo, Jin-Ho ;
Journal of Microbiology and Biotechnology, volume 8, issue 3, 1998, Pages 203~207
Fed-batch fermentations with different feeding media were carried out in order to increase the productivity of invertase expression using a recombinant Saccharomyces cerevisiae containing plasmid pRB58. Two batch cultures showed the expression of the SUC2 gene at a low concentration of glucose, suggesting that glucose concentration could be used as a control variable in a fed-batch operation mode. In the fed-batch culture by feeding the basal medium, cell mass and specific invertase activity did not increase much as compared with the simple batch culture. A series of fed-batch cultures revealed that the sucrose-supplemented medium increased cell mass whereas the enriched medium did specific invertase activity. To capitalize on the synergism of the sucrose-supplemented medium and the enriched medium, the sucrose-supplemented enriched medium was used as a feeding medium. The fed-batch culture using this medium resulted in a 2.4-fold increase in cell mass and a 1.9-fold enhancement in specific invertase activity compared with those of the batch culture. The increase in cell mass and specific invertase activity led to a marked increase in total invertase activity, 250U/ml, which was 6.3 times higher than that of the batch culture.
Production of Cellulase by Trichoderma reesei Rut C30 in Wheat Bran-containing Media
Yu, Xiao-Bin ; Yun, Hyun-Shik ; Koo, Yoon-Mo ;
Journal of Microbiology and Biotechnology, volume 8, issue 3, 1998, Pages 208~213
The effect of the addition of wheat bran to the growth medium on the production of cellulolytic enzymes of Trichoderma reesei Rut C30 was studied in batch culture using shake flasks. The activity of cellulase was enhanced by the addition of wheat bran to the cellulase production medium.
buffer was used for pH control during cellulase production. As a result, high cellulase activities were obtained in shake flask culture; a CMC (carboxymethyl cellulose) activity of 125.78 U/ml was obtained from 2% Avicel- and 3% wheat bran-containing medium and an FP (filter paper) activity of 12.85U/ml was obtained from 1% Avicel- and 5% wheat bran-containing medium after 6 days of cultivation.
Cloning, Expression, and Nucleotide Sequencing of the Gene Encoding Glucose Permease of Phosphotransferase System from Brevibacterium ammoniagenes
Yoon, Ki-Hong ; Yim, Hyouk ; Jung, Kyung-Hwa ;
Journal of Microbiology and Biotechnology, volume 8, issue 3, 1998, Pages 214~221
A Brevibacterium ammoniagenes gene coding for glucose/mannose-specific enzyme II (
) of the phosphoenolpyruvate-dependent phosphotransferase system (PTS) was cloned by complementing an Escherichia coli mutation affecting a ptsG gene, and the complete DNA nucleotide sequence was determined. The cloned gene was identified to be a ptsG, which enables the E. coli transportment to use glucose more efficiently than mannose as the sole carbon source in an M9 minimal medium. The ptsG gene of B. ammoniagenes consists of an open reading frame of 1,983 nucleotides putatively encoding a polypeptide of 661 amino acid residues and a TAA stop codon. The deduced amino acid sequence of the B. ammoniagenes
, the highest degree of sequence similarity with the Corynebacterium glutamicum EII specific for both glucose and mannose. In addition, the
sequence similarities with sucrose-specific and
-glucoside-specific EIIs of the several bacteria belonging to the glucose-PTS class. The 161-amino-acid C-terminal sequence of
is also similar to that of E. coli enzyme
, specific for glucose (
). The B. ammoniagenes
consists of three domains; a hydrophobic region (EIIC) and two hydrophilic regions (EIIA, EIIB). The arrangement of structural domains, IIBCA, of the
is identical to those of EIIs specific for sucrose or
-glucoside. While the domain IIA was removed from the B. ammoniagenes
the remaining domains IIBC were found to restore the glucose and mannose-utilizing capacity of E. coli mutant lacking
of the E. coli mutant.
contains a histidine residue and a cysteine residue which are putative phosphorylation sites for the protein.
Cometabolic Removal of Xylene Isomers by Alcaligenes xylosoxidans Y234
Yeom, Sung-Ho ; Lee, Jung-Heon ; Yoo, Young Je ;
Journal of Microbiology and Biotechnology, volume 8, issue 3, 1998, Pages 222~228
The characteristics of cometabolic removal of xylenes by Alcaligenes xylosoxidans Y234 were investigated. m-Xylene was found to be degraded while ο- and p-xylene were biotransformed into cresols in the presence of benzene or toluene. A lower level of benzene was required than that of toluene to remove the same amount of xylenes, which suggested benzene was a more effective primary substrate than toluene. ο-Xylene was found to be the most toxic to Alcaligenes xylosoxidans Y234 followed by p-xylene and m-xylene. Rates of cell decay during cometabolic removal of ο-, m-, or p-xylene were decreased by up to
when benzene-adapted cells were inoculated. Xylenes were removed efficiently using benzene-adapted cells.
Effect of 1-[(2-Hydroxyethoxy)methyl]-6-(phenylthio)thymine (HEPT) Derivatives on Bacterial Growth
Gang, Jin-Gu ; Yun, Hong-Chul ; Son, Jong-Chan ; Hwang, Se-Young ;
Journal of Microbiology and Biotechnology, volume 8, issue 3, 1998, Pages 229~236
6-Substituted derivatives of 1-［(2-hydroxyethoxy)methyl］-6-(phenylthio)thymine (HEPT) were synthesized by introducing alkyl groups with the aid of chlorotrimethylsilane, and then purified ranging 40 to 81 % of yield. Because of their peculiar structures, we presumed that HEPT derivatives would contain extra biological activities other than their already known anti-human immunodeficiency viral (HIV -1) activities. In this study, we investigated the possible effects of the HEPT derivatives on bacterial growth and found their selective antibiotic activities against gram-positive strains. We could not observe the corresponding activity from a disc-zone test, but confirmed the activity by liquid cultivation. Since the growth rate of cells was easily recovered, the antibiotic function was suggested to be bacteriostatic. We also suggested that the intracellular fate of HEPT derivatives would be fast. A HEPT derivative f-3 was shown to synergize unidirectionally toward chloramphenicol (Chr). With 0.1 mM f-3, the Chr-directed growth-inhibitory curve appeared 4 hours earlier than found without the additive. Interestingly, from the data of SDS-polyacrylamide gel electrophoresis (PAGE), we found that a membrane-bound protein having a molecular weight of 70-kDa was overexpressed by f-3 in S. aureus.
Effect of Environmental Factors on Flavonol Glycoside Production and Phenylalanine Ammonia-lyase Activity in Cell Suspension Cultures of Ginkgo biloba
Kim, Min-Soo ; Lee, Won-Kyu ; Kim, Hwa-Young ; Kim, Chul ; Ryu, Yeon-Woo ;
Journal of Microbiology and Biotechnology, volume 8, issue 3, 1998, Pages 237~244
A study was carried out to elucidate the relation between the production of flavonol glycosides and the change of phenylalanine ammonia-lyase activity in cell suspension cultures of Ginkgo biloba by the unassisted and synergistic effects of various factors. The quercetin production showed a mixed-growth-associated pattern in cell suspension cultures. Fluorescent light and UV radiation increased phenylalanine ammonia-lyase (PAL) activity, and resulted in the increase of the production of quercetin and kaempferol ten- and four-fold, respectively, as compared to that obtained in the normal culture condition. The cell growth of Ginkgo biloba was enhanced .at higher temperatures whereas the quercetin production was at its maximum at low temperatures. Moreover, the quercetin production was increased by temperature change during the culture period. In particular, the quercetin production was at the highest level when the culture temperature was elevated from
. The addition of phenylalanine as a precursor in the culture medium stimulated an 8-fold increase in the production of quercetin; the addition of naringenin caused a l0-fold increase. The quercetin production was also greatly increased by feeding enzyme cofactors such as 2-ketoglutarate and ascorbic acid in the culture medium, but specific PAL activity was not increased except with phenylalanine feeding. The synergistic effect of UV radiation and naringenin feeding was observed, resulting in the increase of flavonol glycoside production at a rate higher than in any other case investigated.
Cloning and Expression of a Collagenase Gene from the Marine Bacterium Vibrio vulnificus CYK279H
Kim, Bong-Jo ; Kim, Hak-Ju ; Hwang, Sun-Hee ; Bae, Seoung-Kwon ; Ha, Soon-Duck ; Kim, Jong-Deog ; Kong, Jai-Yul ;
Journal of Microbiology and Biotechnology, volume 8, issue 3, 1998, Pages 245~250
A gene encoding an extracellular collagenase from the marine bacterium Vibrio vulnificus CYK279H was cloned into E. coli JM83 using the multicopy plasmid vector pUC19. The cloned strain of recombinant E. coli showing collagenase activity had an insert fragment of 3.5 kb and was named E. coli JM83/pKCL 279H. The cloned strain produced two different collagenase during cultivation. These enzymes, named collagenase-I and -II, were purified from the culture supernatant. SDS-PAGE indicated that collagenase-I had a molecular weight of 41 kDa and collagenase-II had a weight of 37 kDa. The N-terminal amino acid sequence of collagenase-I from the cloned strain, E. coli JM83/pKCL279H was determined and was not found to be similar to any other known collagenases. The optimum pH and temperature of the purified collagenase-I were 7.8 and
Purification and Characterization of Cycloinulooligosaccharide Fructanotransferase from Bacillus macerans CFC1
Kim, Hwa-Young ; Choi, Yong-Jin ;
Journal of Microbiology and Biotechnology, volume 8, issue 3, 1998, Pages 251~257
Cycloinulooligosaccharide fructanotransferase (CFTase) which produces cyclofructan from inulin was purified 332-fold from a culture broth of Bacillus macerans CFCl. The molecular mass of the CFTase was estimated to be 110 kDa by SDS-polyacrylamide gel electrophoresis and gel filtration, indicating that the enzyme has a monomer structure. The maximal level of enzyme activity was observed at pH 7.5 and
. The enzyme was stable in the pH range 6.0 to 9.5, and at temperatures up to
for 1 h. The enzyme activity was completely inhibited in the presence of 0.5 mM
ion. None of sucrose (GF), l-kestose (GF2), or nystose (GF3) were found to be substrates for the CFTase, but inulooligosaccharides larger than nystose were attacked by the enzyme. The CFTase catalyzes not only the cyclization as the major reaction, but also disproportionation and coupling reactions involving intermolecular transfructosylation in the same manner as cyclodextrin glucanotransferase (CGTase) (EC 22.214.171.124).
Purification and Characterization of the Bacillus sp. KK-l
-Xylosidase from a Recombinant Escherichia coli
Jung, Kyung-Hwa ; Chun, Yong-Chin ; Lee, Jae-Chan ; Park, Seung-Hwan ; Yoon, Ki-Hong ;
Journal of Microbiology and Biotechnology, volume 8, issue 3, 1998, Pages 258~263
-Xylosidase was purified from the recombinant Escherichia coli carrying the Bacillus sp. KK-1
-xylosidase gene (xylB). The molecular mass of the purified enzyme was estimated to be 62 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. However, the apparent molecular mass of the
-xylosidase was 140 kDa, indicating that the native
-xylosidase has an oligomeric structure composed of two identical subunits. The isoelectric point was determined to be pH 5.5. The enzyme was highly active on p-nitrophenyl-
-D-xylopyranoside but it barely hydrolyzed xylan substrates, and did not exhibit activity towards carboxymethylcellulose and p-nitrophenyl-
-D- glucopyranoside. The enzyme had a pH optimum for its activity at pH 6.5 and a temperature optimum at
. The enzyme activity was completely inhibited by the presence of
, and also markedly inhibited by D-xylose and D-glucose.
Extradiol Cleavage of Two-ring Structures of Biphenyl and Indole Oxidation by Biphenyl Dioxygenase in Commamonas Acidovorans
On, Hwa-Young ; Lee, Na-Ri ; Kim, Young-Chang ; Kim, Chi-Kyung ; Kim, Young-Soo ; Park, Yong-Keun ; Ka, Jong-Ok ; Lee, Ki-Sung ; Min, Kyung-Hee ;
Journal of Microbiology and Biotechnology, volume 8, issue 3, 1998, Pages 264~269
Commamonas acidovorans SMN4 showed wide growth substrate spectra for various aromatic hydrocarbons. Strain SMN4 was able to grow on biphenyl producing a meta-cleavage compound, yellow 2-hydroxy-6-oxophenylhexa-2,4-dienoic acid with a spray of 2,3-dihydroxybiphenyl, while it also grew on catechol, developing yellow 2- hydroxymucoic semialdehyde with a spray of 100 mM catechol. Thus these results indicate that two-ring structures of biphenyl were cleaved by meta-mode in upper and lower pathways. Strain SMN4 metabolized various substituted biphenyl compounds and xylene to the corresponding benzoate derivatives through oxidation of the ring structures. It was clearly shown that biphenyl can be a common inducer in the oxidation of biphenyl and 2,3-dihydroxybiphenyl. Various compounds were examined for their suitability to serve as substrates for indole oxidation, indicating that biphenyl, benzoate, and succinate are quite good inducers of indigo production due to the activity of biphenyl dioxygenase. This results suggest that indigo formation is by means of the combined activities of biphenyl dioxygenase and tryptophanase.
Purification and Characterization of a Bacillus sp. DG0303 Thermostable
-Glucosidase with Oligo-l,6-glucosidase Activity
Park, Jong-Sung ; Kim, Il-Han ; Lee, Yong-Eok ;
Journal of Microbiology and Biotechnology, volume 8, issue 3, 1998, Pages 270~276
-glucosidase was purified to homogeneity from moderately thermophilic Bacillus sp. DG0303. The thermostable
-glucosidase was purified by ammonium sulfate fractionation, ion-exchange chromatography, preparative polyacrylamide gel electrophoresis (PAGE), and electroelution. The molecular weight of the enzyme was estimated to be 60 kDa by SDS-PAGE. The optimum temperature for the action of the enzyme was at
. It had a half-life of 35 min at
. The enzyme was stable at the pH range of 4.5~7.0 and had an optimum pH at 5.0. The enzyme preparation did not require any metal ion for activity. The thermostable
-glucosidase hydrolyzed the
-1,6-linkages in isomaltose, isomaltotriose, and panose, and had little or no activity with maltooligosaccharides and other polysaccharides. The
(mM) for p-nitrophenyl-
-D-glucopyranoside (pNPG), panose, isomaltose, and isomaltotriose were 4.6, 4.7, 40.8, and 3.7 and the
) for those substrates were 5629, 1669, 3410, and 1827, respectively. The N-terminal amino acid sequence of the enzyme was MERVWWKKAV. Based on its substrate specificity and catalytic properties, the enzyme has been assigned to be an oligo-1,6-glucosidase.
Hepatoprotective Effect of Extracellular Polymer Produced by Submerged Culture of Ganoderma lucidum WK-003
Song, Chi-Hyun ; Yang, Byung-Keun ; Ra, Kyung-Soo ; Shon, Dong-Hwan ; Park, Eun-Jeon ; Go, Geon-Il ; Kim, Young-Hwoan ;
Journal of Microbiology and Biotechnology, volume 8, issue 3, 1998, Pages 277~279
An extracellular polymer (exo-polymer) with hepatoprotective properties was produced after a 6-day submerged mycelial culture of Ganoderma lucidum WK-003. The glutamic pyruvic transaminase (GPT) activities in the serum of intoxicated Sprague-Dawley rats were decreased from 871 to 263 by the oral administration of the exo-polymer (20 mg/kg/day) for 4 consecutive days. Rhamnose, arabinose, xylose, mannose, galactose, and glucose were found in the exo-polymer along with aspartic acid, glutamic acid, histidine, serine, glycine, arginine, alanine, tryptophan, valine, phenylalanine, isoleucine, and leucine.
Efficient Cloning of the Genes for RNA Polymerase Sigma-like Factors from Actinomycetes
Kim, Soon-Ok ; Hyun, Chang-Gu ; Suh, Joo-Won ;
Journal of Microbiology and Biotechnology, volume 8, issue 3, 1998, Pages 280~283
We have cloned the RNA polymerase sigma-like factors from a wide range of actinomycetes by using specific primers with the polymerase chain reaction (PCR). The specific oligonucleotide primers were designed on the basis of amino acid sequences of conserved regions from HrdA, B, D of Streptomyces griseus as well as from the rpoD box of many eubacteria. The consensus sequences were from the rpoD box and helix-turn-helix motif involved in -35 recognition. The designed primers were successfully applied to amplify the DNA fragments of the hrd homolog genes from 8 different strains of actinomycetes which produce a wide variety of important antibiotics. The 480 bp of the DNA fragment was amplified from all 8 strains, and it was identified as a part of hrdA and hrdB as we designed. The deduced amino acid sequence of PCR-amplified DNA fragments were highly homologous to those of other known RNA polymerase sigma factors of S. griseus and Streptomyces aureofaciens. Therefore, this study with specifically designed primers will support rapid cloning of the RNA polymerase sigma factors which recognize different classes of promoters from actinomycetes, and it will also be helpful in understanding the relationship of promoters and sigma factors leading to heterogeneity of RNA polymerases in actinomycetes.
Molecular Cloning and Sequence of URA5 Gene Encoding Orotate Phosphoribosyl Transferase (OPRTase) from Entomopathogenic Fungus, Metarhizium anisopliae
HWANG, CHER WON ; DONG KYU LEE ; SUN CHEOL KANG ;
Journal of Microbiology and Biotechnology, volume 8, issue 3, 1998, Pages 284~286
A ura5 gene encoding Orotate Phosphoribosyl Transferase (OPRTase) of Metarhizium anisopliae was cloned by PCR methods and sequenced. The sequenced ura 5 gene encodes a polypeptide of 234 amino acid residues. This deduced amino acid sequence showed high similarity to other fungi OPRTase and there was no intron sequence between ATG starting codon and TGA ending codon.
Acarbose Effect for Dexran Synthesis, Acceptor and Disproportionation Reactions of Leuconostoc mesenteroides B-512FMCM Dextransucrase
Kim, Do-Man ; Park, Kwan-Hwa ; Robyt, John F. ;
Journal of Microbiology and Biotechnology, volume 8, issue 3, 1998, Pages 287~290
Acarbose effectively inhibited the synthesis of dextran, and the inhibition pattern was a noncompetitive type with a
value of 1.35 mM. It also inhibited the disproportionation reaction of dextransucrase with isomaltotriose and decreased the efficiency of the maltose acceptor reaction. Increased concentration of dextransucrase or maltose in reaction digests, however, decreased the degree of inhibition by acarbose.
Deer Antler Extract Selectively Suppresses Hyphal Growth in Dimorphic Fungus, Candida albicans
Park, Hyun-Sook ; Jeon, Gil-Ja ; Choi, Won-Ja ;
Journal of Microbiology and Biotechnology, volume 8, issue 3, 1998, Pages 291~294
Transfer of Candida albicans grown in Sabouraud medium to the RPMI medium induces the transition from a nonpathogenic yeast form to a pathogenic hyphal form. This transition was severely inhibited in a dose-dependent manner when deer antler extract was added to the RPMI medium in a nontoxic range (up to
). In that range, deer antler extract inhibited the hyphal transition and cell growth, whereas no effect was observed on the yeast growth. When hydrophobic or hydrophilic fractions were prepared by detergent-solubilization of deer antler extract, the hydrophobic fraction showed a large degree of inhibition of the hyphal growth in Candida albicans. Neither fraction affected the growth in the yeast form. The pattern of chitin localization in the culture of the yeast form grown in RPMI in the presence of deer antler extract was confirmed by calcofluor staining and this exhibited strongly the suppression of hyphal transition.
An Efficient Approach for Cloning P450 Hydroxylase Genes from Actinomycetes
Hyun, Chang-Gu ; Kim, Jung-Mee ; Hong, Soon-Kwang ; Suh, Joo-Won ;
Journal of Microbiology and Biotechnology, volume 8, issue 3, 1998, Pages 295~299
Oligonucleotide primers were designed and successfully applied to amplify DNA fragments of P450 hydroxylase genes from actinomycetes which produce a large variety of medically important metabolites. Primers were designed based on several regions of strong similarities in amino acid sequence of P450 hydroxylases from a variety of actinomycetes, primarily in the regions of an oxygen binding site and a heme ligand pocket. These primers were used to amplify DNA fragments from seven different actinomycetes species producing a variety of different compounds. The deduced amino acid sequences of the isolated fragments revealed significant similarities to known P450 hydroxylase including the product of the suaC or subC genes from Streptomyces griseolus that is capable of metabolizing a number of sulfonylurea herbicides, and to the product of the
from S. carbophilus that produces a specific HMG-CoA reductase inhibitor. This method should help researchers in cloning the P450 hydroxylase genes involved in the biosynthesis of useful compounds.