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REFERENCE LINKING PLATFORM OF KOREA S&T JOURNALS
> Journal Vol & Issue
Microbiology and Biotechnology Letters
Journal Basic Information
Journal DOI :
The Korean Society for Applied Microbiology and Biotechnology
Editor in Chief :
Volume & Issues
Volume 20, Issue 6 - Dec 1992
Volume 20, Issue 5 - Oct 1992
Volume 20, Issue 4 - Aug 1992
Volume 20, Issue 3 - Jun 1992
Volume 20, Issue 2 - Apr 1992
Volume 20, Issue 1 - Feb 1992
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The Effects of Branched Chain Amino Acids and Small Metabolites on the Biosynthesis of Acetolactate Synthase in Serratia rnarcescens ATCC 25419
Microbiology and Biotechnology Letters, volume 20, issue 2, 1992, Pages 115~121
The effects of branched chain amino acids and small metabolites in growth media on the biosynthesis of Serratia marcescens ATCC 25419 acetolactate synthase (ALS) were examined. ALS activ~ty was gradually decreased by isoleucme or leucine among the range from 1 mM to 20 rnM, while the activity was increased 40% by isoleucine under low concentration (0.5 mM). ALS activity was also increased about 40% by valine among 2 to 4 mM ranges, but the activity was decreased only 10% at 20 mM. ALS activity was decreased 25% and 70% by the simultaneous addition of all three branched chain amino acids at 2 mM and 10 mM, respectively. Among several small metabolites tested, ALS activity was increased about 2-fold by cAMP at 2 mM. These data suggest that Sorrtrtiti rnorcewns ALS is muitivalently repressed by branched chain amino acids, but not repressed by valine alone.
Production and Purification of
Repressor Protein by the Use of a Runaway Replication Plasmid Vector
Microbiology and Biotechnology Letters, volume 20, issue 2, 1992, Pages 122~128
Runaway replication plasmid pSY35AT was used for the production of
repressor protein. E, coli MC1065 having plasmid pSY35AT was shifted from
repressor protein produced was purified by a modification of the purification method of wild type cI repressor. The concentration of purified
repressor protein was 0.11 mg/ml. The binding assay of
repressor and right promoter - right operater (
) labeled with
was done. Relative activity of purified cIx5, repressor was higher about 23 times than that of cell free extract. A higher value of the temperature in the binding assay led to a lower value of the binding activity.
Molecular Cloning of Serratia marcescens Chitinase Gene into Escherichia coli
Microbiology and Biotechnology Letters, volume 20, issue 2, 1992, Pages 129~135
A chitinase gene of Serratia marcescens ATCC 27117 was cloned and expressed in Escherichiu di. A genomic library of S, marcescens was constructed with pUC 19 and screened using the swollen chitin agar plate for chitinolytic clones. A positive clone showing chitinclearance contains a recombinant pCHI 89, composed of 8.9 Kb chromosomal DNA fragment and pUC 19. Plasmid pCHI 89 produced 58 KD chitinase in E. coli, which was coincided with one of five extracellular chitinases produced by S. nzarccscens. Restriction endonuclease cleavage sites of the 8.9 Kb insert DNA fragment were mapped. E. coli JM109 harboring pCHI 89 inhibits the growth of a plant pathogenic fungus, Fusarium oxysporum.
Molecular Cloning and Expression of Bacillus stearothermophilus
-D-Xylosidase Gene in E. coli
Microbiology and Biotechnology Letters, volume 20, issue 2, 1992, Pages 136~142
Bacillus stearothemophilus isolated from soil was identified to express multiple extracellular xylanases. Two HindIII restriction fragments of 5.4 and 6.4 kb from B. stearothermophilus genomic DNA were cloned into pBR322 to obtain recombinant plasmids pMG0l and pMG02, respectively, which enabled E. coli HBlOl cells to produce
-D-xylosidase activity. By subcloning into pUC18 and Southern blotting, the loci of the
-D-xyiosidase genes were elucidated to be on non-homologous DNA fragments of 2.2 kb from pMGOl(pMG1) and 1.0 kb from pMG02(pMG2), respectively. The two enzymes produced in E. coli cleaved xylobiose, xylotriose, xylotetrose and xylotetrose to produce xylose as a major end product. The gene on pMG1, distinct from that on pMG2 was observed to encode a bifunctional protein that displayed both P-D-xylosidase (EC.188.8.131.52) and a-L-arabinofuranosidase activities (EC.184.108.40.206).
Purification and Properties of
-Glucosidase from Mococcus halophilus
Microbiology and Biotechnology Letters, volume 20, issue 2, 1992, Pages 143~149
A bacterial strain No. 2, which highly produced a-glucosidase, was isolated from Kimchi and identified to be a similar species of Pediococcus halophilus. This enzyme was purified by protamine sulfate, ammonium sulfate fractionation, ion exchange and gel filtration. The maximal a-glucosidase activity was observed at pH 6.0 and this enzyme was stable at pH 6.0~ 7.5. The optimum temperature of this enzyme activity was
, but enzyme activity was gradually lost above
. This enzyme was activated by 10 mM MgCh and inhibited by 10 mM mercaptoethanol. The kinetics of PNPG(p-Nitrophenyl-a-D-glucopyranoside) and maltose were Kp0.52 mM/27.5 pg protein,
= 0.021 mM/min 27.5
= 0.32 mMD7.5
= 0.025 mM/min 27.5
protein, respectively. The molecular weight of
-glucosidase was about 37, 000.
Properties of an Extracellular 5-Fluorocytosine Deaminase
Microbiology and Biotechnology Letters, volume 20, issue 2, 1992, Pages 150~155
- Some properties of an extracellular cytosine deaminase excreted from an isolate from soil samples were examined after 20~80%' ammonium sulfate fractionation. The enzyme catalyzed the conversion of cytosine and 5-fluorocytosine into uracil and 5-fluorouracil by substrate specificity, respectively. The optimum temperature and storage time on the stability of the enzvme preparation were below
keeping above 90% of the residual activity and near 4 days keeping above 80% of the residual one in Tris-HCI buffer. The maximum activity was also obtained at 8.0 in pH and 37'C in temperature. The pHs and temperatures for enzyme activity ranged from 8.0~8.5 and from 37~
. respectively. The presence of
in the reaction mixture resulted in the marked inhibition in enzyme activity, but 1 mM of
. slightly increased the activity. The enzyme preparation was heavily affected by most of inhibitors tested such as 1 mM of EIITA, NaCN and pentachlorophenol, and completely inactivated by p-CMB and TCA of 1 mM, or 10 mM.
Purification and Characterization of Cyclodextrin Glucanotransferase from Bacillus sp. El
Microbiology and Biotechnology Letters, volume 20, issue 2, 1992, Pages 156~163
Bacillus sp. was isolated from soil for its strong activity of cyclodextrin glucanotransferase (CGTase, EC 220.127.116.11). The enzyme was purified by gel filtration and anion exchange column chromatography using FPLC. The purified enzyme exhibited its maximum CGTase activity in the pH range of 6~8 and the temperature range of 50~
. The molecular weight was estimated as 114,000 by SDS-PAGE. The isoelectric point of the enzyme was 4.3. The CGTase of Bacillus sp. E l produced
-cyclodextrin mainly and did not produce a-cyclodextrin. The product ratio of
-cyclodextrin was 7:l.
Properties of Cellulase Produced from Cellulomonas sp. YE-5
Microbiology and Biotechnology Letters, volume 20, issue 2, 1992, Pages 164~168
Enzymatic properties of avicelase, carboxymethyl cellulase (CMCase) and P-glucosidase produced by Cellulomonas sp. YE-5 were studied. Optimal temperature and pH of avicelase were 40t and 6.0, and those of CMCase and P-glucosidase were
and 6.5. Avicelase and CMCase were stable between pH 5.0 and 9.5, and &glucosidase was stable between pH 5.5 and 8.0. Avicelase and P-glucosidase were inactivated when incubated at
for 6 hrs, and CMCase was at
for 6 hrs. All cellulases were strongly inhibited by
values of avicelase for avicel, CMCase I and CMCase II for CM-cellulose, and (
-glucosidase for p-nitrophenyl-
-D-glucoside (PNPG) were 4.76, 16.4, 16.4
/ml and 3.51 mM, respectively.
Production and Purification of Alkaline Protease from Streptomyces sp.
Microbiology and Biotechnology Letters, volume 20, issue 2, 1992, Pages 169~177
An alkaline protease producing microorganism was isolated from soil and identified as Streptomyces griseus HC-1141. The optimum culture condition of Streptomyces griseus HC- 1141 for the production of alkaline protease was as follows; 0.5% casein, 0.05% ammonium chloride, 0.1% ferrous sulfate. 2.0% lactose, pH 8.0 and 84 hrs. The enzyme was purified about 53 folds by ammonium sulfate treatment, DEAE-cellulose ion exchange chromatography and gel filtratioo on Sephadex G-150. The homogeneity of the purified enzyme was verified by polyacrylamide gel electrophoresis. The molecular weight was estimated to be 31,000 on sodium dodecyl sulfate polyacrylamide gel electrophoresis. This enzyme consists of glycine and glutamic acid as major amino acids. The N-terminal and C-terminal residues of the alkaline protease were leucine and histidine respectively.
Purification of Cephalosporin C Produced by Cephalosporium acrernoniurn
Microbiology and Biotechnology Letters, volume 20, issue 2, 1992, Pages 178~182
For an industrial-scale purification and production of cephalosporin C from a culture broth of Ceplzalos#mium nmemonium CSA-2.8A3 mutant, ultrafiltration, column chromatography, reverse osmosis, and spray drying were empolyed. Above 90% of yield and high purity of cephalosporin C were obtained through WA-30, HP-20, XAD-2000 and SK-1B column chromatographies. Especially, in the tendom operation of the columns, the recovery yield was increased up to 96%. The purified cephalosporin C was stable at
and in acidic condition, while it was unstable at room temperature and in alkaline condition at pH above 8.0. Cephalosporin C powder or a final product prepared by spray drying contained 85.554 of sodium cephalosporin C, 6.3%' of water, 4.63% of free $
ions. and traces of metal ions.
Cultural Conditions of Lactococcus sp. 1112-1 for Production of Bacteriocin-like Substance
Microbiology and Biotechnology Letters, volume 20, issue 2, 1992, Pages 183~189
Cultural conditions of Lactococcus sp. 1112-1, a bacteriocin producing strain, were studied for enhancing its production with regard to environmental and nutritional factors. Optimal compositions of culture medium for bacteriocin production were glucose 20 g/l as carbon source, casein acid hydrolyzate 15 g/l as nitrogen source, and sodium acetate 3 g/l, ammonium citrate 2 g/l as morganic salt with other basal components. The optimal pH of medium and fermentation temperature were 6.2 and
, respectively. This strain required exclusively riboflavin and pantothenic acid for growth and bacteriocin production. In a 1l batch culture, stationary phase emerged after 8.5 hours of fermentation when 1.81 g/l of biomass was accumulated. The maximum antimicrobial activity was 3,894 IU/ml after 12 hours.
Formation of PEG/Dextran Aqueous Two-Phase System for Starch Hydrolysis Using
Microbiology and Biotechnology Letters, volume 20, issue 2, 1992, Pages 190~195
In the polyethylene glycol/dextran aqueous two-phase systems, volume ratio was increased and partition coefficient was decreased with the increase of potyethylene glycol molecular weight and concentration. However the volume ratio was decreased and the partition coefficient was increased with the increase of dextran molecular weight. On the other hand, the volume ratio and the partition coefficient were decreased with the increase of dextran concentration. Continuous enzymatic hydrolysis of soluble starch with
-amylase which was produced by Bacillus amyloliquefaciens IF0 14141 was investigated in polyethylene glycol/dextran aqueous two-phase systems. Nonreacted soluble starch and
-amylase were reused in these systems.
-Amylase activity was maintained more than 100 hrs by recycling of
-amylase from bottom of settler to reactor.
Biopolyrner Production of Zoogloea ramigera in Batch, Fed-Batch and Continuous Culture Processes
Microbiology and Biotechnology Letters, volume 20, issue 2, 1992, Pages 196~202
Zoogloea ramigera 115 was selected for the production of viscous microbial polysaccharide for bioflocculants usage. Batch, fed-batch, and continuous culture processes were examined with regard to the high biopolymer production. Several carbon sources were tested, including glucose, lactose, molasses, and cheese whey. The C/N ratio of 90 was most effective for biopolymer production from glucose, while the C/N ratios of 30 for lactose and 60 for both molasses and cheese whey substrate gave a maximum production. Fed batch culture proved more effective to increase final biopolymer concentration than batch culture. Continuous fermentation with two stages modifying C/N ratio increased the productivity. The production rates were a maximum at dilution rate of 0.048
for molasses and at 0.096
for cheese whey.
A Study on the Conditions of Demethyltetracycline Fermentation
Microbiology and Biotechnology Letters, volume 20, issue 2, 1992, Pages 203~206
Conditions of fermentation for the production of demethyltetracycline were examined using the mutant, which was obtained through the cell fusion of demeclocycline producing strains, The optimum temperature and the initial pH of broth for demethyltetracycline fermentation were
and 6.7, respectively. Unlike any other cases, the control of pH with alkali solution during the fermentation process affected the productivity. As a general rule, the larger the inoculum size the higher the early consumption of sugar and the viscosity of broth, which means that fermentation proceeds more rapidly as the inoculum size is increased. The highest productivity was shown when the inoculum size was 5% (v/v), and the phase of seed also influenced the fermentation. Among the parameters of pre-culture thus examined, pH was the most important factor.
Studies on the Production of Serratiopeptidase from Serratia Culture
Microbiology and Biotechnology Letters, volume 20, issue 2, 1992, Pages 207~212
An anti-inflammatory agent, serratiopeptidase, was produced from the culture of the Serratia marcescens. The effects of carbon sources, nitrogen sources and inducers on the production were investigated. Citrate was found to be inhibitory in the production of serratiopeptidase. The enzyme was synthesized in the synthetic medium without inducers, albeit low level of synthesis. But the synthesis was increased by the addition of proteinaceous substrate and leucine. Induction of extracellular proteinase by its end-product was discovered, which is not common in the proteinase synthesis in the bacteria. By the glucose fed-batch culture, we found the possible catabolite repression on the production of serratiopeptidase.
Effect of Magnesium Sulfate on Sisomicin Fermentation
Microbiology and Biotechnology Letters, volume 20, issue 2, 1992, Pages 213~218
Fermentation patterns were changed by adding magnesium sulfate to the fermentation broth and its effect on enhancement of sisomicin production was investigated. When cell growth was expressed by DNA content, trophophase and idiophase were separated, but not by dry cell weight. On the other hand, addition of magnesium sulfate had the antibiotic accumulated inside the cells be liberated into the outside, and this effect resulted in improving the final antibiotic yield. The maximum antibrotic yield was obtained when 100 mM magnesium sulfate was added after one day of cultivation, and enhanced more than three times compared to that of the control to which it was not added.
Effect of Lactic Acid Bacteria on the Growth of Yeast from Mul-kimchi
Microbiology and Biotechnology Letters, volume 20, issue 2, 1992, Pages 219~224
The changes of yeast population were investigated in Mul-kimchi containing 3% salt, fermented at
. The total viable count increased to the maximum at the optimum ripening period and then decreased rapidly. Among twenty-nine strains isolated at the optimum ripening period, the yeasts of genus Saccharomyces were predominant. The growth of five strains, Saccharomyces saitoanus Y17, Saccharomyces capensis Y29, Saccharomyces chevalieri Y13, Kluyveromyces fragilis Y2, Torulopsis candida Y9, was measured in mixed culture with each selected lactic strains, hctobaczllus plantarum Lp2, Pedzococcus pentosaceus PI, Leuconostoc mesenteroides Lu5. The results indicated that all the yeasts tested were inhibited significantly by lactic strains, however the sensitivity of yeast strains varied greatly.
Development of an Enzyme-Linked Immunosorbent Assay for the Iletection of Aflatoxin
Microbiology and Biotechnology Letters, volume 20, issue 2, 1992, Pages 225~232
In order to develop an enzyme-linked immunosorbent assay(ELISA) for detecting aflatoxin
, we produced and purified antibodies, thereafter established and evaluated methods of direct and indirect competitive ELISA. Anti-AFB, antisera, produced by immunizing rabbits with
-1-(0-carboxymethy1)oxime-bovine serum albumin conjugate (
-BSA), were removed of anti-BSA antibodies by quantitative precipitation reaction and further purified by ammonium sulfate precipitation and DEAE-Sephadex A-50 ion exchange chromatography. Purified IgG fractions were used as anti-
antibodies. The antibodies, whose titer was deterrnined extremely high above
, showed low cross-reactivity of 3~34% against
analogues such as G2, B2, and GI. From the standard curves of direct and indirect competitive ELISA for AFBI, the detection ranges were found 0.2~20 and 1~10, 000 ng/ml(ppb) respectively. In their sensitivity, stability, simplicity, and rapidity, the direct method was more suitable than the indirect method for practical use.
Relationship between the Organic Content and the Number of Sdphate-Reducing Bacteria in the Tributaries to the Han River
Microbiology and Biotechnology Letters, volume 20, issue 2, 1992, Pages 233~235
The number of sulphate-reducing bacteria (SRB) in some of the tributaries to the Han River was determined by the most probable number method using Postgate's Medium E.Higher number of SRB were obtained in the streams to which industrial waste water is discharged than those receiving only domestic waste water.