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REFERENCE LINKING PLATFORM OF KOREA S&T JOURNALS
> Journal Vol & Issue
Microbiology and Biotechnology Letters
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Journal DOI :
The Korean Society for Applied Microbiology and Biotechnology
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Volume & Issues
Volume 18, Issue 6 - Dec 1990
Volume 18, Issue 5 - Oct 1990
Volume 18, Issue 4 - Aug 1990
Volume 18, Issue 3 - Jun 1990
Volume 18, Issue 2 - Apr 1990
Volume 18, Issue 1 - Feb 1990
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Effectcs of Plant Growth Regulators on Growth and Berberine Production in Cell Suspension Cultures of Thalictrum rugosum
Microbiology and Biotechnology Letters, volume 18, issue 4, 1990, Pages 327~330
The effects of various plant growth regulators, both auxins and cytokinins, on cell growth and berberine production were investigated in cell suspension cultures of Thafictrum rugosum. Indole-%-acetic acid (IAA) was found to be the best for berberine production among five examined plant growth regulators and the optimum concentration of IAA was 1
. The enhancement compared to control 2, 4-dichlorophenoxyacetic acid (2, 4-D) was more than 60%. Simultaneous addition of cytokinins such as kinetin and 6-benzylamiroyurine (BA) was inhibitory.
Characteristics of Antitumorial Antibiotics B-1123 from Aspergillus terreus
Microbiology and Biotechnology Letters, volume 18, issue 4, 1990, Pages 331~337
An antitumor antibiotic named B-1123 substance was isolated from the culture filtrate of a new isolate fungus identified as Aspergillus terreus. The fermentation yield reached about 23 mg per liter of the broth. The B-1123 substance, chlorine containing antibiotic, has the molecular formular of
. Its structure was determined to be geodin by spectroscopic data. It is active against some Gram-positive bacteria and it prolongs the life span of mice inoculated with Ehrlich carcinoma.
Isolation and Structural Analysis of MB4-03, an
-Amylase Inhibitor Produced by Streptomyces sp. DMCJ-49
Microbiology and Biotechnology Letters, volume 18, issue 4, 1990, Pages 338~343
-amylase inhibitor was isolated from the culture broth of Streptomyces sp. DMCJ-49 and purified through ion-exchange chromatography, adsorption, and gel filtration. The results of various instrumental analyses showed that the inhibitor was one of oligosaccharides that had glucoses as its major component and that its molecular weight was about 2000. And one methyl group which seemed to be related with the inhibitory activity of this compound was identified. From the CMR spectrum, it was elucidated that this compound was composed of
-D-glucopyranoses which were linked together by
(I -, 4) bond configuration. As the inhibitory effect of this compound was reduced after incubation with
-amylase, the maltose units was seemed to exist at non-reducing terminal side of it.
Partial Purification and Characterization of the Alkaline Protease from Baccillus sp.
Microbiology and Biotechnology Letters, volume 18, issue 4, 1990, Pages 344~351
An alkalophilic microoganism producing a detergent-resistant alkaline protease was isolated from soil and identified as Baeiltus sp. The alkaline protease has been partially purified by ammonium sulfate fractionation, DEAE-Cellulose, CM-Cellulose and Sephdex G-100 column chromatography. The purified alkaline protease was highly active at pH 12-13 toward casein and stable at pH values from 6 to ll. The optimum temperature for the enzyme reaction was
. The enzyme was completely inactivated by diisopropyl fluorophosphate (DFP) indicating that the enzyme was serine protease, but considerabiy stable in the presence of surface active agents.
Synergistic Effect of Glucoamylase and
-Amylase in Enzymatic Hydrolysis of Raw Corn Starch in an Agitated Bead Reaction System
Microbiology and Biotechnology Letters, volume 18, issue 4, 1990, Pages 352~359
The synergistic effect of glucoamylase and a -amylase on the hydrolysis of raw corn starch in an agitated bead reaction system was studied by investigating the changes of sugar profiles, the granular structure, particle size distribution, and X-ray diffraction pattern of residual raw corn starch. The enzymatic hydrolysis of raw corn starch was greatly enhanced by synergistic effect of glucoamylase and
-amylase. Even though the sugar profiles were mainly determined by the mixing ratio of glucoamylase and
-amylase; raw starch was mainly converted to glucose directly without accumulation of any significant amount of oligosaccharides. The cavity formation and fragmentation phenomena of raw corn starch granule subjected to enzyme reaction were analyzed by means of SEM and the particle size distribution. The X-ray diffraction pattern of raw starch was not changed at the initial stage of reaction but slightly changed at the late stage of hydrolysis, which may be caused by the preferential degradation of amorphous region by enzymatic reaction, not by the destruction of microcrystalline structure of raw corn starch.
Purification and Some Properties of Rutinosidase from Arthrobacter sp.
;Toshio Omori;Tohru Kodama;
Microbiology and Biotechnology Letters, volume 18, issue 4, 1990, Pages 360~367
The several glycoside hydrolysing enzymes related to rutin degradation are found to be rhamnosidase, glucosidase and rutinosidase. Rutinosidase was purified to electrophoretic homogeneity from cell extracts of rutin-degrading strain, MT-57, which was identified as a Arthrobacter sp. Its molecular weight was estimated to be 42, 000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 40, 000 by gel filtration. The optimum pH for enzyme was found to be 7.5, and relatively stable in alkaline solution. The optimum temperature for enzyme was
, being stable up to
for 20 min. The Bm value of enzyme for rutin was 0.5
. The enzyme activity was increased by the chelating agent such as EDTA,
, and 8-hydroxyquinoline, was strongly inhibited by
. The enzyme had high substrate specificity in the rutinoside.
Purification and Characterization of the External Invertase Constitutively Produced by Rhodotorula glutinis K-24
Microbiology and Biotechnology Letters, volume 18, issue 4, 1990, Pages 368~375
Rhodoto& ghtbth~ K-24 was found to produce external invertase in addition to internal and cell wall bound invertase. External invertase was purified to an electrophoretically homogeneous state and partitally characterized and was compared with internal and cell wall bound invertase of which procedures for purification and characterization were reported previously. The enzyme was purified by ethanol precipitation, column chromatographies on DEAE-Sephadex A-50 and SP-Sephadex C-50, and gel filtration on Sephadex G-100. The molecular weight and subunit molecular weight of external invertasGwere estimated to be 220,000 and 100,000, respectively. The isoelectric point of the enzyme was about pH 6.0. The optimum pH and temperature for enzyme activity were pH 4.0 and
, respectively. The enzyme remained stable at the wide range, from pH 3.0 to 11.0 and stable up to
, but was inactivated at temperatures above that.
, SDS and p-CMB inhibited the enzyme activity. The
value of the enzyme for sucrose was
M. From these results, the three isozymes from Rh. glutinis K-24 seem to have the similar enzymatic properties, but to differ in molecular and subunit weights.
Purification of Cellulase Produced from Cellulomonas sp. YE-5
Microbiology and Biotechnology Letters, volume 18, issue 4, 1990, Pages 376~382
An extracellular cellulase producing bacterium YE-5 was isolated from soil, and identified as a Cellulomonas sp. by its taxonomical characteristics. The maximal activities of avicelase (0.35 units/ml), CMCase (3.18 units/ml), FPase (0.315 units/ml) and
-glucosidase (0.882 units/ml) were obtained when this strain was cultured for 48 hrs at
in a medium containing 0.8% (w/v) Solka floc, 0.06010 (wlv) urea, 0.1% (w/v)
, 0.1% (w/v)
, 0.2% (w/v) bacto peptone, 0.2% (w/v) yeast extract and pH 6.5. The cellulase was purified by ammonium sulfate fractionation, DEAE-Sepharose column chromatography and Sephadex 6-100 column chromatography from culture filtrate of Cellulomonus sp. YE-5. The molecular weights of purified avieelase, CMCase I, and CMCase II were estimated to be about 95,000 ~ 105,000, 46,000 ~ 47,000 and 120,000 ~ 125,000, respectively.
Effect of Cellobiose Octaacetate, Avicel, and KC-flock on Production of Avicelases from Penicilliurn verruculosum
Microbiology and Biotechnology Letters, volume 18, issue 4, 1990, Pages 383~389
During the cultivation of Penkillium uerrmulosum in the media containing cellobiose octaacetate (COA), avicel, or KC-flock as an inducer and as a sole carbon source for 21 days, cellulolytic activity and SDS-PAGE pattern of proteins in the culture broth were investigated. Protein concentration and cellulolytic activity were highest in the COA medium. As cultivation period was increased, protein content and avicel hydrolytic activity of culture broth were increased as similar extent but neither
-glucosidase nor CMC hydrolytic activity was correlated to protein content. When crude proteins from the culture broth were separated on DEAE column by HPLC, distribution of avicel-hydrolytic activities were well correlated with that of major proteins. From those results it was suggested that three major proteins having 60 K, 68 K, and 76 K of Mr. were avicel-hydrolytic enzymes.
Purification of Trichoderma viride Cellobiohydrolase by Immunoaffinity Chromatography
Microbiology and Biotechnology Letters, volume 18, issue 4, 1990, Pages 390~393
A cellobiohydrolase was purified from the culture broth of Trichoderma uiride by using immunoaffinity chromatography. A single protein band in polyacylamide gel electrophoresis and isoelectrofocusing after immunoaffinity purification corresponded to cellobiohydrolase activity. A immunoaffinity purified cellobiohydrolase is more effective in the hydrolysis of highly crystalline cellulose than amorphous cellulose.
Optimization of Switching Time from Growth to Product Formation for Maximum Productivity of Recombinant Escherichia coli Fermentation
Anant Y. Patkar ;
Microbiology and Biotechnology Letters, volume 18, issue 4, 1990, Pages 394~400
Maximization of productivity of recombinant cell fermentations requires consideration of the inverse relationship between the host cell growth rate and product formation rate. The problem of maximizing a weighted performance index was solved by using optimal control theory for recombinant E. coli fermentation. Concentration of a growth inhibitor was used as a control variable to manipulate the specific growth rate, and consequently the cloned-gene expression rate. Using a simple unstructured model to describe the main characteristics of this system, theoretical analysis showed that the optimal control profile results in an initial high growth rate phase followed by a low growth rate and high product formation rate phase. Numerical calculations were done to determine optimal switching times from the growth to the production stage for two representative cases corresponding to different dependency of the product formation rate on the growth rate. For the case when product formation rate is sensitive to the specific growth rate, the optimized operation yields about 60% increase in the final product concentration compared with a simple batch fermentation.
Metabolic Control of Maintenance for the Production of pro-Urokinase from Human Thyroid cells
Microbiology and Biotechnology Letters, volume 18, issue 4, 1990, Pages 401~405
Maximum specific pro-UK production rate was achieved at 15 mllmin of perfusion rate as
/h/cell by cytostatic cultivation of human cell line 579 with DMEM and 590 FBS. As perfusion rates were increased, glutamine uptake rates were also increased but ammonium production rates remained relatively constant, which resulted in low ratio of ammonium to glutamine at high perfusion rate. Partially it quantitatively explains why the productivity is increased in perfusion cultivations. At maintenance period of 15 days by controlling metabolic process, such as 5 mM of glucose, 2 mM of gtutamine, 10% of air saturation and pH 6.2, high speecific product production rate and product yield on substrate were obtained as
/h/cell abd 0.226 mglg of glucose, respetively. This product yield corresponds to 0.223 mg/day of productivity at 10 mllmin of perfusion rate.
Controlled Expression of Promoter from Alkali-tolerant Bacillus sp. DNA in Fed-batch Culture
Microbiology and Biotechnology Letters, volume 18, issue 4, 1990, Pages 406~410
The influence of glucose concentration on cell growth rate and on the expression level of the strong promoter obtained from alkali-tolerant Bacillus sp. YA-14 chromosomal DNA was studied. In fed-batch culture, the promoter activity could be maximized by maintaining a very low level of glucose concentration in the broth and glucose consumption rate below 1.08g/g cell-h. The induction of the promoter was possible by addition of sporulation medium after the cell was grown in growth medium with only low level of CAT activity.
The Production of 1,4-Androstadiene-3,17-Dionefrom Sterols by Brevibacterium erythrogenes
Microbiology and Biotechnology Letters, volume 18, issue 4, 1990, Pages 411~416
Microbiological conversion of sterols to 17-ketosteroids has been recongnized as a source for commerical preparation of steroidal drugs. For the purpose of strain development, we isolated microorganisms through enrichment culture method and identified an isolate strain. The strain was closely related to Brevibacterium ergthrogenes. The optimal conditions for 1, 4-androstadiene-3, 17-dione (ADD) formation were as follows; pH 7.4, lactose 0.2%, beef extract 0.2%, bentonite 0.5% in the chlolesterol fermentation medium. Maximum production was obtained with the addition of
'-dipyridyl (1 mM, final conc.) at 17-20 hours after incubation.
Optimum Culture Conditions for the Production of Fructosyl transferase by Aureobasidium pullulans C-23
Microbiology and Biotechnology Letters, volume 18, issue 4, 1990, Pages 417~422
For optimal production of fructosyl transferase in AureobasidiumpuZZulane C-23, the effect of fermentation conditions for cell growth and fructosyl transferase production were investigated. Sucrose was excellent carbon source. Sucrose concentration for the optimum production of fructosyl transferase was 35%. Enzyme productivity was significantly increased by addition of ammonium oxalate and yeast extract. A time course study for the enzyme production by Aureobasidium pullutans C-23 was carried out. At 2 days incubation, the production of intracellular enzyme was maximum. The extracellular enzyme production was found to be increased up to 6 days.
Degradation of Phytic acid in Chungkookjang Fermented with Phytase-producing Bacteria
Microbiology and Biotechnology Letters, volume 18, issue 4, 1990, Pages 423~428
Three strains among 8 isolates from the fermented chungkookjang were shown the strong phytase productivities. The phytase activities in manufacturing chungkookjang with thrse bacteria were maximized after incubating at 35-
, pH 7.0 for 5 day. The contents of same amino acids and riboflavin were increased in chungkookjang manufactured with these phytase-producing bacteria and the rate of phytic acid degradation was much higher in chungkookjang manufactured with a single or mixed cultures of these bacteria than in traditional chungkookjang.
Expression of Developmentally Regulated Promoter of Alkali-tolerant Bacillus sp. YA-I4
Microbiology and Biotechnology Letters, volume 18, issue 4, 1990, Pages 429~432
The promoter isolated from chromosomal DNA of an alkali-tolerant Bacillus sp. YA-14 was subcloned and biochemically characterized. Also the relationships between the promoter activity and sporulation were investigated. In alkali-tolerant Bacillus sp. and Bacillus subtilis, the activity of promoter began to increase at the onset of sporulation with the same mode, and repressed in the presence of 1.0% (wtv) glucose. Among five spoO genes, three epoO genes (spoOB, spoH, spoOJ) were required for promoter expression.
DNA Rearrangement of TOL Plasmid in Pseudomonas putida PpGl Harbouring CAM Plasmid
Microbiology and Biotechnology Letters, volume 18, issue 4, 1990, Pages 433~436
The TOL plasmid, pWWO, conjugally transferred from Pseudomonas putida mt-2 was dissociated into TOL* and TOL
A in P. putidu PpGl carrying CAM plasmid. The TOL* was integrated into the CAM plasmid, and the resulting plasmid was designated as CAM::TOL*. The introduction of NAH plasmid, belonging to Inc P9 incompatibility group, into P. putida CSTBA carrying CAM::TOLt plasmid and TOL A plasmid did not affect m-toluate catabolism, but resulted in expelling the TOL
Increased Antifungal Activity with Genetic Development of Antagonistic Pseudomonas stutzeri YPL-1 against Fusariym solani
Microbiology and Biotechnology Letters, volume 18, issue 4, 1990, Pages 437~441
For the genetic development of more powerful antagonistic Pseudomom - YPL-1 as a biocontxol agent against soilborne plant pathogenic Fuaarium solani causing root rot of many important crops, mutants improving the productivity of chitinase were obtained by mutation with UV radiation or NTG treatment, P. stutzeri YPL-M26 (UV mutant) and P. stutzeri YPL-MI78 (NTG mutant) could improve the productivity of chitinase by 2.5 and 2.0 times, and its antifungal activity by 1.7 and 1.5 times, respectively. The antifungal mechanism of P. stutzeri YPL-M26 was caused by lysis of the fungal cell wall by hydrolytic enzymes such as chitinase. The antifungal activity of crude chitinase of P. stutzeri YPLM26 on the mycelial growth of F. solani was observed to be much higher than that of the original strain. The enzymes produced by P. stutzeri YPL-M26 were the same as the original strain in enzymatic properties such as optimal pH and temperature.