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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
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Volume & Issues
Volume 16, Issue 6 - Dec 1988
Volume 16, Issue 5 - Oct 1988
Volume 16, Issue 4 - Aug 1988
Volume 16, Issue 3 - Jun 1988
Volume 16, Issue 2 - Apr 1988
Volume 16, Issue 1 - 00 1988
Selecting the target year
Purification and Properties of Extracellular Inulinase of Pseudomouas sp.
Microbiology and Biotechnology Letters, volume 16, issue 4, 1988, Pages 259~264
Two forms of extracellular inulinase, designated as PI and PII were detected in the crude enzyme preparation from n species of Pseudomonas isolated from soil. PI and PII were purified to homogeneity by ammonium sulfate fractionation, DEAE Sephadex A-50 chromatography, Sephadex G-100 and Sephadex G-200 gel filteration. Both isoenzymes catalyzed specifically and endowise the cleavage of the
-2,1-fructofranoside linkage of inulin, and displayed no action upon sucrose, raffinose and levan. The optimal pH values for the PI and PII enzyme were pH 5.5 and 6.0, respectively and the highest activity of the two enzymes was observed at 55
. The Km values of PI and PII were calculated to be 2
M and 5
Screening of Thermotolerant Yeast Strain for Ethanol Fermentation
Ryu, Beung-Ho ; Nam, Ki-Du ; Kim, Hae-Sung ; Kim, Dong-Seuk ; Ji, Young-Ae ; Jung, Soo-Ja ;
Microbiology and Biotechnology Letters, volume 16, issue 4, 1988, Pages 265~269
For the purpose of developing new thermotolerant yeast strains for ethanol fermentation, yeasts were isolated from molasses and screened for their fermentation ability at elevated temperatures. Three candidate strains were screened. These strains preferred pH 5.0 and 34
for their ethanol production. Under such conditions the three strains showed average ethanol productivity of 75g ethanol per liter of fermentation broth in n synthetic medium containing glucose as substrate. These strains were identified as Saccharomyces cerevisiae and Kluveromyces marxianus.
Incidence of Plasmids in Marine Bacteria Isolated from the Bunker-C Oil Enriched Culture
Park, In-Sick ; Park, Jung-Youn ; Jin, Deuk-Hee ; Hong, Yong-Ki ;
Microbiology and Biotechnology Letters, volume 16, issue 4, 1988, Pages 270~274
Samples used for the enrichment culture were collected from the sea water of suspected chronic petroleum contamination in the vicinity of Pusan, Chungmu and Ulsan ports, Korea. Alkaline Iysis and agarose gel electrophoresis techniques were employed to screen these isolates for the presence of plasmid DNA. There were n little differences in the percentage of isolates containing plasmids between sampling sites of unpolluted sen water (22％) and polluted son water (25％). Bacterial isolates taken from the Bunker-C oil enriched culture showed significantly more plasmid incidence (29％). About two thirds of strains grown on a variety of hydrocarbons were Gram negative strains of which 33％ contained one or more plasmids. Multiple plasmids were observed in 23％ of the plasmid-carrying strains. Forty one percent of the plasmids detected were estimated to have a mass of 20 kb or more.
Intrageneric Protoplast Fusion between Alkalophilic Bacillus sp. F204 and Bacillus sp. K 17
Microbiology and Biotechnology Letters, volume 16, issue 4, 1988, Pages 275~281
To develop cellulase and xylanase-producing strain by protoplast fusion, alkalophilic Bacillus sp. F204 and K17 were treated with NTG(N-methyl-N'-nitro-N-nitrosoguanidine) and isolated anti-biotics resistant strains of S20 (Km
) and G70 (Str
). The frequency of protoplast formation was about 95% when cells of mid-log phase were treated with 200
/ml Iysozyme at 37
for 30-45 minutes. Under addition of 0.4-0.5M sodium succinate, 0.5% casamino acid, 1.5% polyvinylpyrrolidone, 25mM MgC1
and 50mM CaC1
to the regeneration medium, the regeneration frequency of Bacillus sp. F204 and K17 was 24.9% and 26.2%, respectively. The fusion frequency was 6.6
in the presence of 30% polyethylene glycol 6000 containing 50mM
for 5 minutes. Cellulase complex and xylanase activities of fusant were compared with parental strains.
Kinetics of Cultivating Large Quantities of Mammalian Cells
Microbiology and Biotechnology Letters, volume 16, issue 4, 1988, Pages 282~286
Growth kinetic parameters for mass cultivation of Chinese Hamster Ovary (CHO) cells are estimated by measuring oxygen uptake rates. It Is found that there is strong correlation between cell growth and oxygen consumption, showing that correlation factor is 0.83. Derived linear model predicts actual cell density very well. It tells that oxygen uptake rate can play important role in indirectly measuring cell density when conventional method of estimating cell density is no longer meaningful due to heavy cell clumpings. Cell yield per oxygen consumption,
and mass transfer coefficient for oxygen, Ka are also estimated as 1.26
consumed and 1.01/h, respectively. Average specific growth rate over all runs is 2.891/day for CHO cells with producting 2 grams of tPA per day under continuous perfusion operations.
Interaction between Lactobacillus acidophilus and Kluyveromyces fragilis on the Metabolism of Amino Acids in Soymilk
Microbiology and Biotechnology Letters, volume 16, issue 4, 1988, Pages 287~292
The interaction between Lactobacillus acidophilus and Kluyveromyces fragilis on the utilization of amino acids in soymilk was investigated. K. fragilis assimilated relatively well various amino acids such as Met., ILe., Phe., Leu., Thr., Lys., Val., Arg., Tyr., Ser., Asp., Ala. and Glu. that existed only in trace amounts in soymilk. K. fragilis did not utilized Gly., while hi accumulated His. L. acidophilus hydrolyzed soyprotein to liberate various amino acids. Among various amino acids, it utilized Met., ILe., Thr., Tyr., Ser., Val. and His. as growth factors and accumulated Leu., Phe., Lys., Arg., Glu., Asp. and Ala. among the essential amino acids required by K. fragilis and Gly. These results implied that K. fragilis grew on amino acids that existed only in trace amounts in soymilk, but it's growth was stimulated by amino acids such as Leu., Phe., Lys., Arg., Glu., Asp. and Ala. ac-cumulated by L. acidophilus.
Stability of Spheroplasts from Saccharomyces cerevisiae D-71 and Zygosaccharomyces rouxii SR-S
Microbiology and Biotechnology Letters, volume 16, issue 4, 1988, Pages 293~296
Stability of spheroplasts prepared from Saccharomyces cerevisiae D-71, a thermophilic strain and Zygosaccharomyces rouxii SR-S, an osmotolerant strain were studied. Stability of spheroplast from Saccharomyces cerevisiae D-71 was highest in 0.8M KCI and 1.0M sorbitol ; that from Zygosaccharomyces rouxii SR-S was highest in 0.4M KCI and mannitol and that from both strains was less than 10% for sonic oscillation at 20Kc for 60 sec. In centrifugation at 10000 x g for 10 min., stability of spheroplast from Saccharomyces cerevisiae D-71 was 93% and that from Zygosaccharomyces rouxii SR-S was 84%. Breakage of spheroplast from Saccharomyces cerevisiae D-71 was 99% and that from Zygosaccharomyces rouxii SR-S was 55% for UV irradiation with 15W UV lamp at a distance of 20 cm for 60 min.
Characterization of Fusant from Protoplast Fusion between Saccharomyces cerevisiae D-71 and Zygosaccharomyces rouxii SR-S
Microbiology and Biotechnology Letters, volume 16, issue 4, 1988, Pages 297~302
The protoplasts of Saccharomyces cerevisiae D-71, a thermophilic strain and Zygosaccharomyces rouxii SR-S, an osmotolerant strain were fused, and a fusant (FS-RN 1) was selected, then was characterized for its genetic stability, DNA content, cell capacity, growth rate, tolerance to salts and chemicals,
-fructofuranosidase level and ethanol fermenting activity. After 6 months of preservation, 5.8% of the fusant clones were segregated to parental types. The DNA content and cell capacity of the fusant were greater than those of the parental strains. Lag period of growth for the fusant was longer than those for the parents. The fusant colonies showed pink-color reaction to triphenyltetrazolium chloride(TTC) test. The fusant appeared to have resistances to NaCl at moderate levels between both parental strains, and resistances to KCI, sodium propionate and cycloheximide similar to either one of the parents.
-Fructofuranosidase activity of the fusant was 24.2
/IU/g(dry wt) for 3 days culture. Ethanol yields ofter 4 days of fermentation by the fusant at 3
were : 6.0%(v/v) from 40% of glucose and 8.8%(v/v) from 20% of sucrose.
Protoplast Regeneration and Interspecific Fusion of the Genus Cellulomonas
Microbiology and Biotechnology Letters, volume 16, issue 4, 1988, Pages 303~309
In order to establish the process of interspecific protoplast fusion of the genus Cellulomonas capable of utilizing of cellulose, C. flavigena NCIB 12901 and Cellulomonas sp. CSI-1, the optimum conditions for the regeneration and fusion were examined. The condition of suitable osmotic stabilizer for the protoplast regeneration of C. flavigena was established by using 0.4M sorbitol. And then, by addition of 3% po]yvinyl pyrrolidone (PVP) to cell wall regeneration medium, regeneration frequency was increased 3 times higher than that without PVP addition. The optimum conditions for the interspecific protoplast fusion between auxotrophic and antibiotics resistant mutants were obtained with 40%(W/V) of PEG (polyethylene glycol) 6000 as the fusogenic agent and 25mM of CaCl
on treating time for 15 min. The fusion frequency between mutants was from 2.0
under the optimum conditions. The fusants were confirmed to revert from protoplast to cells of rod type during regeneration process and the aggregation of protoplast by PEG was observed. Also the progress of fusion was observed by scanning electron microscopy, Many isolated fusants were shown to be complement clones of both parents which occured at a high frequency among the isolated clones.
Properties of Chorismate Mutase from intrasporangium sp.
Microbiology and Biotechnology Letters, volume 16, issue 4, 1988, Pages 310~315
Two isoenzymes of chorismate mutase(E.C.188.8.131.52) designated as chorismate mutase I(CM I) and chorismate mutase II(CM II), were detected and partially purified from a sp. of intrasporangium isolated from soil. CM I and CM II had pH optima of pH 6.5 and 8.0, respectively and showed the same temperature optimum of 45
. The activation energy of the enzymatic reaction was estimated to be 14.7kcal/ mole with CM I and 10.8kcal/mole with CM II. The affinity of isoenzyme CM I for substrate(Km= 1.35mM) was almost the same level as that of CM II(Km = 1.22mM). Both isoenzymes were stable at pH values ranged from pH 6.5 to 9.0, but rapidly denaturated at temperatures above 45
. CM II was activated about 7
of its activity by
while CM I was slightly inhibited by the same metal ions. Thiol compounds were found not to be necessary for stability of the two enzymes but Co
and EDTA had a little stabilizing effect on CM II only. p-Chloromercuribenzoate strongly inactivated the activities of both enzymes but the reducing agents such as dithiothreitol and L-cysteine protected them against the pCMB inhibition.
Cloning of Pectate Lyase Gene of Alkali-tolerant Bacillus sp. YA-14 and Its Expression in Escherichia coli
Yu, Ju-Hyun ; Park, Yoon-Suk ; Kim, Jin-Man ; Kong, In-Soo ; Chung, Yong-Joon ;
Microbiology and Biotechnology Letters, volume 16, issue 4, 1988, Pages 316~319
Pectate Lyase (PL) was cloned from alkali-tolerant Bacillus sp. YA-14 into Escherichia coli MB1000 by inserting HindIII-generated DNA fragment into the HindIII site of pBR322 and then screening recombinant transformant for the ability to hydrolyze sodium polypectate on agar plate, The recombinant plasmid, called pYPC29, was isolated, and the size of the cloned HindIII fragment was found to be 1.6 kb. The PL gene was stablely maintained and expressed efficiently in Escherichia coli. The Pt accumulated largely in the periplasmic space of Escherichia coli clones.
Properties of Glucoamylase Isozymes Produced by Aspergillus sp.
Park, Inshik ; Youngho Chung ;
Microbiology and Biotechnology Letters, volume 16, issue 4, 1988, Pages 320~326
Glucoamylase (EC 184.108.40.206) of Aspergillus sp. isolated from soil was partially purified by Sephacryl S-200 gel filtration and DEAE-Sephacel ion exchange chromatography, The glucoamylase activity was separated into two isozymes after DEAE-Sephacel ion exchange chromatrography. The optimum pH and temperature for both glucoamylase isozymes (GI, GII) were identical; pH 4.5 and temperature,
. The molecular weights of GI and GII Isozymes were estimated to be 105,000, which were measured by gel filtration on Sephacryl S-200. Both isozymes were stable at pH ranges of 2 to 7, and up to 6
. Glycerol was effective to stabilize the both isozymes. The activation energies of GI and GII isozymes were 10.63 and 10.33 kcal/mole, respectively. The enzyme activities of both isozymes were completely inactivated by addition of 0.1% Hg
. In kinetic studies, the Km values of GI isozyme for soluble starch, dextrin, and glycogen were 0.62%, 0.32%, and 1.02%, respectively. For GII isozyme, they became 0.66%, 0.23%. and 0.14% for the substrates.
Optimization of Fermentation Conditions for Production of Recombinant Human Interleukin-2 in Escherichia coli
Lee, In-Young ; Kim, Myung-Kuk ; Na, Doe-Sun ; Hahm, Kyung-Soo ; Moon H. Han ; Lee, Sun-Bok ;
Microbiology and Biotechnology Letters, volume 16, issue 4, 1988, Pages 327~333
For optimal production of recombinant human interleukin-2 (IL-2) in E. coli the effect of fermentation conditions on cell growth, IL-2 production, and stability of recombinant cells were investigated. Among the complex nutrients tested in this work, yeast extract, peptone and corn steep liquor were found to be effective for recombinant cell growth. The recombinant cells were maintained stably under repression condition (3
), but the stability of recombinant cells were drastically reduced upon induction of IL-2 expression (42
) even under the selection pressure. Addition of antibiotics to the culture medium resulted in the cell growth inhibition without significant improvement in recombinant stability. When the expression of IL-2 gene was induced at different growth phases, highest IL-2 production was achieved by the induction of IL-2 at the middle-exponential growth phase. It was found that the production of IL-2 significantly inhibited the cell growth and the ex-pression of other genes in the plasmid.