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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 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
Selecting the target year
Screening and Identification of a Potent Fungus for Producing Raw Corn Meal Saccharifying Enzyme
Microbiology and Biotechnology Letters, volume 18, issue 6, 1990, Pages 547~552
We have been searching microorganisms which produce highly active raw starch saccharifying enzyme and also have a good cultivation characters in submerged culture. About 170 strains of molds isolated from soil and compost were tested for their amylase productivity on plate contained 2% raw corn meal. Thirty-four strains out of 170 strains produced clearance on the plates, and were tested for their raw starch saccharifying activity. Then, 4 strains which had shown relatively high levels of saccharifying activity were selected. Among them, Strain No. 55 was found to have highest level of raw starch saccharifying activity, and selected for the further studies. In this paper, the morphological, physiological and cultural characteristics of Strain No. 55 were described. Based on the results obtained in these experiments, Strain No. 55 was identified to be a similar species to Aspergillus niger.
Isolation and Identificatioh~ of a Phthalate Ester Degrading Bacterium and the Optimal Culture Conditions for Production of One Degrading Enzyme
Microbiology and Biotechnology Letters, volume 18, issue 6, 1990, Pages 553~559
A strain degrading phthalate ester was isolated from a sludge of Taegu area and identified as a strain of Klebsiella. The optimum culture conditions for the protocatechuate dioxygenase production were also investigated. This strain produced the enzyme in question under the shaking cultivation at
for the 48 hrs in the medium containing 0.1% protocatechuate as the sole carbon source, 0.1% ammonium sulfate and 0.1% yeast extract as the nitrogen source and mineral salt mixture of magnesium sulfate, sodium chloride, calcium chloride, ferric chloride, manganese sulfate, zinc sulfate and cupric sulfate. This enzyme was intracellularl j localized and probably linked to cell membrane, and induced by protocatechuate.
Transformation of Trichoderma koningii Using Isolated Nuclei
Microbiology and Biotechnology Letters, volume 18, issue 6, 1990, Pages 560~565
When protoplasts from auxotrophie mutant of Trkhoderma koningii CUT121(Lys-, Met-) were mixed with isolated nuclei of wild type T. koningii ATCC 261 13 and treated with PEG solution, protrophic colonies were produced with frequency of more than 30 percent. One of segregants from prototrophic colonies showed increased xylanase activity and other polysaccharide-hydrolyzing activities comparable to those of wild type strain. Through measurement of DNA contents, induced segregation, and analysis of isozyme patterns, it was revealed that the prototrophic colonies were transformants resulted from exchange of genetic materials between the two kinds of nuclei used. These results suggest that nuclei transfer technique is more efficient than conventional protoplast fusion technique for strain improvement of Trichoderma species.
-galactosidase Biosynt hesis in Lactobacillus sporogenes
Microbiology and Biotechnology Letters, volume 18, issue 6, 1990, Pages 566~570
-galactosidase formation was studied with Lactobacillus sporogenes. Synthesis of the enzyme was effectively induced by isopropyl-
-D-thiogalactopyranoside (IPTG) or galactose, and to a much lower level by lactose. When 15 mM glucose was added at the different intervals to the cultures that had been in contact with IPTG, the same levels of inhibition of the enzyme synthesis were observed (approximately one-third the differential rate of a control culture without glucose). This suggests that glucose did not interfere with the entry of the inducer into the cells, but interfere with the formation of
-galactosidase through catabolite repression. The glucose inhibitory effect was not overcome by adding CAMP or cGMP to the culture media.
Anticomplementary and Antitumor Activities of the Alkali Extract from the Mycelia of Lentinus edodes 1'11105
Microbiology and Biotechnology Letters, volume 18, issue 6, 1990, Pages 571~577
Alkali extract obtained from mycelia of Lentinus edodes IY105 was shown to have potent anticomplementary activity and alternative complementary activity in vitro. It was also shown to activate reticuloendothelial system of ICR mice in the carbon clearance. Amount of carbohydrates and protein of the extract were 17% and 42% respectively. It was found that carbohydrates were consisted of 5 monosaccharides and protein was consisted of 16 amino acids. Antitumor activity was observed in the alkali extract treated group of sarcoma 180 bearing ICR mice.
Produ cti on of Cyclomaltodextrin from Bacillus stearothermophilus
Microbiology and Biotechnology Letters, volume 18, issue 6, 1990, Pages 578~584
A microorganism capable of producing high level of extracelluar cyclomaltodextrin glucanotransferase(EC 18.104.22.168; CGTase) was isolated ’rom soil. The isolated strain No. 239 was identified as Bacillusstearothermophilus. The maximal CGTase production (about 7.0 unitslml) was observed in medium containing2% soluble starch, 0.5% defatted soybean meal, 0.1%
with initial pH 7.0. The strain was cultured at
for 48 hr with reciprocal shaking. At 0.83% substrated concentration potato starch was the optimum substrate with 50.1% conversion to cyciodextrin (CD)after the reaction at
for 24 hr (CGTase 10 unitlg starch). Using soluble starch as substrate (5% substrate concentration, CGTase 10 unitlg starch), the maximum conversion of 40% was obtained at11 hr reaction, and the ratio of
-CD production at this time were 1.0:1.3:0.4, respectively., respectively.
Cyclodextrin Glucanotransferase from Bacillus stearothermophilus:Purification by Affinity Chromatography and Its Properties
Microbiology and Biotechnology Letters, volume 18, issue 6, 1990, Pages 585~590
The cyclodextrin glucanotransferase (CGTase) was purified from the culture broth of Bacillus stearothermophilus by ammonium sulfate precipitation and affinity chromatography. The specific activity of the CGTase increased by about 31-fold from 111.5 U/mg protein to 3445.0 Ulmg protein. The SDSPAGE indicated that the purified CGTase was homogeneous and the molecular weight of the purified CGTase was about 78,000. The optimum pH and temperature was 6.0 and
, respectively. This enzyme was stable from pH 5.5-10.0. The enzyme retained its full activity at the incubation temperature up to
and calcium ion increased the thermal stability. The isoelectric point was about 4.8.
Production and Properties of Tannase from Lenzites betulina
Microbiology and Biotechnology Letters, volume 18, issue 6, 1990, Pages 591~598
Six species under the basidiomycetes were screened for extracellular tannase (tannin acyl hydrolase EC 3.1. 1.20) production in submerged culture and Lenzites betulina was found to be most effective for the production of tannase. The optimum cultural conditions for tannase production were
, pH 6.0 and 21 days of culture period, The efficient composition of culture medium for the production of tannase was performed in synthetic medium containing tannic acid, 2g; sucrose, 5g; bacto-peptone, 2g; ,
, 2 mg; thiamine HCl, 100 ug and distilled water 100 ml, The tannase produced from Lenzites bdulin*r was 223.3 unit (umole of gaUic acidiml of brothlmin). The tannase had an optimal reaction conditions ofpH 6.0 and temperature of
. The enzyme was stable at temperature below
and lost its activity by 50% above
. And the stable pH range was 5.5 to 6.0.
The Production and Purification of Chitinase from Aeromonas salmonicida YA7-625
Microbiology and Biotechnology Letters, volume 18, issue 6, 1990, Pages 599~606
A chitinase-producing bacterium, Aeromonas salmonicida YA7-625, was isolated from domestic seashore muds. The preferable medium composition for the production of chitinase was as follows: colloidal chitin 1.26% (w/v), tryptone 2.95% (w/v),
0.15% (w/v) and
, 0.15% (w/v) (pH 8.5). The highest enzyme production was observed after cultivation of 48 hours at 27OC. The chitinase of Aeromonas salmonicida YA7-625 was purified successively by ammonium sulfate precipitation, affinity adsorption, hydroxylapatite column chromatography and gel filtration. The optimal temperature and pH for the activity of purified chitinase were
and 7.0, respectively. The molecular weight of purified chitinase was ca. 200,000 daltons and apparent Km value of it was 1.276 mglml on colloidal chitin
Alcaligenes eutrophus 균주의 성장과 Poly-Beta-hydroxybutyrate 합성에 미치는 포도당과 암모늄농도의 영향
Microbiology and Biotechnology Letters, volume 18, issue 6, 1990, Pages 607~612
The biodegradation of Aroclor 1242 was investigated by the mixed cultivation of the natural bacterial isolates and a genetically engineered microorganism (GEM). The natural strain of MS-1003 degraded the Aroclor 1242 through the ortho-cleavage pathway, while the other strains through the meta-cleavage pathway. When the MS-1003 strain was additionally inoculated into the 1 day culture of the DJ-26 strain and then cultivated for 2 days, the Aroclor was degraded up to 86% and resulted in increase of the meta-cleavage product. But in the MS-1003 culture inoculated with the DJ-26, degradation of the Aroclor was limited to the level of each pure culture. By the mixed cultivation of the DJ-26 strain together with the DJ-12 or its GEM strain of DF-10, which degrades the Aroclor through the meta-cleavage pathway, degradation of the Aroclor as well as production of the meta-cleavage compound were lower than those of each pure culture. The degradation of Aroclor 1242 by the GEM strain was not improved over the parental strain. Therefore, a form of cometaboiism of Aroclor 1242 was found in the mixed culture of the DJ-26 and MS-1003 strains which degrade the Aroclor through the different metabolic pathway, but in the mixed culture of the DJ-26 and DJ-12 strains degrading Aroclor 1242 through the same pathway, a kind of competetion for the substrate was observed.
Inhibitory Effect of Nisin upon Kimchi Fermentation
Microbiology and Biotechnology Letters, volume 18, issue 6, 1990, Pages 620~623
To examine the inhibitory effect of nisin on Kimchi, comparison of the fermentation pattern was studied between the Kimchi added nisin (100 WIg) and the control Kimchi at 15cC. The Kimchi added nisin was showed pH 4.03 at 7 days fermentation, on the other hand the control Kimchi showing pH 4.04 at 5 days. And total acidity (lactic acid%) showed 0.47,0.69,0.88 at 5,9, 14 days fermentation compared with the control Kimchi showing 0.57,0.93, 1.13 respectively. Maximum growth of lactic acid bacteria on the control Kimchi indicated 1.8, 1.6 x 108 CFU/ml at 7 days but on presence of nisin indicated 9.5,6.4 x 107 CFU/ml at 5 days. In conclusion, nisin showed inhibitory action to Kimchi fermentation from pH, total activity and lactic acid bacteria count results.
New Antibiotics Produced by SEreptomyces mekmosporofaciens I. Taxonomy of the producing microorganism
Microbiology and Biotechnology Letters, volume 18, issue 6, 1990, Pages 624~632
Strain 88-GT-161 producing new phthalic acid derivative and basic macrolide antibiotics was identified as being S. melanosporofuciens based on numerical taxonomic data. However, 4 unit characters among 139 units were clearly different from the common properties of 6 strains belonging to cluster No. 32 represented by the name of S. violaceoniger or S. violaceusniger, leading us to designate as a variety of S. melunosporofaciens. This paper describes the taxonomic characteristics of the strain. Isolation and chemical structures, including biological activities of the active compounds produced by this strain will be presented elsewhere.
Molecular Cloning and Expression of Cellulase of Gene of Pseudomonas sp. in Escherichia coli
Microbiology and Biotechnology Letters, volume 18, issue 6, 1990, Pages 633~639
The genes for cellulases of Pseudomonas sp. LBC505 and CYC10, potent cellulase complex-producing strains, were cloned in Escherichia coli with pUC19. Recombinant plasmids pLCl and pLC2 were isolated from transformants producing cellulase by Congo red staining, and their genes cloned were 0.7 kb and 4.6 kb HindIII fragments, respectively. The inserts of pLCl and pLC2 were hybridized to chromosomal DNAs digested with HindIII from Pseudomona~ sp. LBC505 and CYC10, respectively. Immunodiffusion assays revealed that pLC1-and pLC2-encoded cellulase showed similarity with that of host strains. About 24% of cellulase activity was observed in the extracellular fraction of E. coli carrying pLC1, and its activity was higher about 1.4 times than that of LBC505. The enzymatic properties of pLC1 and pLC2 encoded cellulase were the same as those of cellulase from host strains. HPLC analysis and substrate specificity showed that cellulases were the same as those of cellulase from host strains. HPLC analysis and substrate specificity showed that cellulases cloned were endocellulase.
Molecular Cloning of Escherichia coli cdd Gene Encoding Cytidine/Deoxycytidine Deaminase.
Microbiology and Biotechnology Letters, volume 18, issue 6, 1990, Pages 640~646
We have cloned the cdd gene from E. coli C600 using (cdd-) as a host. From the sequenced promoter region of E=, coli cdd gene which has been determined by Valentin-Hansen P. (1985), we synthesized the 23 mer oligonucleotides corresponding to the transcription initiation region and used as a probe for cloning of the cdd gene by Southern blotting. The isolated fragments in the blotting were introduced to the colony hybridization after transforming it into the E. coli JF611 (cdd-, pyr double mutant), and we identified the hybridized band at 27 kb long. From the original insert of 27 kb fragment in theBamHI site of pBR322, the 5.3 kb fragment containing the cdd gene was isolated by subsequent deletion and subeloning. From the derived plasmid pTK509, further deletion and subcloning were performed and clarified that the cdd gene was located in the 2.1 kb of SaZI/DraI segment in the insert of pTK605. The polypeptide encoded by the cloned DNA was appeared to be a molecular mass of 33,000.
Transfer of Insecticidal Toxin Gene in Plants:Cloning of Insecticidal Protein Gene in Bacillus thuringiensis
Microbiology and Biotechnology Letters, volume 18, issue 6, 1990, Pages 647~652
The production of delta-endotoxin crystal and the cloning of endotoxin protein gene in Bscillus thuringiensis subsp. kurstaki HD1 strain were studied. The strain produced bipyramidal crystals (
) in their cells during sporulation. The B. thuringiensis contained about 10 plasmid DNA elements ranging from 2.1 to 80 kilobases. The 73 kb plasmid DNA, the 29 kb BamHI fragment and the 7.9 kb Pstl DNA fragment hybridized to the pHL probe. The 7.9 kb fragment was eluted and cloned in the PstI site of pBR322 vector and transformed into E. coli HB101, which produced insecticidal proteins killing Bornbyx mori larvae.
Cloning and Expression of Schwanniomyces castellii Starch Gene
Microbiology and Biotechnology Letters, volume 18, issue 6, 1990, Pages 653~659
The gene encoding glucoamylase from Schwanniomyces cagtellii CBS 2863 was cloned and expressed in Saccharomyces cerevisiae. Southern blot analysis confirmed that this glucoamylase gene was derived from the genomic DNA of Schwanniomyces ccastellii and that no DNA fragments corresponding to 5.1 or 1.3 kb of Sch. casteltii DNA were detected in S. cereuisiae. The glucoamylase activity from S. cerevisiae transformant was approximately 2,000 times less than that of donor yeast. No expression was found in E. coti. The secreted glucoamylase from S. cerevisiae transformant was indistinguishable from that of Sch. eastellii on the basis of molecular weight and enzyme properties.
A Stable Preservation of Extracellular Nonoccluded Virions from Autographa californica Nuclear Polyhedrosis Virus Infection
Microbiology and Biotechnology Letters, volume 18, issue 6, 1990, Pages 660~661
A stable preservation method of extracellular non-occluded virion of Autographa californica nuclear polyhedrosis virus (AcNPV) was studied. AcNPVL-1 strain infected to Spodoptera frugiperda cell line and then the culture media were centrifuged. After centrifugation the supernatant containing extracellular nonoccluded virions of the AcNPV was harvested and incubated at
. Even after the extracellular nonoccluded virions were incubated at
for about 11 years, the infectivity and multiplication property of the nonoccluded virions in the S. frugiperda cell line were normal. However the titers of the nonoccluded virions in TC-100 medium measured about 11 years ago decreased from
pfu per ml. The AcNPV genome DNA fragment patterns from digestion with Hind11 and EcoRI restriction endonucleases did not change. The AcNPV nonoccluded virions were stable at
in the cultured medium of more than 10 years and the preservation of AcNPV nonoccluded virions at
is easy and useful for handling.