• Microbiology and Biotechnology Letters
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• v.18 no.4
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• pp.429-432
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• 1990

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.

• Microbiology and Biotechnology Letters
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• v.17 no.2
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• pp.160-164
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• 1989

A 5.7Kb EcoRI fragment containing alkaline amylase gene of Bacillus sp. AL-8 obtained in the previons experiment (10) was transformed in B. subtilis via plasmid pUB110. The enzymatic proper-ties of the amylase produced by the transformants were Identical to those of the donor strain. Thus, the alkaline amylase activity from the transformant was maximum at pH 10 and 5$0^{\circ}C$. And the enzyme was very stable over the ranges of alkaline pH. In order to determine the location of the alkaline amylase gene within the 5.7Kb DNA fragment, the fragment was subcloned in E. coli. It was found that the alkaline amylase gene was located k EcoRI fragment of 3.7Kb.

• Food Science and Preservation
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• v.5 no.3
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• pp.292-298
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• 1998

The isolates from putrefying soybean curd were identified as Acinetobacter calcoaceticus, Bacillus cereus, Bacillus sp., Cardiobacterium sp., Escherichia coli, Klebsiella pneumoniae, Pantoea sp., Salmonella typhimurium, Staphylococcus aureus, Xenorhabdus luminescens, Yersinia sp.. The existence percentages of the bacteria from putrefying soybean curd at room temperature storage were Bacillus cereus J55 23.57%, Xenorhabdus luminescens J48 22.73%, Acinetobacter calcoaceticus J61 22.26%, Klebsiella pneumoniae J62 21.25%, Salmonella typhimurium J51 2.87%, Pantoea sp. J57 2.65%, Bacillus sp. J58 1.43%, Cardiobacterium sp. J54 1.26%, Escherichia coli J53 1.20%, Staphvlococcus aureus J6O 0.93%, Yersinia sp. J50 0.05%, respectively. Four out of eleven bacteria as B. cereu J55, X. luminescens J48, Ac. calcoaceticus J61, Kl. pneumoniae J62 putrefied soybean curd and those bacteria produce amylase or proteinase as a extracellular enzyme. But S. typhimurium J51, Pantoea sp. J57, Bacillus sp. J58, Cardiobacterium sp. J54, E. coli 153, St. aureus J60, Yersinia sp. J50 were not putrefied soybean curd. The isolates detected to resistant on various antimicrobial agents. The majority were resistant to aminoside antiboitics as amicacin, gentamicin, tobramycin and were susceptible to ${\beta}$-lactamine antibiotics as penicillin G, oxacillin, cephalothin cefazolin, cefamandole.

• Microbiology and Biotechnology Letters
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• v.30 no.2
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• pp.123-128
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• 2002

A bacterium producing the extracellular xylanase was isolated from soil and has been identified as a Bacillus sp. strain. The isolate, named Bacillus sp. AMX-4, was shown to be similar to B. subtilis strain on the basis of its chemical compositions. The xylanase of culture supernatant was most active at 50℃ and pH 6.0. The additional carbon sources including monosaccharides, disaccharides, wheat bran, and rice straw increased the enzyme productivity. Especially, the maximum xylanase productivity was reached 29.2 units/ml in LB medium supplemented with 1.5％ (w/v) xylose, which was 16-folds more than that in LB medium. As the results of investigating the effects of xylose on cell growth and xylanase productivity of Bacillus sp. AMX-4, increase of xylanase production was owing to the induction of xylanase biosynthesis. It was also found that the enzyme production was in association with the growth of Bacillus sp. AMX-4.

• Food Science and Biotechnology
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• v.15 no.5
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• pp.704-709
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• 2006

The mucilage production and tyrosine content in soy milk cake (SMC) fermented by Bacillus firmus NA-1, Bacillus subtilis GT-D, and B. subtilis KU-A was improved by fortification with 10% defatted soybean flour. The fibrinolytic activity and consistency of the SMC were drastically increased by solid-state fermentation for 1 day. However, the consistency of the fermented SMC gradually decreased during fermentation for 3 days. Furthermore, the tyrosine content of the freeze-dried powder of SMC fermented by three Bacillus sp. was 9 times higher than that of unfermented SMC. The soybean proteins, including the 7S and 11S subunits, were partially digested during alkaline fermentation, producing lower molecular-weight peptides. The fibrinolytic enzyme produced in SMC fermented by B. firmus NA-l and B. subtilis KU-A exhibited higher thermal stability than that of B. subtilis GT-D fermentation. The powder obtained from B. subtilis GT-D fermentation had an ${\alpha}$-amylase activity and lower consistency compared to those of B. firmus NA-1 and B. subtilis KU-A. In addition, this powder contained 6.3% moisture content, 27% crude protein content and 9 units of fibrinolytic activity and proteolytic activity.

• Journal of Microbiology and Biotechnology
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• v.1 no.2
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• pp.102-110
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• 1991

Alkalophilic Bacillus sp. YJ-451, which was isolated from soil at several area in Korea, produced a novel type of bacteriolytic enzyme (cell wall peptidoglycan hydrolase) extracellulary. The cell wall hydrolytic activity was identified as a clear zone on sodium dodecyl sulfate polyacrylamide gel electrophoresis containing 0.2% (w/v) cell wall of Bacillus sp. as substrate. This enzyme was successively purified 66 fold with 3.2% yield in culture broth by ammonium sulfate precipitation, CM-cellulose column chromatography, and gel filtration, followed by hydroxylapatite column chromatography. The molecular weight of the purified enzyme was estimated to be 27,000 by sodium dodecyl sulfate polyacrylamide gel electrophoresis and gel filtration column chromatography. The optimum pH and temperature for the activity of the enzyme were pH 10.0 and $50^{\circ}C$, respectively. The enzyme was stable between pH 5.0 and 10.0 and up to $40^{\circ}C$. Among the microorganisms used in this experiment the enzyme was active against most of gram negative strains and the genus Bacillus such as B. megaterium, B. licheniformis, B. circulans, B. pumilus, B. macerans, B. polymyxa. The release of dinitrophenylglutamic acid but not reducing group from cell wall peptidoglycan digested by the enzyme suggested that the enzyme is a kind of peptidase which hydrolyzes the peptide bond at the amino group of D-glutamic acid in the peptidoglycan.

• YAKHAK HOEJI
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• v.42 no.6
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• pp.552-557
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• 1998

Acyl CoA synthetase inhibitor, was purified from the culture broth of a Bacillus sp. B-6, which had been isolated from soil, by chloroform extract, silica gel column chro matography and preparative TLC. The purified acyl CoA synthetase inhibitor showed higher Antifungal activity against C. al-bicans (MIC: 8${\mu}$g/ml). Though the analysis of UV spectrum, melting point, IR spectrum, Mass-spectrum, $^1H$-NMR and $^{13}C$-NMR spectrum, the inhibitor could be identified as phenazine-l-carboxylic acid.

• Journal of Microbiology and Biotechnology
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• v.15 no.3
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• pp.537-543
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• 2005

Subtilisin (EC 3.4.21.14) is the major extracellular alkaline serine protease of Bacillus species. Previously, we found that subtilisins did not migrate in the electrophoretic field in the Laemmili buffer system due to their high pI values (over 8.8); however, it formed a 'binding mode' at the top of the separating gel [5]. Utilizing this characteristic, four subtilisins from Bacillus sp. strains (e.g., B. subtilis 168, B. subtilis KCTC 1021, B. amyloliquefaciens KCTC 3002, and Bacillus sp. DJ-1 and DJ-4) were easily and quickly identified by an over-running electrophoretic technique with a miniscale culture supernatant (less than 20 ml) without any column chromatographic steps. Two subtilisins (DJ-l and a recombinant version) from Bacillus sp. DJ-l were characterized, and the enzymatic properties were determined by SDS-fibrin zymography and densitometric analysis. Based on this observation, the recombinant pro-subtilisin DJ-l showed the same 'binding mode,' similar to native subtilisin DJ-l. On the other hand, mature subtilisin DJ -1 without pro-peptide showed no enzymatic activity.

• Korean Journal of Microbiology
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• v.45 no.2
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• pp.208-214
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• 2009

To avoid ambiguity in counting the number of colony, about 1,500 of colonies grown on B. cereus selective agar plates were grouped into 12 types by morphological difference and then identified by biochemical and 16S rDNA nucleotide sequence. Among them, seven colony types with 11 to 15 mm diameters of halo were identified as B. cereus or B. cereus subsp. cytotoxis. Five mm sized colonies with no halo, which have not been considered as B. cereus according to the manufacturer's manual, were identified as B. cereus. A colony type with double halos of only 6 mm in diameter was also B. cereus. Other three types were proven to be Enterococcus sp., Brevibacillus sp., and B. subtilis, respectively. PCR results showed that only 9 types that are identified as B. cereus strains harbor at least one of B. cereus toxin genes.

• Microbiology and Biotechnology Letters
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• v.39 no.1
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• pp.49-55
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• 2011

Thirty Streptomyces sp. and 200 Bacillus sp. isolated from Korean soils and traditional foods were screened for their abilities to inhibit ${\alpha}$-glucosidase and produce 1-deoxynojirimycin (DNJ). This screening identified a Bacillus sp. bacterium that strongly inhibited ${\alpha}$-glucosidase and produced high levels of DNJ from Chungkookjang, a Korean traditional food. The bacterium was characterized in terms of its biochemical and molecular biological properties such as sugar utilization, cellular quinone composition, cell wall fatty acid composition, and 16S rDNA sequence. In addition, scanning electron microscopy was used to visualize the morphology of the bacterium. These analyses identified the bacterium as B. subtilis, a bacterium with Generally Recognized as Safe (GRAS) status. The selected strain was named B. subtilis MORI.