• 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.

• Microbiology and Biotechnology Letters
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• v.23 no.1
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• pp.53-59
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• 1995

A protease isolated and purified 51 fold from the culture filtrate of a soil bacterium, Bacillus sp. KUN-17, which was appeared to be a monomeric protein with molecular weight of 38, 000 daltons, was suggested to be involved in the serine (-alkaline) protease (E.C 3.4.21.14) since its activity was selectively inhibited by phenylmethylsulfonyl fluoride (PMSF) and required 40$\circ$C and pH 10.5 for optimal condition. The half-life of the enzyme activity was 1 hr at 55$\circ$C, and the activity was maintained even under high concentrations of SDS or urea. The enzyme was indicated to perform random proteolysis from the fact that most of the chromogenic substrates employed were hydrolyzed by the enzyme. The affinity of the enzyme for natural proteins was approximately 10-times higher than ester compounds, and both substrates showed mutual inhibitory effect competitively for the enzyme activity.

• Journal of Life Science
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• v.14 no.1
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• pp.193-197
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• 2004

A continuous enrichment culture procedure was used to isolate bacteria from various soil sources capable of suppressing large patch disease of turfgrass. Six isolates consistently suppressed large patch in turfgrass, and ranged in the spectrum of extracellular enzymes that they expressed. The best disease- suppressing isolate, TBM912, expressed protease, CMCase, and pectinase activity and inhibited the growth of Rhizectonin solani and Betrytis cinerea in vitro. Here we show that this strain also produces an antibiotic that was identified by TLC, SDS-PACE and HPLC analysis as lipopeptide.

• Journal of the Korean Society of Food Science and Nutrition
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• v.29 no.1
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• pp.49-56
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• 2000

The 2-O-$\alpha$-D-glucopyranosyl L-ascorbic acid (AA-2G) which was enzymatically glucosylated with the cyclodextrin glucanotransferase (CGTase) [EC 2.4.1.19] from Bacillus sp. JK-43 has been reported previously. The presnet experiments examined the optimal conditons for the productio of AA-2G from AA and soluble starch, and characterized the properties of the CGTase from Bacillus sp. JK-43. The reaction mixture for the maximal production of AA-2G was followings; 12% total substrate concentration, 1,400 usits/mL of CGTase and a mixing ratio of 2 : 3(g or AA : g of soluble starch). Under this condition, 1.76mM of AA-2G, which corresponded to 2.53% yield based on AA, was produced after incubation for 24hrs at 45$^{\circ}C$ (pH 5.5). The optimum pH and temperature for the CGTase activity were 6.0 and 45$^{\circ}C$, respectively. The enzyme was stable at pH 5.5 to 9.5, and at temperature up to 5$0^{\circ}C$. The thermostability of the enzyme could be enhanced up to 6$0^{\circ}C$ by the addition of 30mM CaCl2.

• Applied Biological Chemistry
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• v.40 no.5
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• pp.369-374
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• 1997

An endochitosanase-producing bacterium was isolated from soil and identified as a strain of Bacillus sp. The isolate was gram positive, rod shape $(0.4-0.6{\times}1.6-2.2{\mu}m)$, endospore-forming, catalase positive, and mobility positive, and grown at pH 4.5-11.0 and upto $42^{\circ}C$ in the medium containing 2% NaCl. RAPD analysis of the DNA purified from the strain was also performed, and the chitosanase-producing strain was named as Bacillus sp. P16. The culture supernatant of the strain showed strong liquefaction activity and rapidly decreased viscosity of chitosan solution. By TLC and HPLC, chitooligosaccharides of DP 2-7 were separated and identified from the enzyme hydrolyzates of chitosan. The chitosanase from Bacillus sp. P16 was thus regarded as an endo-splitting type.

• Microbiology and Biotechnology Letters
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• v.42 no.2
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• pp.99-105
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• 2014

A Bacillus strain capable of hydrolyzing locust bean gum was isolated as a producer of extracellular mannanase by way of an enrichment culture in an acidic medium from homemade soybean pastes. The isolate YB-1401 showed a biochemical identity of 61.1% with Brevibacillus laterosporus, while the nucleotide sequence of its 16S rDNA had the highest similarity with that of Bacillus amyloliquefaciens. The mannanase productivity of the Bacillus sp. YB-1401 was drastically increased by mannans. Particularly, maximum mannanase productivity was reached at approximately 265 U/ml in LB medium supplemented with konjac glucomannan (4.0%). The mannanase was the most active at $55^{\circ}C$ and pH 5.5. Mannanase activity was completely maintained after pre-incubation at pH 3.5 to 11.0 for 1 h. The predominant products resulting from the mannanase hydrolysis were mannobiose and mannotriose for LBG, guar gum or mannooligosaccharides. A small amount of mannose was also detected in the hydrolyzates.

• Journal of Microbiology and Biotechnology
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• v.9 no.2
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• pp.223-226
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• 1999

A bacterial strain producing high level of an extracellular phytase was isolated from cooked rice and identified as a strain of Bacillus sp. and designated as Bacillus sp. KHU-10. Optimum culture conditions were investigated for the maximum productivity of phytase by Bacillus sp. KHU-10. 1.0% Maltose and 1.0% peptone with 0.5% beef extract were the best carbon source and nitrogen source, respectively. The addition of $CaCl_2$, stimulated the enzyme productivity with concentration between 0.01% and 0.2%, in the medium. Although sodium phosphate increased the cell mass, the enzyme activity decreased. Calcium phytate and wheat bran containing phytate did not enhance the enzyme production. Under the optimum medium, the production of the phytase reached the highest level of 0.2 unit/ml after 4 days of incubation.

• Korean Journal of Environmental Biology
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• v.27 no.4
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• pp.384-390
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• 2009

An antifungal antibiotic-producing bacterium was isolated from soil and identified as Bacillus sp. CJ-1. The culture supernatant was found to have a strong and stable antifungal activity against Colletotrichum gloeosporioides. Culture conditions for the maximum antifungal activity were examined. Glucose and yeast extract were selected as the best carbon and nitrogen sources. The optimum C/N ratio was 3. The optimum temperature and initial pH were determined as $35^{\circ}C$ and 6.0, respectively. Under these conditions, the production for the antibiotic was maximized at 72 hr at $35^{\circ}C$ after cultivation. Microscopic observation showed that the culture supernatant of Bacillus sp. CJ-1 had a strong inhibitory activity on the mycelial growth of the test strain at above $12.5\;{\mu}L\;mL^{-1}$ of concentration.

• 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 Veterinary Service
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• v.40 no.1
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• pp.71-74
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• 2017

The first case of liver infection caused by Sphingomonas sp. and Bacillus sp. in a wild rodent is reported. A captured wild rodent, Apodemus agrarius (A. agrarius), presented with multiple liver abscess-like nodules (diameter 0.7~2.4 mm) in which Gram-positive and Gram-negative bacilli were detected simultaneously. These were grown in aerobic and anaerobic cultures, respectively, and were identified as Sphingomonas sp. and Bacillus sp., respectively, according to 16S rRNA sequencing.