• Journal of Ginseng Research
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• v.28 no.1
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• pp.67-70
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• 2004

Bacillus subtilis B-4228 selected from ginseng field soil for prevention of rusty root was tested for the control of ginseng root rot. In petri-plate dual culture, mycelial growth of Cylindrocarpon destructans was inhibited by B-4228 and hyphal swelling of C. destructans was occurred. In pot experiment with C. destructans-contaminated soil B-4228 dipping of ginseng seedling showed significant preventive effect of root rot (p=0.01), percent healthy root 82% and 20% for treatment and control, root rot rate 6% and 50.4%, respectively.

• Microbiology and Biotechnology Letters
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• v.34 no.4
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• pp.311-317
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• 2006

Using PCR amplification, we cloned a cellulase gene (ce/H) from the Bacillus subtilis AH18 which has plant growth-promoting activity and antagonistic ability against pepper blight caused by Phytophthora capsici. The 1.6 kb PCR fragment contained the full sequence of the cellulase gene and the 1,582 bp gene deduced a 508 amino acid sequence. Similarity search in protein database revealed that the cellulase of B. subtilis AH18 was more than 98% homologous in the amino acid sequence to those of several major Bacillus spp. The ce/H was expressed in E. coli under an IPTG inducible lac promoter on the vector, had apparent molecular weight of about 55 kDa upon CMC-SDS-PAGE analysis. Partially purified cellulase had not only cellulolytic activity toward carboxymethyl-cellulose (CMC) but also insoluble cellulose, such as Avicel and filter paper (Whatman No. 1). In addition, the cellulase could degrade a fungal cell wall of Phytophthora capsici. The optimum pH and temperature of the ce/H coded cellulase were determined to be pH 5.0 and $50^{\circ}C$. The enzyme activity was activated by $AgNO_3$ or $CoCl_2$. However its activity was Inhibited by $HgC1_2$. The enzyme activity was activated by hydroxy urea or sodium azide and inhibited by CDTA or EDTA. The results indicate that the cellulase gene, ce/H is an antifungal mechanism of B. subtilis AH18 against phytophthora blight disease in red-pepper.

• Microbiology and Biotechnology Letters
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• v.38 no.1
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• pp.84-92
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• 2010

Antibacterial compound from Bacillus subtilis MJP1 was purified using C18 Sep-Pak cartridge, ion exchange chromatography, and gel filtration chromatography. The purified antibacterial compound showed antibacterial activity against Listeria monocytogenes, Bacillus subtilis, Staphylococcus aureus subsp. aureus, and Enterococcus faecalis. The purified antibacterial compound was found to be stable at $100^{\circ}C$ for 5 min and in the pH range of 3.0~9.0, but it was unstable at pH 10.0. It was inactivated by proteinase K and pronase E, and heat treatment at $121^{\circ}C$ for 15 min, but it was stable with lipase and $\alpha$-amylase treatment, which indicated its proteineous nature. Ultra performance liquid chromatography and electrospray ionization tandem mass spectrometry analysis were used to identify the purified antibacterial compound and confirmed the existence of two peptides (3356.54 Da, 3400.5244 Da).

• Food Science and Preservation
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• v.15 no.2
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• pp.169-173
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• 2008

Bacillus subtilis subsp. subtilis constitutes 90% of the total viable bacteria present on Capsosiphon fulvescens. We found that hydrogen peroxide (50 ppm) and NaOCl (50 ppm) were more effective than electrolyzed water (EW, 50ppm) against B. subtilis subsp. subtilis that was isolated from this seaweed. Relative to a control, 50 ppm hydrogen peroxide reduced the total viable population by $1.8{\pm}0.4$ log CFU/g, whereas 50 ppm EW increased the total viable population by $1.7{\pm}0.5$ log CFU/g. CFUs were evaluated following 30 days of storage at $4^{\circ}C$ using air- and vacuum-packaging. Samples treated with 50 ppm hydrogen peroxide and NaOCl showed a $1.6{\pm}0.1$-fold decrease in initial hardness ($7.9{\times}10^6dyne/cm^2$), while the samples treated with 50 ppm EW had a $2.1{\pm}0.1$-fold decrease in initial hardness ($7.9{\times}10^6dyne/cm^2$). Again, measurements were performed after storage at $4^{\circ}C$ for 20 days. This study indicates that B. subtilis subsp. subtilis is the most common contaminant in aerobically or anaerobically packaged seaweed and should therefore be the main target for quality control during long-term storage. Hydrogen peroxide and NaOCl are more effective than EW in inhibiting B. subtilis subsp. subtilis and in reducing total bacterial loads in air- and vacuum-packaged seaweed.

• Microbiology and Biotechnology Letters
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• v.37 no.4
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• pp.405-407
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• 2009

A Bacillus subtilis mannanase gene was subcloned into an Escherichia coli- Corynebacterium lactofermentum shuttle vector pHE83, and the resultant plasmid pHE83M was transferred into an endogenous plasmid-free strain of C. lactofermentum. Mannanase produced by the recombinant C. lactofermentum (pHE83M) was secreted extracellulary at the level of 86%, and the remaining activity of mannanase was detected in the cell-free extract. The maximum mannanase productivity of the recombinant strain reached 8.1 unit/mL in the culture filtrate of LB medium. According to the zymogram of mannanase on SDS-PAGE, it was found that the mannanase produced by the recombinant C. lactofermentum could be maintained stably with a migration identical to the mannanase produced by the parental strain, B. subtilis WL-3.

• Journal of the Korean Society of Food Science and Nutrition
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• v.35 no.1
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• pp.115-120
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• 2006

To convert the soybean curd residue (SCR) to functional food ingredient, alkaline fermentation of SCR was performed by Bacillus firmus NA-1 and Bacillus subtilis GT-D for 22 hr at $42^{\circ}C$. The micronized full-fat soy flour (MFS) was fortified to reduce the moisture content as well as to supply protein source. The mucilage and flavor productions in the fermented SCR were enhanced by the fortification of $20\%$ MFS. The peptide production from the SCR fermented with B. subtilis GT-D substantially increased when judged by the detectable amount of tyrosine $(480\;mg\%)$. The production of fibrinolytic enzyme was increased by the fermentation for 22 hr, indicating the relative activity of $62\%$ (B. firmus NA-1) and $47\%$ (B. subtilis GT-D), respectively. The SCR fermented by B. firmus NA-1 and B. subtilis GT-D indicated the consistency of $1.95\;Pa{\cdot}s^n\;and\;0.21\;Pa{\cdot}s^n$, respectively. After freeze-drying, the protease activity (615 unit/g) and a-amylase activity (180 unit/g) were obtained from SCR fermented by Bacillus firmus NA-1 and Bacillus subtilis GT-D, respectively.

• Korean Journal of Microbiology
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• v.43 no.4
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• pp.331-336
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• 2007

A bacterium producing the alkaline pretense was isolated from Chungkookjoug, and was identified as Bacillus subtilis JK-1 based on morphological, physiological and biochemical characteristics, as well as phylogenetic analysis using 16S rRNA gene sequence. The optimum pH and temperature of the pretense activity were pH 9.0 and $55^{\circ}C$, respectively. This enzyme was stable at the temperatures $40{\sim}80^{\circ}C$. The maximum alkaline pretense production was obtained when 1.0% (w/v) xylose, 1.0% (w/v) yeast extract and 0.3% (w/v) $CuSO_4$ were used as carbon source, nitrogen source and mineral source. Under the optimal condition, growth of the isolate was reached at stationary phase after 12 hr followed by incubation, the alkaline pretense production reached a maximum level with $16{\sim}20$ hr cultivation.

• Microbiology and Biotechnology Letters
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• v.45 no.1
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• pp.12-18
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• 2017

Microbial strains exhibiting proteolytic activity were isolated from kimchi, one of traditional fermented foods in Korea. Eight strains formed clear zones around their colonies when grown on TSA plates supplemented with skim milk. MBE/L865 exhibited 2.6-fold higher protease activity than that of control strain (Bacillus subtilis KCTC13112). MBE/L865 was identified as B. subtilis and deposited in the Korean Collection for Type Cultures under the accession number of KCCM43059. The optimum growth conditions for B. subtilis KCCM43059 were determined to be $37^{\circ}C$ and pH 8. The strain showed maximum protease activity ($429.37{\pm}18.65U/mg$ protein) at $60^{\circ}C$ and pH 6. Further, B. subtilis KCCM43059 had a higher salt (NaCl) tolerance than that of the control strain.

• Journal of Life Science
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• v.12 no.1
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• pp.77-86
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• 2002

Chitin, a $\beta$-1,4 polymer of N-acetyl-D-glucosamine, is one of the most abundant organic compounds in nature. Chitinase (EC 3.2.1.14) is an enzyme that degrades chitin to chito-oligosaccharides, diacetyl rhitobiose and N-acetyl-D-glucosamine. An extracellular chitinase-producing bacterial strain was isolated from soil and named to as Bacillus subtilis JK-56. Optimum culture condition of B. subtilis JK-56 for the production of chitinase was 1% chitin, 0.5% polypepton, 0.1% KCl, 0.05% MnS $O_4$.4$H_2O$, 37$^{\circ}C$, initial pH 7.0 and 40 hour culture time. When B. subtilis JK-56 was grown in the optimum medium, one major active band and two minor active bands were detected by native-PAGE and active staining of the gel. Among them, the major band was purified from the culture supernatant by 70% ammonium sulfate precipitation and native-PAGE with BIO-RAD Model 491 Prep-Cell and named as Chi-56A. Its molecular weight was estimated to be 53kDa monomer and the isoelectric point (pI) was pH 4.3. The pH and temperature for the optimum activity of Chi-56A were pH 6.0 and $65^{\circ}C$, respectively. Chi-56A was stable up to $65^{\circ}C$ and in alkaline region. Its $K_{m}$ value for colloidal chitin was 17.33g/L. HPLC analysis of the reaction products confirmed that Chi-56A was an exo type chitinase.e.

• Microbiology and Biotechnology Letters
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• v.30 no.3
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• pp.210-215
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• 2002

A bacterium degrading soy protein was isolated from Korean traditional fermented foods. The isolated strain was identified as Bacillus subtilis, and named as B. subtilis EB464. The optimum pH and temperature of the protease produced by 5. subtilis EB464 were pH 9.0 and $50^{\circ}C$, respectively. The protease was stable in the range of pH 6~10 and below $40^{\circ}C$. The content of water-soluble protein and free amino acid of the medium were increased from 4.2% to 20.6% and ken 1.9% to 22.0%, respectively, by solid-state fermentation of soybean meal with B. subtilis EB464 for 72 h.