• Biotechnology and Bioprocess Engineering:BBE
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• v.10 no.3
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• pp.186-191
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• 2005

In this study, a microorganism-produced protease was used to improve the quality of fabrics. First, the protease-producing bacteria were isolated from soils, and one of them was selected and identified as Bacillus sp. SJ-121. The optimal medium composition for its growth and protease production was determined to be as follows: glucose 1g/L, soybean meal 0.5g/L, soy peptone 0.5, $K_2HPO_4\;0.2,\;MgSO_4\cdot7H_2O\; 0.002,\;NaCl\;0.002,\;and\;Na_2CO_3g/L$. Also, the optimal temperature for the production of the protease by Bacillus sp. SJ-121 was about $40^{\circ}C$ at pH 7. The wool and silk were treated with the protease from Bacillus sp. SJ-121. Following the protease treatment, changes in the surface of a single yarn of the fabrics were observed by both an optical microscope and a scanning electron microscope (SEM). Changes in the K/S value of the wool and silk were measured by spectrophotometric analysis, in order to determine the amount of dye uptake in the fabrics. We also performed a tensile strength examination in order to determine the degree and nature of mechanical changes in single yarns of the wool and silk fabrics. By increasing the protease treatment time to 48 h, the dyeing characteristics of the fabrics were enhanced, and the surfaces of the single yarns of the fabrics became smoother, due to the removal of soil and scale in them. However, no mechanical changes were detected in the fabrics. Therefore, we suggest that proper treatment of the protease produced by Bacillus sp. can improve the quality of silk and wool.

• Applied Biological Chemistry
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• v.46 no.3
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• pp.165-170
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• 2003

The antioxidative activity of antioxidative substances produced from several bacterial strains isolated from fermented foods were tested by $DPPH\;({\alpha},{\alpha}'-diphenyl-{\beta}-picrylhydrazyl)$ free radical scavenging activity. One of the strains showing the highest antioxidative activity was identified as Bacillus sp. based on the morphological, biochemical, physiological characteristics, and 16S rRNA sequence, and named FF-7. The most optimal medium condition for the production of antioxidative substance from Bacillus sp. FF-7 was 2% galactose as carbon source and l% tryptone as nitrogen source. The antioxidative substance produced from FF-7 in these cultural medium was also tested by in vitro experimental models, the peruxidation of linoleic acid and the peroxidation of rat tissues microsomes by using thiobarbituric acid (TBA) for assay of free malondialdehyde production. The antioxidative activity against lipid peroxidation of rat tissues microsomes was shown in the following order; brain 97.50% > heart 79.95% > kidney 77.84% > spleen 77.47% > testis 69.96% > liver 62.45%. The antioxidative substance produced from FF-7 on linoleic acid peroxidation by IBA method was effectively inhibited during four days, and 0.05% BHT (butylated hydroxytoluene) used comparative control was also effectively inhibited. Results showed that the highest antioxidative activity by DPPH method of antioxidative substance produced from Bacillus sp. FF-7 was obtained by supplementing 2% galactose as carton source and l% tryptone as nitrogen source in cultured medium, this substance effectively inhibited the formation of TBARS in brain microsome in vit개 system and in linoleic acid peroxidation.

• Food Science and Preservation
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• v.8 no.1
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• pp.92-101
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• 2001

In order to develop the Production and application of cholesterol oxidase, a cholesterol degradation bacteria which produces a remarkable amount of extracellular cholesterol oxidase has been isolated from Korea traditional salt fermented flat fish. The isolated strain was identified as a strain of Bacil1us sp. based on its morphological, physiological characteristics and cellular fatty acid compositions. Experiments were carried out to optimize the condition of cholesterol oxidase production using Bacillus sp. SFF34. Bacillus sp. SFF34 was shown to give the maximum yield of cholesterol oxidase in the medium containing 2.0% glucose, 0.5% yeast extract, 0.02% MgSO$_4$$.$7H$_2$O, 0.025% K$_2$HPO$_4$, 0.15% NH$_4$NO$_3$ and 0.2% cholesterol. The optimum culture conditions, temperature, initial pH and agitation speed were 30$^{\circ}C$, 7.0 and 150rpm respectively. The enzyme production reached a maximum level at 24 hrs of cultivation(2.42 U/ml).

• Journal of Microbiology and Biotechnology
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• v.12 no.1
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• pp.153-156
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• 2002

The characterization of a partially purified, cellulase-free, thermostable alkaline xylanase from thermoalkalophilic Bacillus sp. JB-99 was investigated. The xylanase production was the highest when birchwood xylan was added to a medium containing finely powdered rice bran, showing 4,826 IU$ml^-1$ of activity for 15 h of incubation. The partially purified xylanase exhibited an optimum temperature and pH at $70^C{\circ}$ and 10, respectively. The enzyme was stable at pH 5-11 at $50^C{\circ}$. The xylanase activity was strongly inhibited by $Hg^2+$, while dithiothreitol, cysteine, and ${\beta}$-mercaptoethanol enhanced the activity.

• Journal of Microbiology and Biotechnology
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• v.30 no.5
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• pp.777-784
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• 2020

Self-sufficient P450s, due to their fused nature, are the most effective tools for electron transfer to activate C-H bonds. They catalyze the oxygenation of fatty acids at different omega positions. Here, two new, self-sufficient cytochrome P450s, named 'CYP102A15 and CYP102A170,' from polar Bacillus sp. PAMC 25034 and Paenibacillus sp. PAMC 22724,respectively, were cloned and expressed in E. coli. The genes are homologues of CYP102A1 from Bacillus megaterium. They catalyzed the hydroxylation of both saturated and unsaturated fatty acids ranging in length from C₁₂-C₂₀, with a moderately diverse profile compared to other members of the CYP102A subfamily. CYP102A15 exhibited the highest activity toward linoleic acid with K_m 15.3 μM, and CYP102A170 showed higher activity toward myristic acid with Km 17.4 μM. CYP10A170 also hydroxylated the Eicosapentaenoic acid at ω-1 position only. Various kinetic parameters of both monooxygenases were also determined.

• Korean Journal of Environmental Biology
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• v.28 no.2
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• pp.95-100
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• 2010

Burkholderia cepacia PBSA-7, Bacillus licheniformis PBSA-8 and Burkholderia sp. PBSA-9 previously collected from Korea soil (Joo and Kim, 2009) were analyzed for the presence of genes encoding proteins operative in the degradation of poly(butylene succinate-co-butylene adipate; PBSA). Polymerase chain reaction analyses revealed a 1.5 kb fragment of the lipase gene (lip A) in B. cepacia PBSA-7 and Burkholderia sp. PBSA-9, while B. licheniformis PBSA-8 harbored the same gene fragment at 600 bp. The three strains possessed "Gly-X1-Ser-X2-Gly" and "Ala-X1-Ser-X2-Gly" lipase sequence regions. Burkholderia sp. PBSA-7 lip A displayed 36~40% homology with the family 1-1 lipases and 82~92% homology with the family 1-5. Burkholderia sp. PBSA-8 lip A was 64~65% homologous with the subfamily 1-4 lipases, but displayed no homology with the subfamily 1-5 lipases. Burkholderia sp. PBSA-9 lip A displayed 35~37% homology with the family I1 lipases and 83~94% homology with the family I2 lipases, similar to Burkholderia sp. PBSA-7.

• Journal of Applied Biological Chemistry
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• v.56 no.4
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• pp.241-244
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• 2013

Nitrate is one of the major nutrients in plants, and nitrate fertilizer often overused for the high yields of crops. Nitrate deposit in soil became one of the major reasons causing salt stress. Specially, salt stress is a serious problem in the soils of plastic film or glass houses. In this study, six microorganisms have been isolated from the wet soils near the disposals of livestock farms and their nitrate uptake activities were investigated. These bacteria were able to remove nitrate as high as 1,000-3,000 ppm (10-50 mM). The strain PCE3 showed the highest nitrate uptake activity and it removed more than 3,700 ppm. In order to identify these bacteria, genes of 16S rRNA were sequenced and analyzed. Phylogenetic trees were constructed with the neighbor-joining methods. Among these bacteria, strain PCE3 was identified as Bacillus species. When the growth and nitrate uptake activities were measured, both were maximal at $37^{\circ}C$ and optimal pH was pH 7-9. Bacillus sp. PCE3 removed nitrate up to 40-60 mM (2,500-3,700 ppm) depending on the nitrate concentration in media. Therefore, Bacillus sp. PCE3 can be a good candidate for the microbial remediation of nitrate-deposited soils in glass and plastic film houses.

• Microbiology and Biotechnology Letters
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• v.33 no.1
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• pp.24-28
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• 2005

A bacterial strain D­1 found to have potent fibrinolytic activity was isolated from Korean traditional Doenjang. It was identified as Bacillus sp. based on its 16S rRNA sequence analysis, morphological and physiological characteristics.

• Korean Journal of Food Science and Technology
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• v.23 no.1
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• pp.93-97
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• 1991

The enzymatic properties of purified CGTase from alkalophilic Bacillus sp. YC-335 have been examined. Apparent Vmax values of the enzyme in transferring glycosyl residues ${\alpha}-,\;{\beta}-and\;{\gamma}-cyclodextrin(CD)$ to sucrose were $16.13,\;21.8\;and\;9.8{\mu}moles/min/mg\;protein$, respectively and Km values of the corresponding CD were 1.68, 0.33 and 0.37 mM, respectively. A number of saccharides, specially starch hydrolyzates such as glucose and maltose, could activate the dextrinizing activity of the enzym. However, the dextrinizing activity was inhibited by ${\beta}-CD$. It was found from Lineweaver-Burk plot that the inhibition of CGTase by ${\beta}-CD$ was noncompetitive. High performance liquid chromatographic analysis showed that the enzyme has three kinds of activity ; transglycosylation and disproportionation as well as cyclization.

• Microbiology and Biotechnology Letters
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• v.31 no.3
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• pp.216-223
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• 2003

A 1.3-kb of chitosanase gene (choA) encoding 45-kDa polypeptide was cloned, expressed, and characterized from a newly isolated Bacillus cereus H-1. The chitosanase protein (ChoA) of B. cereus H-l was purified to homogeneity by ammonium sulfate precipitation and CM-sephadex column chromatography. Optimum pH was around 7, and stable pH range in the incubation at 50 C was 4-11. Optimum temperature was around 50 C, and enzyme activity was relatively stable below 45 C. ChoA showed the activities toward carboxymethyl cellulose (CMC) in addition to soluble or glycol chitosan. Based on MALDI-TOF MS analysis of purified ChoA, the entire amino acid sequence of ChoA was interpreted by database searching of previously known Bacillus chitosanases. A 1.6 kb of PCR product of corresponding chitosanase gene was obtained and its DNA sequence was determined. The deduced amino acid of choA revealed that ChoA have a 98% homology with those of Bacillus sp. No.7-M strain and Bacillus sp. KCTC0377BP. The recombinant ChoA protein was expressed in E. coli DH5$\alpha$. Deduced amino acid comparison of choA with other chitosanases suggested that it belongs to family 8 microbial endo-chitosanase with chitosanase-cellulase activity.