• Microbiology and Biotechnology Letters
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• v.9 no.2
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• pp.91-97
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• 1981

A thermophilic soil isolate Bacillus sp. Y-127 was selected for the production of thermostable amylase. The strain was used for the enzyme production and the thermostable amylase was characterized. The optimum cultural conditions for the enzyme production were 6$0^{\circ}C$ at pH 7.0 for 32 hours using a mineral medium containing 2% soluble starch and 0.2% yeast extract. The extra-cellular enzyme was purified about 123-folds with about 6% recovery. The purified enzyme was stable at pH between 4.0 and 7.0, and temperature up to 6$0^{\circ}C$.

• Journal of Environmental Science International
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• v.30 no.2
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• pp.161-172
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• 2021

This study was initiated to isolate the microorganisms removing phosphorus (P) from domestic sewage and to investigate the effects of environmental factors on the growth and P removal of the isolated bacteria. Microorganisms isolated from the sewage were identified as Chryseobacterium sp., Stenotrophomonas maltophilia, and Bacillus licheniformis. Among them, Bacillus licheniformis was selected as the P removal microorganism. The environmental factors considered in this study included initial phosphorus concentration, temperature, pH, and carbon source. At initial P concentrations of 10, 20, and 30 mg/L, the P removal efficiencies were 100.0%, 84.0%, and 16.5%, respectively. At 20℃, 30℃, and 40℃, the P removal efficiencies were 0%, 75.8%, and 60.6%, respectively. The removal efficiencies of phosphorus according to pH were 1.6%, 91.7%, and 51.1% at pH 5, pH 7, and pH 9, respectively. Using glucose, acetate, and glucose + acetate as carbon sources yielded P removal efficiencies of 80.9%, 33.6%, and 54.1%, respectively. Therefore, the results from the study demonstrated that the P removal efficiencies of Bacillus licheniformis were the highest when the initial P concentration, temperature, pH, and carbon source were 10 mg/L, 30℃, 7, and glucose, respectively.

• Environmental Engineering Research
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• v.15 no.3
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• pp.141-147
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• 2010

The objective of this study was to assess the biofouling characteristics of the Bacillus biofilm formed on reverse osmosis (RO) membranes. For the study, a sporogenic Bacillus sp. was isolated from the seawater intake to a RO process, with two distinct sets of experiments performed to grow the Bacillus biofilm on the RO membrane using a lab-scale crossflow membrane test unit. Two operational feds were used, 9 L sterile-filtered seawater and 109 Bacillus cells, with flow rates of 1 L/min, and a constant 800 psi-pressure and pH 7.6. From the results, the membrane with more fouling, in which the observed permeate flux decreased to 33% of its initial value, showed about 10 and 100 times greater extracellular polymeric substances and spoOA genes expressions, respectively, than the those of the less fouled membrane (flux declined to 20% of its initial value). Interestingly; however, the number of culturable Bacillus sp. in the more fouled membrane was about 10 times less than that of the less fouled membrane. This indicated that while the number of Bacillus had less relevance with respect to the extent of biofouling, the activation of the genes of interest, which is initiative of biofilm development, had a more positive effect on biofouling than the mass of an individual Bacillus bacterium.

• The Korean Journal of Food And Nutrition
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• v.9 no.4
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• pp.385-391
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• 1996

To produce low salt fermented anchovy by an accelerated method with Asp. oryzae and Bacillus sp. koji and change of physicochemical properties in the fermentation during 60 days were examined. The contents of moisture, crude protein, ash and salinity of salted anchovy changed little during the fermentation with 62.5~63.8%, 12.0~14.1%, 12.8~13.8%, and 12.8~13.8%, respectively. but crude lipid decreased from 15.5~15.8% initially to 13.1~13.9% finally. The p during the fermentation decreased slowly until day 50 and increased afterwards. Acidity increased remarkably on day 10 and changed little afterwards. This increase in acidity was particularly observed in the use of Asp. oryzae koji. Amino nitrogen contents sharply increased until day 20 wit 686.0~756.0mg% and then increased slowly. Ammonia nitrogen contents in the use of koji increased until day 40 or 50 and decreased after that ; while those without koji steadily increased until day 60. The TBA values for all the samples reached the highest point on day from 20 to 30 and decreased afterwards. The TBA values and ammonia nitrogen contents were higher in Bacillus sp. koji than in Asp. oryzae koji. The alcohol contents of anchovy paste a little decreased during 10 days, increased slowly after that until day 50, and then decreased. The content of alcohol was higher in the use of koji than in the non koji.

• Applied Biological Chemistry
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• v.46 no.3
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• pp.176-182
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• 2003

An alkaline fibrinolytic protease-producing bacteria was isolated front Korean traditional soy sauce and identified as Bacillus subtilis K7 from the results of analyses of its morphological and physiological properties, $API^{\circledR}$, and Biolog system. The enzyme was purified by 75% ammonium sulfate fractionation, QAE-Sephadex anion and SP-Sephadex cation exchange column chromatography and Sephadex G-100 gel filtration. The specific activity of the purified enByme was 233.9 unit/mg protein and the yield of enzyme was 3.8%. The homogeneity of the purified enzyme was confirmed by polyacrylamide gel electrophoresis. Molecular mass of the enzyme was estimated about 21,500 Da by SDS-polyacrylamide get electrophoresis and gel chromatography. The optimum temperature and pH for the enzyme activity were $40^{\circ}C$ and 9.0, respectively. The enzyme was stable in a pH range of 5.0 to 12.0, and 60% of its activity was lost on heat treatment at $50^{\circ}C$ for 20 min. The activity of the purified enzyme was inhibited by the presence of $Fe^{2+},\;Ag^{2+},\;Cu6{2+}$, iodoacetate, ethylene diamine tetraacetic acid (EDTA), and trans-1,2-diaminocycloheane-N,N,N',N'-tetraacetic acid (CDTA). The results indicates that the enzyme requires a metal ion for its enzymatic activity.

• Journal of Microbiology
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• v.41 no.3
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• pp.196-201
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• 2003

The object of this study was to characterize Bacillus strains GB-017 and GB-0356, which produce antifungal substances, especially for plant pathogens. In addition, this study was undertaken to characterize the culture conditions required for the production of antifungal substances and to document some of the properties of the antifungal substance produced by these soil-isolated strains. Strains GB-0365 and GB-017 were found to be bacillus-shaped, gram-positive and motile, and to inhibit Botrytis cineria, Fusarium sp., Pythium sp., and Rhizoctonia solani. Antagonistic activity was maintained up to pH 9.0, and the antifungal activity was stable to heat at 80$^{\circ}C$ for 1 h. Antifungal substances were separated and purified using ion exchange and adsorption columns including WK-I0(H$\^$＋) (pH 7.0), HP20 column (pH 3.0) and IPA (pH 3.0). and IPA. Its UV absorption spectrum showed major peaks at 231 and 259 nm, corresponding to polyene and lactone. A fast atom bombardment mass spectrum (FAB MS) showed a highest peak at 441 m/z and major peaks at 192, 205, and 370 m/z.

• Journal of Applied Biological Chemistry
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• v.42 no.3
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• pp.107-112
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• 1999

A carboxymethyl-cellulase (CMCase) was purified from the culture supernatant of Bacillus sp. KD1014 by ultrafiltration, ammonium sulfate precipitation, and a series of chromatography on QAE-Sephadex A-50, hydroxylapatite and Sephadex G-75. The purified CMCase was a single protein of 32 kDa, showed an optimum activity at $60^{\circ}C$ and pH 6.0, and had a half-life of 23 min at $70^{\circ}C$. The enzyme activity was not influenced by metal ions such as $Mg^{2+},\;Fe^{3+},\;K^+,\;Zn^{2+}$, and $Cu^{2+}$ at a concentration of 1.0 mM, partially inhibited by $Mn^{2+}$ and $Ag^+$, and significantly inhibited by pentachlorophenol (PCP). The purified enzyme showed a 3.9-times higher activity on lichenan than on CMC, but hardly cleaved xylan, starch, avicel, laminarin, filter paper and levan. The results of activity staining of the purified enzyme separated by native and denaturing gel electrophoresis suggested that the CMCase might exist in dimeric, oligomeric or aggregated form as well as in monomeric form. The enzymatic cleavage products from cellotetraose indicated that the CMCase possessed transglycosylation activity.

• The Plant Pathology Journal
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• v.38 no.5
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• pp.490-502
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• 2022

Xanthomonas oryzae pv. oryzae (Xoo) causes bacterial leaf blight (BLB) disease in rice (Oryza sativa L.) and it is among the most destructive pathogen responsible for severe yield losses. Potential bacterial biocontrol agents (BCAs) with plant growth promotion (PGP) abilities can be applied to better manage the BLB disease and increase crop yield, compared to current conventional practices. Thus, this study aimed to isolate, screen, and identify potential BCAs with PGP abilities. Isolation of the BCAs was performed from internal plant tissues and rhizosphere soil of healthy and Xoo-infected rice. A total of 18 bacterial strains were successfully screened for in vitro antagonistic ability against Xoo, siderophore production and PGP potentials. Among the bacterial strains, 3 endophytes, Bacillus sp. strain USML8, Bacillus sp. strain USML9, and Bacillus sp. strain USMR1 which were isolated from diseased plants harbored the BCA traits and significantly reduced leaf blight severity of rice. Simultaneously, the endophytic BCAs also possessed plant growth promoting traits and were able to enhance rice growth. Application of the selected endophytes (BCAs-PGP) at the early growth stage of rice exhibited potential in suppressing BLB disease and promoting rice growth.

• Preventive Nutrition and Food Science
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• v.9 no.2
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• pp.138-143
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• 2004

Soybean curd residues (SCR) obtained from hot and cold manufacturing processes were fermented by indigenous microorganisms, Lactobacillus rhamnosus LS and Bacillus firmus NA-l for 15 h at 37$^{\circ}C$. The pH, acidity, viable cell counts, and tyrosine content were evaluated in samples with variations in sugar, starter and type of SCR. The raw Doowon SCR (D-SCR, cold-processed) fermented by indigenous microorganism had a 0.9% acidity and 6.7 ${\times}$ 10$^{7}$ CFU/g viable cell counts, compared with the 0.11 % acidity and 6.7 ${\times}$ 10$^{6}$ CFU/g viable cell counts of raw fermented Pulmuwon SCR (P-SCR, hot-processed). After fermentation of raw P-SCR with 1 % glucose and 1 % L. rhamnosus LS starter, the viable cell counts, tyrosine content and acidity were 4.7 ${\times}$ 10$^{8}$ CFU/g, 16.3 mg% and 0.9%, respectively. In addition, the raw P-SCR fermented with Bacillus firmus NA-l as co-starter had a 0.45% acidity, 2.4 ${\times}$ 10$^{8}$ CFU/g lactic acid bacteria, and 3.3 ${\times}$ 10$^{6}$ CFU/g Bacillus sp. In particular, the tyrosine content was increased 5 fold. The drying of fermented SCR was completed by hot-air drying (5$0^{\circ}C$) within 12 h; the dried P-SCR and D-SCR had 1.8 ${\times}$ 10$^{7}$ CFU/g and 5.3 ${\times}$ 10$^{6}$ CFU/g viable cell counts, respectively. The concentrate of methanol extract from fermented D-SCR inhibited the initial cell growth of E. coli, Staphylococcus aureus and Pseudomonas aeruginosa in liquid culture.

• Microbiology and Biotechnology Letters
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• v.31 no.2
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• pp.103-110
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• 2003

The regulation of pyrimidine nucleotide synthesis has been proved to be controlled by a regulatory protein PyrR-mediated attenuation in the Gram-positive bacteria. After several bacterial genome sequencing projects, we have discovered the PyrR orthologues in the databases for Haemophilus influenzae and Synechocystis and sp. PCC6803 genome sequences. To investigate whether these PyrR orthologue proteins regulate pyrimidine nucleotide synthesis as well as the cases of Bacillus, the PyrR regions of each strains were amplified by PCR and cloned with pUC19 or T-vector in Escherichia coli and with a shuttle vector pHPS9 for E. coli and B. subtilis. For the regulation test of the PyrR orthologues, the aspartate-transcarbamylase (ATCase) assay was carried out. From the results of the ATCase assay, it was confirmed that Synechocystis sp. PCC6803 could not restore by pyrimidines to a B. subtilis, PyrR but H. influenzae PyrR could. For Purification of PyrR orthologue proteins, PyrR orthologue genes were cloned into the expression vector (pET14b). Over-expressed product of PyrR orthologue genes was purified and analyzed by the SDS-PACE. The purified PyrR orthologue proteins from H. influenzae and Synechocystis sp. PCC6803 turned out to be molecular mass of 18 kDa and 21 kDa, respectively. The result of uracil phosphoribosyl transferase (UPRTase) assay with purified PyrR orthologue proteins showed that H. influenzae PyrR protein only has UPRTase activity. In addition, we could predict several regulatory mechanisms that PyrR orthologue proteins regulate pyrimidine de novo synthesis in bacteria, through phylogenetic analysis for PyrR orthologue protein sequences.