• Journal of Korean Society of Environmental Engineers
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• v.28 no.9
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• pp.917-925
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• 2006

The aim of our research was to apply experimental design methodology in the optimization of photocatalytic degradation of azo dye(Reactive orange 16). The reactions were mathematically described as a function of parameters amount of $TiO_2(x_1)$, and dye concentration($x_2$) being modeled by the use of the Box-Behnken method. The results show that the responses of color removal(%)($Y_1$) in photocatalysis of dyes were significantly affected by the synergistic effect of linear term of $TiO_2(x_1)$ and dye concentration($x_2$). Significant factors and synergistic effects for the $COD_{Cr}$, removal(%)($Y_2$) were the linear term of $TiO_2(x_1)$ and dye concentration($x_2$). However, the quadratic term of $TiO_2(x_1^2)$ and dye concentration($x_2^2$) had an antagonistic effect on $Y_1$ and $Y_2$ responses. Canonical analysis indicates that the stationary point was a saddle point for $Y_1$ and $Y_2$, respectively. The estimated ridge of maximum responses and optimal conditions for $Y_1:(X_1,\;X_2)$=(1.11 g/L, 51.2 mg/L) and $Y_2:(X_1,\;X_2)$=(1.42 g/L, 72.83 mg/L) using canonical analysis was 93% and 73%, respectively.

• Microbiology and Biotechnology Letters
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• v.46 no.1
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• pp.40-44
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• 2018

An isolate capable of inhibiting the growth of gram-positive bacteria was obtained from the soil of Mushim stream, Cheongju. The isolate was identified as Pseudomonas otitidis PS by 16S rRNA gene sequence analysis. P. otitidis PS produced antibiotics as a secondary metabolite when cultured in 1% soybean meal with 0.5% glucose. The maximum yield was about 0.1%. The antibiotic substance of P. otitidis PS extracted using ethyl acetate displayed a minimum inhibitory concentration of $2{\mu}g/ml$ for Staphylococcus aureus KCTC 1261. The antibiotic substance produced an orange halo on chrome azurol S agar due to siderophore activity. Growth inhibition was decreased when the iron was depleted. Since the antibiotic activity was lost upon the addition of the reducing agent ascorbic acid or during anaerobic culture, it was considered that antibiotic of P. otitidis PS strain exerts its bactericidal effect by the generation of reactive oxygen species.

• Journal of Microbiology and Biotechnology
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• v.23 no.2
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• pp.237-245
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• 2013

Canthaxanthin (cx) is a potent antioxidant that is chemically synthesized at the industrial scale and has imperative applications in the cosmetic and feed industries. An orange pigmented mesophilic bacterium, designated as K44, was isolated from soil samples of Kargil, India. Biochemical tests, 16S rRNA gene sequencing, and FAME analysis of the bacterium indicated it to belong in the genus Dietzia and is distinct from human isolates. The strain showed 98% 16S rRNA gene sequence homology with Dietzia maris DSM 43102. High-performance liquid chromatography profile of the pigments isolated from K44 showed two major peaks absorbing at 465.3 and 475 nm. The liquid chromatography-mass spectrometry (LC-MS) analysis of both these peaks revealed their m/z to be 564. The molecular weights, LC-MS/MS fragmentation patterns, and ${\lambda}_{max}$ of these fractions corresponded to all-trans- (475 nm) and 9-cis-(465.3 nm) cx isomers. The antioxidant activities of cis- and trans-cx isomers isolated from this bacterium were found to differ, where the cis-isomer showed higher free radical, superoxide radical, and reactive oxygen species scavenging activities than the alltrans- isomer, suggesting that 9-cis-cx is more effective as an antioxidant than the all-trans-cx.

• Journal of Microbiology and Biotechnology
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• v.27 no.6
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• pp.1120-1127
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• 2017

Marasmius scorodonius secretes an extracellular laccase in potato dextrose broth, and this enzyme was purified up to 206-fold using $(NH_4)_2SO_4$ precipitation and a Hi-trap Q Sepharose column. The molecular mass of the purified laccase was estimated to be ~67 kDa by SDS-PAGE. The UV/vis spectrum of the enzyme was nontypical for laccases, and metal content analysis revealed that the enzyme contains 1 mole of Fe and Zn and 2 moles of Cu per mole of protein. The optimal pH for the enzymatic activity was 3.4, 4.0, and 4.6 with 2,2'-azino-bis(3-ethylbenzothazoline-6-sulfonate) (ABTS), guaiacol, and 2,6-dimethoxy phenol as the substrate, respectively. The optimal temperature of the enzyme was $75^{\circ}C$ with ABTS as the substrate. The enzyme was stable in the presence of some metal ions such as $Ca^{2+}$, $Cu^{2+}$, $Ni^{2+}$, $Mg^{2+}$, $Mn^{2+}$, $Ba^{2+}$, $Co^{2+}$, and $Zn^{2+}$ at a low concentration (1 mM), whereas $Fe^{2+}$ completely inhibited the enzymatic activity. The enzymatic reaction was strongly inhibited by metal chelators and thiol compounds except for EDTA. This enzyme directly decolorized Congo red, Malachite green, Crystal violet, and Methylene green dyes at various decolorization rates of 63-90%. In the presence of 1-hydroxybenzotriazole as a redox mediator, the decolorization of Reactive orange 16 and Remazol brilliant blue R was also achieved.