• Journal of Korean Society of Environmental Engineers
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• v.34 no.6
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• pp.406-413
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• 2012

Effect of three additives, chitosan, ferric chloride, and MPE50 on membrane fouling reduction was studied. They were introduced with various dosing rate into activated sludge, and changes in filtration resistance measured by the batch cell filtration test were evaluated. Both the filtration resistance and the specific cake resistance were minimized at 20 mg/g-MLSS with chitosan, 70 mg/g-MLSS with ferric chloride, and 20 mg/g-MLSS with MPE50 addition, respectively. Introduction of the additives into the activated sludge resulted in reduction of not only cake resistance, but also fouling resistance. However, the chitosan addition to three different activated sludge resulted in three different optimal dose of 10, 20, 30 mg/g-MLSS, respectively. This implies that the optimal dose is dependent on sludge characteristics rather than a constant value. Overdose above the optimal dosage always aggravated filterability in all cases. Zeta potential of sludge flocs, relative hydrophobicity, floc size distribution, soluble EPS concentration and supernatant turbidity were measured in order to analyze fouling reduction mechanism. Nearly neutral surface charge along with the largest particle size was observed at the optimal dose. This could be explained by particle destabilization and restabilization mechanism as positively charged additives were injected into sludge flocs of negative surface charge. Both soluble EPS concentration and supernatant turbidity also showed the lowest value at the optimal dose. These foulants are believed to be coagulated and entrapped in sludge flocs during flocculation. Chitosan and MPE50 which are cationic polymeric substances showed higher reduction in both soluble EPS and fine particles comparing with ferric chloride.

• Journal of Life Science
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• v.19 no.8
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• pp.1039-1046
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• 2009

The cytochrome P450s (P450s) metabolizing natural products are among the most versatile biological catalysts known in plants, but knowledge of the structural basis for their broad substrate specificity has been limited. The activity of p-coumarate 3-hydroxylase (C3H) is thought to be essential for the biosynthesis of lignin and many other phenylpropanoid pathway products in plants however, all attempts to express and purify the protein corresponding C3H gene have failed. As a result, no conditions suitable for the unambiguous assay of the enzyme are known. The detailed understanding of the mechanism and substrate-specificity of C3Hdemands a method for the production of active protein on the milligram scale. We have developed a bacterial expression and purification system for the plant C3H, which allows for the quick expression and purification of active wild-type C3H via introduction of combinational mutagenesis. The modified cytochrome P450 C3H ($C3H_{mod}$) could be purified in the absence of detergent using immobilized metal affinity chromatography and size exclusion chromatography following extraction from isolated membranes in a high salt buffer and catalytically activated. This method makes the use of isotopic labeling of C3H for NMRstudies and X-ray crystallography practical, and is also applicable to other plant cytochrome P450 proteins.