• Polymer(Korea)
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• v.28 no.4
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• pp.314-320
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• 2004

Soluble aromatic polyimides bearing 4-(4-oxyalkyleneoxystyryl)- pyridines (ethylene and hexylene) as photoreactive side groups were synthesized and characterized. The photoreactive polymers were soluble in various polar organic solvents and their films were easily formed by solution casting. The photoreactivities of the polymers in the film state were approximately 64% at an exposure energy of 1.5 J/$\textrm{cm}^2$. Transmittances of the polymer films were about 85% after annealing at 20$0^{\circ}C$. Therefore, these polymers can be evaluated to be photoreactive polyimides with good transparency and solubility. The dichroic ratios of the polymers with ethylene and hexylene groups as the alkylene spacers were 0.023 and 0.026, respectively. The order parameters of 4'-pentyl-4-bipheny1carbonitrile as a liquid crystal (LC) in the film cells of the former and latter polymers were 0.50 and 0.52, respectively. These results indicate that the polymers show the effect of alkylene spacer on the photoalignments. The LC in the film cells of the polymers was perpendicularly oriented to the electric vector of the linear polarized UV light (LPUVL).

• Journal of Life Science
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• v.19 no.9
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• pp.1218-1225
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• 2009

Difractose anhydrides (DFAs) is studied as a sweetener for diabetics because of its structural property. DFAs have four types: DFA I, III, IV (degradation of levan) and V (degradation of inulin). Especially, DFA IV has been shown to enhance the absorption of calcium in experiments using rats. Levan fructotransferase is an enzyme for producing di-d-fructose-2,6':6,2-dianhydride (DFA IV). To identify structural characterization, we purified wild-type and mutants (D63A, D195N and N85S) of levan fructotransferase (LFTase) from Microbacterium sp. AL-210. These proteins were purified to apparent homogeneity by Ni-NTA affinity column, Q-sepharose ion exchange and gel filtration chromatography and detected by SDS-PAGE. They were also analyzed by circular dichroism (CD) measurements, JNET secondary structure prediction, activity measurements at various temperatures, and pH analysis. The optimum pH for the enzyme-catalyzed reaction was pH 7.5 and optimum temperature was observed at $55^{\circ}C$. Along with wild-type LFTase, mutants were analyzed by CD measurement, fluorescence analysis and differential scanning calorimetry (DSC). N85S showed less $\alpha$-helix and more $\beta$ strand than others. Also, N85S showed almost the same curve as wild-type in their steady-state fluorescence spectra, whereas mutant D63A and D195N showed higher intensity than wild-type. The amino acid sequence of wild-type LFTase was compared to the sequences of exo-inulinase from Aspergillus awamori, a plant fructan 1-exohydrolase from Cichorium intybus, and Thermotogo maritime (Tm) invertase and showed a high identity with Exo-inulinase from Aspergillus awamori.