135 resultados para fourier transform infrared


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Films of poly(hydroxybutyrate-co-hydroxyvalerate) (PHBV) and poly(propylene) (PP), PP/PHBV (4:1), blends were prepared by melt-pressing and investigated with respect to their microbial degradation in soil after 120 days. Biodegradation of the films was evaluated by Fourier transform infrared spectroscopy, scanning electron microscopy, differential scanning calorimetry, and X-ray diffraction. The biodegradation and/or bioerosion of the PP/PHBV blend was attributed to microbiological attack, with major changes occurring at the interphases of the homopolymers. The PHBV film was more strongly biodegraded in soil, decomposing completely in 30 days, while PP film presented changes in amorphous and interface phase, which affected the morphology.

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Poly(hydroxybutyrate-co-valerate) (PHBV) and poly(epsilon-caprolactone) (PCL) PCL/PHBV (4:1) blend films were prepared by melt-pressing. The biodegradation of the films in response to burial in soil for 30 days was investigated by Fourier transform infrared spectroscopy (FTIR), scanning electron microscopy (SEM), differential scanning calorimetry (DSC) and thermogravimetry (TG). The PHBV film was the most susceptible to microbial attack, since it was rapidly biodegraded via surface erosion in 15 days and completely degraded in 30 days. The PCL film also degraded but more slowly than PHBV. The degradation of the PCL/PHBV blend occurred in the PHBV phase, inducing changes in the PCL phases (interphase) and resulting in an increase of its crystalline fraction.

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Films made from a blend of poly(epsilon-caprolactone) and poly(vinyl chloride) (PCL/PVC) retained high crystallinity in a segregated PCL phase. Structural and morphological changes produced when the films were exposed to high potency ultraviolet (UV) irradiation for 10 h were measured by UV-Vis spectroscopy (UV-Vis), Fourier Transform Infrared Spectroscopy (FTIR), and Scanning Electron Microscopy (SEM). They were different to those observed with homopolymer PCL and PVC films treated under the same conditions. The FTIR spectra of the PCL/PVC blend suggest that blending decreased the susceptibility of the PCL to crystallize when irradiated. Similarly, although scanning electron micrographs of PCL showed evidence of growth of crystalline domains, particularly after UV irradiation, the images of PCL/PVC were fairly featureless. It is apparent that the degradation behavior is strongly influenced by the interaction of the two polymers in the amorphous phase.

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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This study investigated the microbial action in soil on poly(L-lactic acid) (PLLA) and polyvinyl chloride (PVC) films and a PLLA/PVC 7 : 3 blend, using Fourier transform infrared spectroscopy (FTIR), contact angle and scanning electron microscopy (SEM). The films (50 mu m) were obtained from the evaporation of dichloromethane solutions and buried in soil columns, in controlled conditions, for 120 days. The results showed that the surface of the PLLA films and blend became 18 and 31% more hydrophilic, respectively. The morphology of the films also changed after 120 days of microbial treatment, particularly that of the PLLA phase in the blend, confirmed by structural and conformational changes in the FTIR CO region at 12001000 cm1 and an increase in the relative intensity of the band at 1773 cm1, which was attributed to C O group vibration due to a rotational isomer in the interlamellar region (semi-ordered region). Besides the biotreated PVC presented changes in the C-Cl band at 738 cm1, due to the presence of some PVC conformational isomer. (C) 2011 Wiley Periodicals, Inc. J Appl Polym Sci, 2012

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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We have studied at a molecular level the interaction of heparins on bothropstoxin-1 (BthTx-1), a phospholipase A(2) toxin. The protein was monitored using gel filtration chromatography, dynamic light scattering (DLS), circular dichroism (CD), attenuated total reflectance Fourier transform infrared (ATR-FTIR) and intrinsic tryptophan fluorescence emission (ITFE) spectroscopy. The elution profile of the protein presents a displacement of the protein peak to larger complexes when interacting with higher concentration of heparin. The DLS results shows two R-h at a molar ratio of 1, one to the distribution of the protein and the second for the action of heparin on BthTx-I structures, and a large distribution with the increase of protein. The interaction is accompanied by significant changes in the CD spectra, showing two common features: a decrease in signal at 208 nm (3 and 6 kDa heparins) and an isodichroic point near 226 nm (3 kDa heparin). FTIR spectra indicate that only a few amino acid residues are involved in this interaction. Alterations in the ITFE by binding heparins suggest that the initial binding occurs on the ventral face of BthTx-1. Together, these results add an experimental and structural basis on the action mechanism of the heparins over the phospholipases A(2) and provide a molecular model to elucidate the interaction of the enzyme-heparin complex at a molecular level. (c) 2005 Elsevier B.V. All rights reserved.

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Bothropstoxin-I (BthTx-I) is a Lys49-PLA(2) from the venom of Bothrops jararacussu that lacks detectable catalytic activity, yet causes rapid Ca2+-independent membrane damage. With the aim of understanding the interaction between BthTx-I and amphiphilic molecules, we have studied the interaction of sodium dodecyl sulphate (SDS) with the protein. Circular dichroism and attenuated total reflection Fourier-transform infrared spectra of BthTx-I reveal changes in the alpha-helical organization of the protein at an SDS/BthTx-I molar ratio of 20-25. At SDS/BthTx-I ratios of 40-45 the alpha-helices return to a native-like conformation, although fluorescence emission anisotropy measurements of 2-amino-N-hexadecyl-benzamide (AHBA) demonstrate that the total SDS is below the critical micelle concentration when this transition occurs. These results may be interpreted as the result of SDS accumulation by the BthTx-I homodimer and the formation of a pre-micelle SDS/BthTx-I complex, which may subsequently be released from the protein surface as a free micelle. Similar changes in the alpha-helical organization of BthTx-I were observed in the presence of dipalmitoylphosphatidylcholine liposomes, suggesting that protein structure transitions coupled to organization changes of bound amphiphiles may play a role in the Ca2+-independent membrane damage by Lys49-PLA(2)s. (c) 2006 Elsevier B.V. All rights reserved.

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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)