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Adsorbents scanning electron microscopy

At a given pressure, the amounts of xenon adsorbed by the different phases allow one to estimate their relative crystallinities, with respect to the most crystalline sample, P32. These results are presented in Table 1. The isotherms of Po and P5 overlap, which implies that both intermediates have the same adsorption capacity. Although the X-ray diffraction and scanning electron microscopy... [Pg.14]

An interesting feature was observed during the study of surfactant adsorption onto LDHs, which was shown previously for the study of SDS adsorption onto an Mg-Al-CCVLDH [10, 11]. Nanoribbon-like image patterns, observed by scanning electron microscopy (SEM), were identified in the adsorbed material obtained at the isotherm plateau. [Pg.444]

Leaching studies indicate that these radionuclides associated with sediment are not in the form of adsorbed ions, but in the form of discrete minerals, or are partly trapped inside the colloidal hydroxides of Fe and Mn coated on the sediment. Further studies by other leaching agents, such as hydroxylamine hydrochloride, and ammonium oxalate, and by X-ray diffraction and scanning-electron microscopy on sediment minerals will reveal the geochemical status of these radionuclides in the sediment. [Pg.277]

Topics 1-3 can be addressed by the combined use of electron microscopy [HRTEM and scanning electron microscopy (SEM)] (47) and methods that probe the surfaces at the atomic level (e.g., by analyzing the modifications induced in the vibrational spectra of simple probe molecules adsorbed on the different coordinatively unsaturated sites (22, 23). [Pg.274]

Figure 12.2. The structure of ice cream mix and ice cream. (A). Fat globules (F) in mix with crystalline fat within the globule and adsorbed casein micelles (C), as viewed by thin section transmission electron microscopy. (B). Close-up of an air bubble (A) with adsorbed fat, as viewed by low temperature scanning electron microscopy. (C). Air bubble (A) with adsorbed fat cluster (FC) that extends into the unfrozen phase, as viewed by thin section transmission electron microscopy with freeze substitution and low temperature embedding. Figure 12.2. The structure of ice cream mix and ice cream. (A). Fat globules (F) in mix with crystalline fat within the globule and adsorbed casein micelles (C), as viewed by thin section transmission electron microscopy. (B). Close-up of an air bubble (A) with adsorbed fat, as viewed by low temperature scanning electron microscopy. (C). Air bubble (A) with adsorbed fat cluster (FC) that extends into the unfrozen phase, as viewed by thin section transmission electron microscopy with freeze substitution and low temperature embedding.
Various types of electron microscopy (TEM, transmission electron microscopy SEM, scanning electron microscopy) and atomic force microscopy (AFM) as well as a host of other spectroscopic techniques (XANES, Auger, LEED, EELS, PES, surface IR, ETV, solid state NMR, etc) give information about the surface structures of solids and also about the state of molecules adsorbed at the surface. [Pg.271]

The amount of adsorbed metal was determined by the weight difference of the pre-and post-sorption sorbent. The structural and morphological change of kaolinite granules during sorption tests was investigated by the powdered X-ray diffraction (XRD) analysis (Philips, X pert MPD) and scanning electron microscopy (SEM) (JEOL, JXA 8600). [Pg.560]

Improved analytical techniques are needed to detect the important configurational and chemical diflFerences among adsorbed films formed spontaneously from complex solutions on various substrates. Internal refiection IR does not reveal significant diflFerences in the adsorbed protein films which accumulate on variously treated Stellite 21 devices (a cobalt-chromium alloy used to make synthetic heart valve struts and seats) in some instances these devices are thrombogenic, and in others they are apparently thromboresistant (39). Yet, scanning electron microscopy reveals that arriving blood platelets can discern diflFerences in the films immediately on contact with them. [Pg.14]

Fig. 7. The effect of adsorbed protein on structure of ice-cream mix, ice cream, and melted ice cream. A-B, ice-cream mix with no surfactant and with added surfactant, respectively, as viewed by thin-section transmission electron microscopy. f= fat globule, c = casein micelle, arrow = crystalline fat, bar = 0.5 pm. See Reference 24 for methodology. C-D, ice cream with no surfactant and with added surfactant, respectively, as viewed by low-temperature scanning electron microscopy, a = air bubble, f = fat globule, bar = 4 pm. See Reference 34 for methodology. E-F, ice cream with no surfactant and with added surfactant respectively, as viewed by thin-section transmission electron microscopy with freeze substitution and low-temperature embedding. a = air bubble, f= fat globule, c = casein micelle, fc = fat cluster, bar = 1 pm. See Reference 13 for methodology. G-H, melted ice cream with no surfactant and with added surfactant respectively, as viewed by thin-section transmission electron microscopy. f= fat globule, c = casein micelle, fn = fat network, bar = 1 pm in G and 5 pm in H. See Reference 24 for methodology. Fig. 7. The effect of adsorbed protein on structure of ice-cream mix, ice cream, and melted ice cream. A-B, ice-cream mix with no surfactant and with added surfactant, respectively, as viewed by thin-section transmission electron microscopy. f= fat globule, c = casein micelle, arrow = crystalline fat, bar = 0.5 pm. See Reference 24 for methodology. C-D, ice cream with no surfactant and with added surfactant, respectively, as viewed by low-temperature scanning electron microscopy, a = air bubble, f = fat globule, bar = 4 pm. See Reference 34 for methodology. E-F, ice cream with no surfactant and with added surfactant respectively, as viewed by thin-section transmission electron microscopy with freeze substitution and low-temperature embedding. a = air bubble, f= fat globule, c = casein micelle, fc = fat cluster, bar = 1 pm. See Reference 13 for methodology. G-H, melted ice cream with no surfactant and with added surfactant respectively, as viewed by thin-section transmission electron microscopy. f= fat globule, c = casein micelle, fn = fat network, bar = 1 pm in G and 5 pm in H. See Reference 24 for methodology.
The surface of ACF of w = 1.45 nm was modified with molecular adsorption-decomposition method using SiCU. SiCU was adsorbed on the ACF and then hydrolyzed by introduction of H2O vapour at 298 K. Afterwards, residual SiCU and produced HCl vapours were removed, and then the treated ACF was heated at 573 K. The amount of the produced hydrated silica was determined by the measurement of the weight change. The micropore structure of the silica-coated ACF was examined by N2 adsorption the t-plot analysis of the N2 adsorption isotherm showed that the micropore width decreases with the silica coating by 0.2 nm the silica coating decreased the micropore volume and surface area from 1.49 ml/g and 2280 m /g to 0.68 ml/g and 1100 m /g, respectively. No spherical silica particles were observed on the external surface of the silica-coated ACF by scanning electron microscopy with a resolution of 10 nm. Therefore, hydrated silica should be deposited entirely on the micropore walls of the ACF. [Pg.582]

Figure 3.1 is a scanning electron microscopy (SEM) photograph of Novozym 435 before and after immobilization of CALB on the matrix (Lewatit). It is obvious that after immobilization, the enzyme has been adsorbed on the surface of the matrix and the surface has been saturated. This observation confirms the results of synchrotron infrared microspectroscopy performed at amide band wavelength on Novozym 435 (Figure 3.2) [5, 6], The researchers measured the intensity of the amide band across the cross-section of a Novozym 435 bead and attributed the presence of amide groups to the location of the enzyme immobilized on the bead. They showed that distribution of CALB on the bead is not homogenous and it mostly saturates the surface of the beads and hardly enters the center. The CALB enzyme is a globular protein with dimensions of 30 A x 40 A x 50 A [10], whereas... Figure 3.1 is a scanning electron microscopy (SEM) photograph of Novozym 435 before and after immobilization of CALB on the matrix (Lewatit). It is obvious that after immobilization, the enzyme has been adsorbed on the surface of the matrix and the surface has been saturated. This observation confirms the results of synchrotron infrared microspectroscopy performed at amide band wavelength on Novozym 435 (Figure 3.2) [5, 6], The researchers measured the intensity of the amide band across the cross-section of a Novozym 435 bead and attributed the presence of amide groups to the location of the enzyme immobilized on the bead. They showed that distribution of CALB on the bead is not homogenous and it mostly saturates the surface of the beads and hardly enters the center. The CALB enzyme is a globular protein with dimensions of 30 A x 40 A x 50 A [10], whereas...
High silicious HZSM-5, which has no activity for catalytic reactions (e.g. cracking) of the adsorbates, was hydrothermaliy synthesized from silica gel in the range of temperature from 433 to 473 K. The prepared zeolites were found to have the same characteristics of the HZSM-5 zeolite by X-ray diffraction analysis. The crystallites were found to have a cubic shape by a scanning electron microscopy photo of the crystallites and these sizes were uniformly 2.1 jtm. [Pg.478]

Due to the fundamental importance of the adsorbed protein film, many methods have been used to characterize its nature. These methods include ellipsometry (3,A), Fourier transform infrared spectroscopy (FTIR) (5,6), multiple attenuated internal reflection spectroscopy (MAIR) (7,8) immunological labeling techniques (9), radioisotope labeled binding studies (j ), calorimetric adsorption studies (jj ), circular dichroism spectroscopy (CDS) (12), electrophoresis (j ), electron spectroscopy for chemical analysis (ESCA) (1 ), scanning electron microscopy (SEM) (15,16,9), and transmission electron microscopy (TEM) (17-19). [Pg.49]


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See also in sourсe #XX -- [ Pg.5 , Pg.297 ]




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