The adsorption spectra of plasticized BDIS (IA-80%) polyamide samples were recorded on a TENSOR 27 Fourier transform infrared spectrophotometer (Bruker, Rheinstetten, Germany) equipped with a Smart Orbit diamond-attenuated total reflection (ATR) accessory. The spectra were collected in the wavenumber range 500–4000 cm−1 at a resolution of 4 cm−1, and the signal averaged over 32 scans. FTIR spectra of water-plasticized BDIS (IA-80%) polyamide were baseline-corrected and normalized to the average of the C=O peaks at 1643 cm−1. FTIR spectra of glycerol and soybean oil were baseline-corrected and normalized to the average of the N–H bending(amide II band) at 1540 cm−1.
Tensor 27 fourier transform infrared
Manufactured by Bruker
Sourced in Germany
The TENSOR 27 is a Fourier transform infrared (FTIR) spectrometer manufactured by Bruker. It is designed to analyze the composition and structure of various materials by measuring their infrared absorption or emission spectra.
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Lab products found in correlation
3 protocols using tensor 27 fourier transform infrared
1
FTIR Analysis of Plasticized Polyamide
2
Characterization of Calcium Hydroxyapatite Adsorbent
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A Hitachi, Japan, S–3000H model scanning electron microscope coupled with energy dispersive X-ray (EDX) was deployed for the elemental composition analysis of CHAp, while a PANalytical, X'Pert PRO, Netherland model of X-ray diffractometer was used to determine the phase purity and crystallinity in an incremental step size of 0.02 using CuKα (γ = 1.54178 °A) within the range of 10° to 60°. A TENSOR 27 Fourier transform infrared (Bruker, Germany) (FT-IR) was utilized for the functional group investigation from 400 to 4000 cm−1. A Tecnai 20 G2 FEI (Netherland) model of Transmission electron microscope (TEM) was used to further investigate the surface morphology of the adsorbent. The zero point charge (pHzpc) of CHAp was performed by using a Zetasizer Nano ZS instrument (Malvern, UK) from a solution of cadmium ion prepared by dissolving 0.1 g of CHAp in 25 ml of cadmium solution.
3
Infrared Spectroscopy Analysis of Protein Aggregates
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The secondary
structure of the protein aggregates/fibrils was analyzed with infrared
spectroscopy using a Tensor 27 Fourier transform infrared (FTIR) instrument
(Bruker Optics). The sample (2.0 μL) was deposited on an attenuated
total reflection crystal, dried with nitrogen gas, and analyzed with
the program OPUS version 5.5. Spectra were averaged over 68 scans
in the 1000–3999 cm–1 range. Data were analyzed
by calculating the atmospheric compensation, subtracting the baseline,
and preparing the second-derivative spectra. Only the amide I band
(1600–1700 cm–1) is shown.
structure of the protein aggregates/fibrils was analyzed with infrared
spectroscopy using a Tensor 27 Fourier transform infrared (FTIR) instrument
(Bruker Optics). The sample (2.0 μL) was deposited on an attenuated
total reflection crystal, dried with nitrogen gas, and analyzed with
the program OPUS version 5.5. Spectra were averaged over 68 scans
in the 1000–3999 cm–1 range. Data were analyzed
by calculating the atmospheric compensation, subtracting the baseline,
and preparing the second-derivative spectra. Only the amide I band
(1600–1700 cm–1) is shown.
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