Type I collagen was extracted from rat tail tendons (N-COL), using a protocol developed in-house, in line with the one reported by Rajan et al. [23 (link)]. Briefly, the collagen fibres were dissected into small portions and dried under a biological hood. The dried fibres were weighted and transferred in 0.2% acetic acid (0.2%AA) creating a stock solution. The collagen was stirred at 4 °C for 3 days, and then triturated using a standard hand blender, in an ice bath to prevent overheating. The obtained homogenized mixture was centrifuged at 3500 rpm, at 4 °C for 45 min, then filtered and stored at 4 °C. Prior to use, the collagen was aliquoted in 50 mL tubes, and frozen at −20 °C for 24 h. The samples were then lyophilized with a Lyovapor L-200 freeze-dryer (Büchi, Switzerland) under vacuum (<0.1 mbar) for 72 h. 1 g of N-COL was added to 5 mL of a solution of acetic acid (40% v/v) in ddH2O (40%AA), to achieve a final concentration of N-COL 20% w/w (named hereafter 20N-COL). The solution was left to stir overnight, at room temperature, to ensure full dissolution of the collagen.
Lyovapor l 200 freeze dryer
Manufactured by Büchi
Sourced in Switzerland
The Lyovapor L-200 is a freeze-dryer designed for laboratory applications. It removes water from frozen samples through the process of sublimation, converting the solid ice directly into water vapor without passing through the liquid phase. The Lyovapor L-200 features a condenser capacity of 8 kg and a shelf capacity of 5 kg.
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Lab products found in correlation
5 protocols using lyovapor l 200 freeze dryer
1
Extraction and Solubilization of Type I Collagen
2
Lyophilization and FESEM Imaging of Collagen-Based Biomaterials
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Before sample examination by Field-Emission Scanning Electron Microscopy (FESEM), GEN/EtOH crosslinked Coll/MBG_Sr4% and Coll/nano-HA bulk samples were frozen at −20 °C and lyophilized for 24 h using a Lyovapor L-200 freeze-dryer (Büchi, Flawil, Switzerland) under vacuum (<0.1 mbar). For the morphological assessment, the lyophilized samples were coated with a 7 nm thin platinum layer and analyzed using a ZEISS MERLIN FESEM instrument.
3
Collagen-MBG Composite Characterization
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Morphological and compositional analyses on Coll/MBG_Sr4% samples were performed to investigate the proper reconstitution of collagen fibers while observing the distribution of the glass particles embedded in the collagenous matrix. In details, Coll/MBG_Sr4% samples were frozen at −20 °C and subsequently lyophilized for 24 h using a Lyovapor L-200 freeze-dryer (Büchi, Switzerland) under vacuum (<0.1 mbar). Cross-sections of lyophilized samples were coated with a 7 nm thin chromium layer and analyzed by field-emission scanning electron microscopy (FESEM) and energy-dispersive X-ray spectroscopy (EDS).
FTIR spectra, in the 4000–650 cm−1 range, were collected by using a Bruker Equinox 55 spectrometer, equipped with MCT cryodetector, at a spectral resolution of 4 cm−1 and accumulation of 32 scans, by using the attenuated total reflection (ATR) mode.
FTIR spectra, in the 4000–650 cm−1 range, were collected by using a Bruker Equinox 55 spectrometer, equipped with MCT cryodetector, at a spectral resolution of 4 cm−1 and accumulation of 32 scans, by using the attenuated total reflection (ATR) mode.
4
Characterization of Collagen-Based Biomaterial
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Morphological evaluation was performed to observe the reconstitution of collagen fibrils at physiological temperature and pH, and the distribution of the inorganic phases into the collagen matrix.
Before printing, bulk samples of Coll/nanoMBG/nanoHA were obtained by pipetting the collagen‐based suspension in a silicon mold, that was subsequently incubated at 37°C for 3 h.
For the analyses, both bulk samples and chemically crosslinked 3D printed scaffolds were lyophilized for 24 h after freezing at −20°C, using a Lyovapor L‐200 freeze‐dryer (Büchi, Switzerland) under vacuum (<0.1 mbar). Cross‐sections of lyophilized samples were sputter‐coated with platinum (7 nm thickness layer) and analyzed through Field‐Emission Scanning Electron Microscopy (FESEM) with a ZEISS MERLIN instrument (Carl Zeiss AG, Oberkochen, Germany).
The chemical composition of the developed biomaterial was then confirmed by means of Fourier‐transform infrared spectroscopy (FTIR) and by using the attenuated total reflection (ATR) mode. The resulting spectrum, in the 4000–650 cm−1 range, were collected by using a Bruker Equinox 55 spectrometer, equipped with MCT cryodetector, at a spectral resolution of 4 cm−1 and accumulation of 32 scans.
Before printing, bulk samples of Coll/nanoMBG/nanoHA were obtained by pipetting the collagen‐based suspension in a silicon mold, that was subsequently incubated at 37°C for 3 h.
For the analyses, both bulk samples and chemically crosslinked 3D printed scaffolds were lyophilized for 24 h after freezing at −20°C, using a Lyovapor L‐200 freeze‐dryer (Büchi, Switzerland) under vacuum (<0.1 mbar). Cross‐sections of lyophilized samples were sputter‐coated with platinum (7 nm thickness layer) and analyzed through Field‐Emission Scanning Electron Microscopy (FESEM) with a ZEISS MERLIN instrument (Carl Zeiss AG, Oberkochen, Germany).
The chemical composition of the developed biomaterial was then confirmed by means of Fourier‐transform infrared spectroscopy (FTIR) and by using the attenuated total reflection (ATR) mode. The resulting spectrum, in the 4000–650 cm−1 range, were collected by using a Bruker Equinox 55 spectrometer, equipped with MCT cryodetector, at a spectral resolution of 4 cm−1 and accumulation of 32 scans.
5
Freeze-drying of EO Extracts
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The frozen remaining water after EO distillation was freeze-dried at − 54 °C and 0.05 mbar, through a BUCHI Lyovapor™ L-200 freeze-dryer (Büchi Labortechnik AG, Flawil, Switzerland). The lyophilized extracts (LE) were ground in a mortar and the obtained powders were maintained at 4 °C until further analyses.
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