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16 protocols using sonopuls hd 3100

1

Comparative Bacterial Proteome Extraction

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The same procedure of preparing bacterial protein lysate was used for the comparison of Salmonella Typhimurium protein expression when cultivated in LB or BHI medium using MS and for immunoaffinity chromatography.
Salmonella Typhimurium was grown overnight at 37 °C in LB and BHI medium, as noted above. The culture was then centrifuged (3,500 × g, 10 min), and a cell pellet was washed 3 times in PBS (Dulbecco’s, Lonza, Switzerland). The cell pellet was resuspended in PBS and sonicated (Sonopuls HD 3100, Bandelin, Germany) with zirconia/silica beads (BioSpec Products, USA). The sonicate was centrifuged at 20,000 × g and the supernatant with proteins was taken. The pellet was then resuspended in 8 M urea (Serva, Germany), 0.1 % SDS (Carl Roth, Germany), 2 % Triton X-100 (Serva, Germany) and 25 mM triethylammonium bicarbonate (Sigma-Aldrich, USA) and centrifuged at 20,000 × g again. The supernatant was mixed with the supernatant from the previous step and together used as an antigen for subsequent analysis.
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2

Synthesis and Anion-Exchange of CsPbBr3 Nanocrystals

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In a typical synthesis,
10 mL of 1-octadecene, 0.5 mL of oleic acid
and 0.5 mL of oleylamine were added to Cs2CO3 (0.1 mmol) and PbBr2 (0.3 mmol) precursor powders. Then,
tip-sonication (SONOPULS HD 3100, BANDELIN) was applied to the mixture
solution at a power of 30 W for 10 min. The as-prepared NC dispersions
were purified without adding any antisolvents by centrifugation at
9000 rpm for 10 min to remove unreacted precursors before redispersing
the NC precipitates in 5 mL of hexane under mild sonication. The obtained
NC dispersions were further centrifuged at 2000 rpm to remove large
NCs. Thus, the obtained CsPbBr3 NCs solution is ready to
undergo an anion-exchange process to prepare the CsPbBrxI3-x NCs.
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3

Particle Size Characterization by FPIA and DLS

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Particle size distribution was determined by Flow Particles Image Analyzer (FPIA), using a Sysmex FPIA 3000 particle size and shape analyser (Malvern Panalytical, Malvern, UK) and by dynamic light scattering (DLS), using a Zetasizer Nano ZS (Malvern Instruments, Malvern, UK). For FPIA analysis, a sample dispersion of 0.5 mg/ml in Milli-Q water was prepared and probe sonicated on ice for 3 min at 30% amplitude, power 25 W, energy delivered into the sample 0.450 kJ/ml, using a Sonopuls HD3100 homogeniser (Bandelin, Berlin, Germany). For DLS analysis, a sample dispersion in Roswell Park Memorial Institute (RPMI) 1640 medium (0.5 mg/ml), with the addition of 10% foetal bovine serum (FBS), was prepared and sonicated as described.
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4

Nanoparticle Size Characterization by DLS and SLS

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The size distribution of the
prepared magnetic nanoparticles (IONs) was evaluated by dynamic light
scattering (DLS), using a Zetasizer Nano-ZS (Malvern Instruments,
UK). Before the measurement, 10 μL of the sample was added to
2 mL of deionized water, filtered by a 0.2 μm PVD filter, and
placed into a disposable cuvette. The size distribution of GPs, mGPs,
and mGPs-RhodB was evaluated by the static light scattering method
using the Horiba Partica LA 950/S2 instrument. Prior to the measurement,
the particle suspension was sonicated by Sonopuls HD 3100 (Bandelin
Electronic) for 5 min at 25 W without pulses.
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5

Optimization of Ginkgo Bioactive Compound Extraction

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Preliminary studies were conducted to assess the efficacy of different solvents and extraction methods in the extraction of GAs. First, the sample and solvent (in a ratio of 1:20, w/v, g/mL) were homogenized by vortexing for 1 min at 3000 rpm (Rx3 Velp Scientifica, Usmate, MB, Italy). Then, for conventional SLE, the mixtures were subjected to agitation for 5, 10, 15, and 20 min with a magnetic stirrer (IKA RCT basic, Staufen, Germany). On the other hand, for UAE, the mixtures were sonicated with a Sonopuls HD 3100 ultrasonic homogenizer (100 W, 60 kHz, Bandelin, Berlin, Germany) equipped with an MS 73 titanium probe (13 mm diameter). The UAE employed an amplitude of 75% in pulsed mode (pulse durations of 0.1 s “on” and 0.2 s “off”) for 5, 10, 15, and 20 min. These experiments were carried out at ambient temperature (around 23 °C) and were performed in triplicate.
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6

Optimization of Cumin Essential Oil Nanoemulsions

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Cuminum cyminum L. essential oil nanoemulsions was prepared using the methods described by Gahruie et al. (2017 (link)) and Chu et al. (2020 ) at ambient temperature (approximately 22°C). CEO (disperse phase) and deionized water (continuous phase) were used to make CEON. First, tween 80 (7.5% v/v) was stirred in deionized water at room temperature (800 rpm, 30 min), and then CEO (7.5% v/v) was added. The obtained mixture was homogenized at 12,000 rpm for 4 min using a laboratory stirrer (OS20‐Pro, Dragon, China). Then, the coarse emulsion was exposed to ultrasonic for 10 min using a homogenizer in ultrasonic (probe) technology (BANDELIN SONOPULS HD 3100, BANDELIN, Germany) with a 30% power output of 225 W and 25 kHz.
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7

Sonication-Assisted Vinyldecanoate Synthesis

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Samples of 10 mL DES containing 0.5 M vinyldecanoate were sonicated for 5 min with 60% amplitude and a cycle of 20 s pulsing and 30 s pause in 50 mL tubes. A Sonopuls HD 3100 ultrasonic homogenizer from Bandelin (Berlin, Germany) equipped with a MS 72 probe was used at a frequency of 20 kHz (with an energy input of 4.654 kJ). The probe was set to an immersion depth of 1.5 cm. During sonication, the samples were cooled in a water bath after which they were immediately used for synthesis.
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8

Recombinant Protein Expression in E. coli

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The synthesis of R.Gva14018I-4 and R.Gva14018I-8 in E. coli Tuner (DE3), ER2566, and ArcticExpress (DE3) was induced with 0.1 mM IPTG, and then cells were cultivated for 2.5 h at 37 °C, 4 h at 25 °C, or 22–24 h at 12–16 °C, respectively. The cells were harvested and disrupted via sonication (Bandelin Sonopuls HD 3100, Bandelin Electronic, Germany). The soluble fraction was separated, and proteins were purified using the His-Spin Protein Miniprep kit (Zymo Research, Irvine, CA, USA). The insoluble fraction was resuspended in PBS containing 2% SDS and incubated for 10 min at 100 °C. The samples were analyzed by 12% SDS-PAGE under reducing conditions.
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9

Physicochemical Characterization of hBNs

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The hBNs were dispersed in double distilled water (ddH2O) by sonication for 2 min at before the analysis (Bandelin Sonopuls HD 3100). A Perkin Elmer Lambda 25 UV-Vis spectrometer was used to obtain absorption spectra. IR spectra were acquired with a Thermo NICOLET IS50 Spectrometer. XRD analysis was performed using a Shimadzu XRD-6000 with a ICDD PDF 4 software. The scanning area was in continuous mode with a scanning range of 2.000–69.980° and a scanning speed of 2.0000°/min. The sampling pitch was set to 0.0200°, and the preset time was set to 0.60 s. Raman spectra of the hBNs were recorded using a Renishaw In Via Reflex Raman Microscopy system (Renishaw Plc., New Mills, Wotton-under-Edge, UK) equipped with a 514 nm Argon ion laser. A minimum of 16 spectra was acquired from a 16-μm2 hBNs sample area. All measurements were performed at least three times.
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10

Preparation of Bioink from Decellularized ECM

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To prepare bioink B, an appropriate amount of dECM was suspended in the PBS×1 solution. The falcon with the suspension was placed in an ice bath, taking care not to shake the suspension. Then, the hydrogel sonication process began. A sonicator, Bandelin Sonopuls HD 3100 (Bandelin electronic GmbH & Co. KG, Berlin, Germany), and a TS 103 sonotrode were used, the amplitude was set to 60%, the sonication time was 5 min, with the process interrupted every 30 s to wait until the temperature dropped to 22 °C. The prepared hydrogel was tightly closed and placed in the refrigerator. Before use in further stages, the falcon with hydrogel was heated in a thermoblock at 37 °C with stirring at 800 rpm; this was to liquefy and de-aerate the hydrogel.
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