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Supra 25k

Manufactured by Hanil

The Supra 25K is a lab equipment product designed for use in research and scientific applications. It features a core function of high-speed centrifugation, capable of reaching up to 25,000 revolutions per minute. The product specifications and technical details are available upon request.

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6 protocols using supra 25k

1

Porcine Blood Plasma Protein Isolation

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Whole porcine blood was freshly obtained immediately after slaughter and
immediately used for plasma preparation. Ethylenediaminetetraacetic acid was
added as anticoagulation agent to fresh porcine blood at 2 g/L and mixed well.
Blood was immediately placed in ice slash and brought back to the laboratory
within 30 min. Samples were centrifuged (Supra 25K, Hanil Science Industrial
Co., Ltd., Incheon, Korea) at 8,000×g for 15 min at 4℃ for plasma
separation. Globulin and albumin proteins were isolated from the separated
plasma using a modified cold ethanol method (Cohn
et al., 1946
).
For the separation of globulin and albumin proteins from the plasma, the plasma
separated by centrifugation was cooled in an ice water bath. Cold ethanol was
then added to the plasma at a final concentration of 7.4%. Next,
centrifugation was performed at 10,000×g for 20 min to remove fibrinogen
and antihemophilic factor. After that, ethanol was added to the supernatant at a
final concentration of 24% and centrifugation was carried out again under
the same conditions (10,000×g for 20 min). The resulting precipitate
(globulin) was stored at 15℃. Ethanol was added to the separated
supernatant at a final concentration of 60%. The precipitate (albumin)
obtained after centrifugation was stored at 15℃.
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2

Doxorubicin-Loaded PCL Nanocapsules: Synthesis

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Dox-PCL nanocapsules were produced by modified double emulsion technique (W/O/W) as described by [33 (link)]. Briefly, 1.5 ml Dox solution (2 mg/ml) were emulsified with 10 mg PCL dissolved in 8 ml DCM using a high speed homogenizer (Tekmar, UK) for 3 min at 5000 rpm to create the first emulsion phase of water-in-oil (W1/O). Then, the first emulsion is transferred to an aqueous solution containing 35 ml 2% PVA and 5 ml 0.5% PEG and are homogenized for 5 min at 8000 rpm to form the second emulsion phase (W1/O/W2). The resulting mixture was left stirred on a magnetic stirrer (C-MAG HS 7, IKA, China) overnight at room temperature, in the dark. After evaporation of DCM, the remaining solution was centrifuged using an ultracentrifuge (supra25K, Hanil science industrial, Korea) for 1 h at 13,000 rpm and 10 C. Finally, the supernatant was decanted and stored to be used later on (“Evaluation of Dox encapsulation efficiency and drug loading” section) and the pellet was resuspended in 2 ml deionized H2O and directly fed into the freeze dryer (Edwards Modulyo, UK) to produce a dried powder of Dox- PCL nanocapsules, which was then collected and kept at 4 °C.
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3

Exfoliation and Dispersion of 2D Materials

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For sample preparation, we purchased graphite and MoSe2 powders from Alfa Aesar. h-BN powder was purchased from Momentive. MoS2 and WS2 were purchased from Sigma Aldrich.
To exfoliate and disperse 2D materials in water from the source powders, we used a bath sonicator, manufactured by Onejon Ultrasonic in Korea. Each material (20 mg) was sonicated in deionized water (200 ml) for 60 h. The operation power was 20 W and frequency was 40 kHz. In addition, the cooling water circulation equipment was built in the sonicator to control the sonication bath temperature. The resulting solution was centrifuged at 600 relative centrifugal force for 30 min using a high speed centrifuge (Supra 25K, HANIL SCIENCE INDUSTRIAL). The final solution was kept either in an atmospheric condition (20 °C) or in an oven (60 °C).
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4

Isolation and Hydrolysis of Cattle Plasma Proteins

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To prepare plasma proteins (PP), from cattle blood plasma, 0.5 N ethylenediaminetetraacetic acid (EDTA) as an anticoagulated was added to fresh cattle blood at a ratio 1:9 (v/v), mixed well, and placed immediately on ice for 30 min. Samples were centrifuged by a refrigeration centrifuge (SUPRA 25 K, Hanil Science, Korea) at 14,000 g for 15 min at 4 °C. The plasma powders were freeze-dried (Clean van 8B Freeze-Dryer, BioTron, Inc., Korea), pulverized, placed in sealed bags, and stored at 4 °C.
To prepare plasma protein hydrolysate (PPH), PP solution [5 % w/v 10 mM sodium phosphate buffer (pH 7.0)] was heat-pretreated (90 °C, 5 min) and then hydrolyzed with Alcalase. The enzyme to substrate ratio (E/S) was 2:100 (g/g). The pH of PP solution was adjusted to the optimal value for Alcalase (pH 8.32) before hydrolysis and was readjusted to the optimal value with 1 M NaOH every 15 min during hydrolysis. Hydrolysates were produced by varying the hydrolyzed time to 338 min and hydrolyzed temperature 54 °C. After hydrolysis, the pH of the solution was brought to 7.0 and the solution was then heated at 95 °C for 5 min to inactivate the enzyme. Degree hydrolysis (DH) was determined by assaying free amino groups with 2, 4, 6-trinitrobenzenesulfonic acid (TNBS) according to Alder-Nissen [16 ]. The DH of hydrolyzed PP was 18.8 %.
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5

Measuring Protein Decomposition in Cheese

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In order to measure the total protein decomposition level during cheese ripening, change in WSN was measured according to the method described in Bütikofer [12 (link)].
The sample used for measurement of the change in WSN was homogenized and centrifuged (Supra 25 K, Hanil Science Industrial, Korea) as described in the pH measurement section, and the filtrate (Whatman No.2) was then colored using the method described in Hull [13 (link)]. Next, the content of WSN was measured at 570 nm using a UV- Spectrophotometer (Smart Plus Spectrophotometer Co., Korea). The content of a nitrogenous compound was calculated according to a linear regression equation obtained by making tyrosine the standard substance.
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6

Extraction and Characterization of C-Phycocyanin

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Spirulina tablets cultured from lava seawater were donated by KIOST (Gyeonggi-do, Korea). Piperazine, sodium chloride, and C-PC (spirulina sp.) were purchased from Sigma Aldrich (USA).
Tris(hydroxymethyl)aminomethane (Tris), ethylenediaminetetraacetic acid (EDTA), disodium salt dihydrate, and sucrose were purchased from USB Corporation (USA). Ammonium sulfate and hydrochloric acid were purchased from DaeJung Chemical Co. (South Korea) and Samchun Chemical Co.
(South Korea), respectively. The following methodologies and relevant kits were used in this study: centrifugation (Supra 25K, Hanil, South Korea); anion exchange chromatography (HiTrap Q HP, GE Healthcare, USA); dialysis (MEMBRA-CEL MC18 X 100 CLR; Serva, Germany); AKTA start puri cation system with Frac30 fraction collector (GE Healthcare, USA); spectroscopy with a microplate reader, equipped with a 50 W xenon ash lamp (Varioskan LUX, Thermo Scienti c, USA); RNeasy Mini kit plus (Takara Bio, Japan); QuantiFasT Reverse Transcription kit (Qiagen, Germany); Rotor-Gene Q PCR (Qiagen, Germany); ultra-centrifugation (Vivaspin 500, MWCO 10000, Sartorius Germany)
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