The determination of sausage emulsion stability was performed as described by Mohamed et al. [20 (link)]. A sample of about 30 g was weighed and placed in a 50 mL centrifuge disposal tube and centrifuged at a speed of 2,800 × g at 4°C for 15 minutes with a high-speed refrigerated microcentrifuge (Tomy Mx-305), to remove air bubbles. The tube was then heated at 70°C for 30 minutes in a water bath (Memmert W350, Germany) and allowed to stay at room temperature. The tube was centrifuged again at a speed of 2,800 × g at 4°C for 15 minutes. The supernatant (S) contained in the tube was poured into a porcelain crucible. The released supernatant was weighed (RS) and dried in an oven (Shimadzu) at 105°C for 16 hours, to obtain the volume of released water (RW). The porcelain crucible was weighed again to determine the weight of fat released (FR). The percentage of fat released (FR) was determined as the difference between the percentages of S and RW.
Mx 305
Manufactured by TOMY
Sourced in Japan
The MX-305 is a laboratory centrifuge designed for general-purpose applications. It features a compact and durable construction, accommodating a range of sample sizes and speeds. The MX-305 provides a reliable and consistent performance for routine centrifugation tasks in research and diagnostic settings.
Automatically generated - may contain errors
Lab products found in correlation
Centrifugal concentrator, by Thermo Fisher Scientific (1 mentions)
High performance liquid chromatography (hplc), by Shimadzu (1 mentions)
Lysozyme, by Fujifilm (1 mentions)
Sodium phytate, by Merck Group (1 mentions)
13hp020an, by Advantec (1 mentions)
Spd m10a, by Shimadzu (1 mentions)
S 5000, by Hitachi (1 mentions)
7 protocols using mx 305
1
Sausage Emulsion Stability Determination
2
Metabolite Extraction and Purification for LC-MS
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Each sample (10 mg DW) was extracted using a vortex with 500 µL of methanol containing 8 μM of two reference compounds (methionine sulfone for the cation and camphor 10-sulfonic acid for the anion analyses), 500 μL of chloroform, and 200 μL of water. The extracted solution was centrifuged at 15,000 g for 3 min at 4 °C (MX-305, TOMY, Tokyo, Japan). The upper layer was evaporated for 30 min at 45 °C by a centrifugal concentrator (Thermo Fisher Scientific K.K., Tokyo, Japan) to obtain two layers. For removing high-molecular-weight compounds, such as oligo-sugars, the upper layer was centrifugally filtered through a PALL Nanosep 3-kDa cutoff filter at 9100 g for 90 min at 4 °C. The filtrate was dried for 120 min by a centrifugal concentrator. The residue was dissolved into 20 μL of water containing 200 μM of internal standards (3-aminopyrrolidine for cation and trimesic acid for anion analyses) that were used for the compensation of migration time in the peak annotation step.
3
Dopamine Quantification in Striatum
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0.2 M HClO4 containing 100 M EDTA disodium salt was used to homogenise a portion of the striatum (20% w/v) for determining dopamine concentration. For 30 min, the homogenate was allowed to deproteinize. The homogenate was then centrifuged for 15 min at 10,000 rpm at 0°C (MX-305, Tomy, Japan). The pH of the supernatant was adjusted with 1 M acetic acid to pH = 3.5 and 0.45 µm membrane filter was used for filtration (Millipore, United States). The reversed–phase HPLC analytical method explained by Arsene AL and co-workers for the determination of dopamine was adopted with some modifications (Arsene et al., 2009 ). Briefly, 5 µm RP 18 (C18) column, Lichrospher®100 (250 mm × 4.6 mm) attached to an HPLC (Shimadzu) equipped with variable wavelength programmable UV/VIS detector, and a Rheodyne injector with a 20 µL loop was used. For the drug analysis class-VP 5.032 software was used. 0.8 mM EDTA disodium salt, 0.65 g sodium heptane sulphonate, 0.12 M sodium dihydrogen phosphate, and 65% methanol was used as mobile phase. Amount of Dopamine was determined at 210 nm using UV detector. HPLC results were expressed as ng/mg protein after adjusting to total tissue proteins.
4
Plasmid DNA Isolation Protocol
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Plasmid DNA was prepared by following the alkaline lysis method (A. Shishir et al. 2014 (link)). Pellet of a 5.0 ml overnight culture grown in LB broth at 30 °C and 120 rpm was lysed with 0.85 ml of lysis solution containing TE buffer (50 mM Tris, 20 mM EDTA; pH 8.5) and lysozyme (2 mg/ml) (Wako, Japan). Then 0.05 ml of 20% SDS solution and 5U proteinase-K (Nacalai tesque, inc. Japan) were added.
Subsequently, 0.03 ml of 3.0 N NaOH was added and mixed gently for 3 min followed by neutralization with 0.06 ml of 2 M Tris-HCl (pH 7.0). Afterward, 0.1 ml of 5.0 M NaCl was added to the suspension and placed on ice for 15 min and centrifuged with 12,000 × g at 4 °C for 15 min (Tomy, MX-305, High-Speed Refrigerated Micro Centrifuge, Japan). The supernatant was then transferred into a fresh microfuge tube and a double volume of ice-cold ethanol was added and incubated at -20 °C for 15 minutes. Afterward, the mixture was centrifuged at 12,000 × g for 15 min and the pellet was air-dried and re-suspended in 50 µl of TE buffer (10 mM Tris, 1 mM EDTA) and preserved at -20 °C after visualization through agarose gel electrophoresis (Promega, USA) (Trevors 1984) (link).
Subsequently, 0.03 ml of 3.0 N NaOH was added and mixed gently for 3 min followed by neutralization with 0.06 ml of 2 M Tris-HCl (pH 7.0). Afterward, 0.1 ml of 5.0 M NaCl was added to the suspension and placed on ice for 15 min and centrifuged with 12,000 × g at 4 °C for 15 min (Tomy, MX-305, High-Speed Refrigerated Micro Centrifuge, Japan). The supernatant was then transferred into a fresh microfuge tube and a double volume of ice-cold ethanol was added and incubated at -20 °C for 15 minutes. Afterward, the mixture was centrifuged at 12,000 × g for 15 min and the pellet was air-dried and re-suspended in 50 µl of TE buffer (10 mM Tris, 1 mM EDTA) and preserved at -20 °C after visualization through agarose gel electrophoresis (Promega, USA) (Trevors 1984) (link).
5
Phytase Activity Determination Protocol
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Phytase activity was determined based on Azeka et al. [24 (link)] and Ou et al. [29 (link)] with modification. Unless stated otherwise, all chemicals were obtained from Nacalai tesque (Kyoto, Japan). One grain was homogenized with 1 mL of 0.5 M sodium acetate buffer, then centrifuged at 15,300× g for 10 min at 4 °C. The supernatant was collected for enzyme activity assay. Sodium acetate buffer and 0.1 g/L sodium phytate (Sigma-Aldrich, St. Louis, MO, USA) were added into a 1.5 μL tube and mixed. The enzyme reaction was initiated by adding crude enzyme into the mixed buffer solution. After incubation, enzyme reaction was terminated with trichloroacetic acid (50% w/v) and centrifuged using high speed refrigerated micro centrifuge (MX-305, Tomy, Tokyo, Japan) at 15,300× g for 10 min at 4 °C. Enzymatic reaction was measured at 50 °C and at soaking temperature of the sample as above. Pi concentration was measured at 655 nm after adding a colour reagent containing ascorbic acid (10% w/v), concentrated H2SO4, and ammonium molybdate (5% w/v). Mixed buffer solution without crude enzyme was used as a blank. To determine the Pi concentration, calibration curves were prepared with 0.03 M KH2PO4. Enzyme activity (U) was expressed as 1 μmol of Pi released from IP6 per minute. Total protein contents were measured using the same extract following the Bradford method [30 (link)].
6
Quantification of Camptothecin in Plant Organs
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The leaf, stem, and root were frozen in liquid nitrogen and stored at -30 °C in a deep freezer until analysis. They were disrupted using a multi-beads shocker (MB-601U, Yasui Kikai Corporation, Japan), and MeOH (1 mL) was added per 100 mg of powdered sample. The mixture was sonicated for 15 min using an ultrasonic washer and stored overnight at 4 °C. On the next day, the extracted sample was centrifuged at 10,000 × g for 10 min (MX-305, Tomy Seiko Co., Ltd., Japan). The supernatant was filtered through a syringe filter (13HP020AN, Advantec, Japan) and analyzed by high-performance liquid chromatography (HPLC) (10AD, Shimadzu Corporation, Japan). A TSK gel ODS-100V column (Tosoh, Japan; 4.6 × 250 mm, 5 mm) was used with a solvent system of acetonitrile: water: formic acid (30:69.9:0.1, v/v). The flow rate of the mobile phase in the column was 1.0 mL min -1 for 25 min, and the injection volume was 10 μL per each sample. The column temperature was set at 40 °C. The chromatogram was monitored at 370 nm on an ultraviolet-visible photodiode array detector (SPD-M10A, Shimadzu Corporation, Japan). The CPT (Sigma-Aldrich, USA) was used as a standard material. The CPT content was calculated using the CPT concentration and dry weight of each organ.
7
Characterization of Cellulose Nanofibers
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and -ChNFs (0.1 w/v%) were diluted with tert-butyl alcohol and precipitated with a centrifuge (MX-305, TOMY SEIKO Co., Ltd., Tokyo, Japan) at 20,000 ×g. After repeating this process several times, the solvent of the supernatant was changed from water to tert-butyl alcohol. The precipitated sample was frozen in a frozen glass bottle and dried under 0.02 MPa vacuum conditions for a few hours. The dried and -ChNFs were coated with an ~2 nm thick osmium layer using an osmium coater (Neoc-STP, Meiwafosis Co., Ltd., Tokyo, Japan).
The sample was observed by a field-emission scanning electron microscope (S-5000, HITACHI Co., Ltd., Tokyo, Japan) operated at 5.0 kV. A histogram of the and -ChNF widths was constructed from four field-emission scanning electron microscopy (FE-SEM) images (number of NF widths ≈ 170) with Image-J (NIH, Bethesda, USA) [28] .
The sample was observed by a field-emission scanning electron microscope (S-5000, HITACHI Co., Ltd., Tokyo, Japan) operated at 5.0 kV. A histogram of the and -ChNF widths was constructed from four field-emission scanning electron microscopy (FE-SEM) images (number of NF widths ≈ 170) with Image-J (NIH, Bethesda, USA) [28] .
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