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Freeze Drying

Freeze Drying is a process that removes water from a substance through the application of low temperature and reduced pressure, allowing the water to sublime directly from the solid to the gas phase.
This technique preserves the structure and composition of the original material and is commonly used in the pharmaceutical, food, and biotechnology industries to stabilize and extend the shelf-life of heat-sensitive products.
The PubCompare.ai platform leverages AI-driven technology to optimize freeze drying processes, helping researchers and professionals locate the best protocols from literature, pre-prints, and patents using intelligent comparisons.
This powerful tool enhances reproducibility and research accracy, allowing users to experience the future of freeze drying optimization today.

Most cited protocols related to «Freeze Drying»

1
Mitochondrial Respiratory Kinetics Assay
Cited 26 times
High-resolution O2 consumption measurements were conducted in 2 mL of buffer Z using the OROBOROS Oxygraph-2k (OROBOROS INSTRUMENTS, Corp., Innsbruck, AT) with stirring at 750 rpm. Buffer Z contained 20 mM creatine hydrate to saturate creatine kinase, which facilitates mitochondrial ADP transport [4 (link), 10 (link), 23 (link)-25 (link)], with the exception of specific experiments on human PmFBs which were conducted in the presence of 24 mM phosphocreatine and 12 mM creatine hydrate (described below). 5 mM pyruvate and 2 mM malate were added as complex I substrates. ADP was titrated in step-wise increments and all experiments were completed before oxygraph chamber [O2] reached 150 μM. At the conclusion of each experiment, PmFBs were washed in double-distilled H2O to remove salts, frozen at -20°C, and dried via lyophilization (Labconco Corp., Kansas City, MO). Polarographic oxygen measurements were acquired in 2-second intervals, with the rate of respiration derived from 40 data points, and expressed as pmol • s-1 • mg-1 dry weight. Dry and wet bundle weights were consistently between 0.2 - 0.6 mg and ∼1.0 to 2.5 mg, respectively. Cytochrome c was added to test for mitochondrial membrane integrity as partial loss of cytochrome c during sample preparation may limit active respiration. A cytochrome c response was dectected in <5% of all experiments and no response generated >10% increase in respiration. No relationship was observed between the relative cytochrome c response and Km when grouping all human and rodent data (R2 = 0.013, p>0.05). Additionally, no significant relationship was observed in humans when using a paired t-test to compare the Km for those experiments showing 0-5% cytochrome c response relative to those few samples exhibiting a 5-10% cytochrome c response. Four PmFBs from each rat or human were run simultaneously in four separate oxygraph chambers. Two of the chambers contained either 100 μM BTS or 25 μM BLEB. A third chamber contained 1.25% DMSO (vehicle, +V) to match the content of DMSO added in the BTS and BLEB conditions with the remaining chamber serving as the control (minus vehicle) condition.
The Km for ADP was determined through the Michaelis-Menten enzyme kinetics - fitting model (Y = Vmax*X/(Km + X)), where X = [free ADP; ADPf] and Y = JO2 at [ADPf], using Prism (GraphPad Software, Inc., La Jolla, CA). This equation was also used to calculate the fraction of maximal mitochondrial respiration in resting human skeletal muscle in vivo. This calculation was performed using the experimentally determined Km values assuming resting [ADPf] to be ∼14.6 μM in human skeletal muscle [6 (link)].
Perry C.G., Kane D.A., Lin C.T., Kozy R., Cathey B.L., Lark D.S., Kane C.L., Brophy P.M., Gavin T.P., Anderson E.J, & Neufer P.D. (2011). Inhibiting Myosin-ATPase Reveals Dynamic Range of Mitochondrial Respiratory Control in Skeletal Muscle. The Biochemical journal, 437(2), 10.1042/BJ20110366.
Publication 2011
Buffers Cell Respiration Creatine Creatine Kinase cytochrome c'' Enzymes Freeze Drying Freezing Homo sapiens Kinetics malate Mitochondria Mitochondrial Membranes NADH Dehydrogenase Complex 1 Oxygen Phosphocreatine Polarography prisma Pyruvates Respiratory Rate Rodent Salts Skeletal Muscles Sulfoxide, Dimethyl
2
Fabrication of Anisotropic Collagen-Chondroitin Scaffolds
Cited 18 times

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Publication 2011
Acetic Acids Aluminum Anisotropy ARID1A protein, human Bos taurus Carbodiimides Collagen Type I Copper Dermis Ethanol Freeze Drying Fungus, Filamentous Molar N-hydroxysulfosuccinimide Phosphates Polytetrafluoroethylene Saline Solution shark cartilage extract Sulfates, Chondroitin Vacuum
3
Preparation of Amyloid-β Peptide
Cited 14 times
Synthetic human Aβ42 peptide was prepared in two separate ways. Firstly the Aβ42 lyophilised powder was dissolved in TFA and dried under a nitrogen stream. The remaining film was dissolved in 100% HFIP to a concentration of 1 mg/ml, sonicated 5 min in a bath sonicator and dried under a nitrogen stream. The HFIP treatment was repeated twice more and on final dissolving the peptide was dispensed into microcentrifuge tubes. After drying under a nitrogen stream, the peptide was further dried under vacuum for 1–2 h to give a clear film.
The second method was to take the original peptide and dissolve it in 10% (w/v) NH4OH at 0.5 mg/ml. The peptide was incubated for 10 min at room temperature followed by sonication (5 min) and then dispensed (0.5 ml) into microfuge tubes. The NH4OH was removed by lyophilisation to yield a salt free fluffy white peptide. All aliquots from both methods were then stored at −80°C. Immediately prior to use, the HFIP- and NH4OH-treated and untreated Aβ42 were dissolved in 60 mM NaOH and the concentration determined by absorbance at 214 and 280 nm using extinction coefficients of 76848 M-1 cm-1 or 1490 M-1 cm-1, respectively. In all cases the resuspended peptide was analysed by mass spectrometry and the peptide found to be unmodified with no trace of HFIP or NH4OH.
Ryan T.M., Caine J., Mertens H.D., Kirby N., Nigro J., Breheney K., Waddington L.J., Streltsov V.A., Curtain C., Masters C.L, & Roberts B.R. (2013). Ammonium hydroxide treatment of Aβ produces an aggregate free solution suitable for biophysical and cell culture characterization. PeerJ, 1, e73.
Publication 2013
Bath Extinction, Psychological Freeze Drying Homo sapiens Mass Spectrometry Nitrogen Peptides Powder seryl-alanyl-leucy-leucyl-arginyl-seryl-isoleucyl-prolyl-alanine Vacuum
4
Preparation and Characterization of Amyloid-beta Peptide Aggregates
Cited 13 times
Fibril and soluble oligomer samples were prepared by first dissolving purified Aβ42 peptides in 1,1,1,3,3,3-hexafluoro-2-propanol, flash freezing in liquid nitrogen, and then lyophilizing to completely remove the solvent. Lyophilized Aβ42 peptides were dissolved in a small volume of 100 mM NaOH at a concentration of 10 mg Aβ42 per ml NaOH, and then brought up in either low salt buffer (10 mM phosphate buffer, 10 mM NaCl, pH 7.4) for oligomer studies or in physiological salt buffer (10 mM phosphate, 150 mM NaCl, pH 7.4) for fibril studies. All samples were titrated to pH 7.4 and filtered with 0.2-micron filters prior to incubation. Oligomer samples were kept at 4 °C for up to 6 h and analyzed by EM, AFM, and immunoblot analysis or flash frozen and lyophilized for solid-state NMR studies. Fibril samples were incubated at 37 °C with gentle agitation for 12 days and then analyzed by EM or pelleted, washed and lyophilized for solid-state NMR studies. Previous studies show that lyophilization of Aβ40 does not appreciably perturb the structure of hydrated oligomers and fibrils 19 (link),36 (link). A final concentration of 200 μM Aβ42 peptide was used for all samples.
Ahmed M., Davis J., Aucoin D., Sato T., Ahuja S., Aimoto S., Elliott J.I., Van Nostrand W.E, & Smith S.O. (2010). Structural conversion of neurotoxic amyloid-β(1–42) oligomers to fibrils. Nature structural & molecular biology, 17(5), 561-567.
Publication 2010
Buffers Freeze Drying Freezing hexafluoroisopropanol Immunoblotting Nitrogen Peptides Phosphates physiology Sodium Chloride Solvents Strains
5
Purification and Preparation of Collagen
Cited 13 times

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Publication 2010
Acetic Acid Collagen Freeze Drying Neoplasm Metastasis Tail Tendons

Most recents protocols related to «Freeze Drying»

1
Synthesis of High-Conductivity Entropy-Stabilized Nanometal Oxide
Not available on PMC !

Example 1

Provided is a preparation method for an A-site high-entropy nanometer metal oxide (Gd0.4Er0.3La0.4Nd0.5Y0.4)(Zr0.7, Sn0.8, V0.5)O7 with high conductivity, the method including the following steps.

    • (1) Gd(NO3)3, Er(NO3)3, La(NO3)3, Nd(NO3)3, Y(NO3)3, ZrOSO4, SnC14 and NH4VO3 were taken at a molar ratio of 0.4:0.3:0.4:0.5:0.4:0.7:0.8:0.5, added to a mixed solution of deionized water/absolute ethyl alcohol/tetrahydrofuran at a mass ratio of 0.3:3:0.5, and stirred for five minutes to obtain a mixed liquid I. The ratio of the total mass of Gd(NO3)3, Er(NO3)3, La(NO3)3, Nd(NO3)3, Y(NO3)3, ZrOSO4, SnC14 and NH4VO3 to that of the mixed solution of deionized water/absolute ethyl alcohol/tetrahydrofuran (0.3:3:0.5) is 12.6%.
    • (2) Para-phenylene diamine, hydrogenated tallowamine, sorbitol and carbamyl ethyl acetate at a mass ratio of 1:0.2:7:0.01 were taken, added to propyl alcohol, and stirred for one hour to obtain a mixed liquid II. The ratio of the total mass of the para-phenylene diamine, the hydrogenated tallowamine, the sorbitol and the carbamyl ethyl acetate to that of the propyl alcohol is 7.5%;
    • (3) The mixed liquid I obtained in step (1) was heated to 50° C., and the mixed liquid II obtained in step (2) was dripped at the speed of one drop per second, into the mixed liquid I obtained in step (1) with stirring and ultrasound, and heated to the temperature of 85° C. after the dripping is completed and the temperature was maintained for three hours while stopping stirring, and the temperature was decreased to the room temperature, so as to obtain a mixed liquid III. The mass ratio of the mixed liquid I to the mixed liquid II is 10:4.
    • (4) The mixed liquid III was added to an electrolytic cell with using a platinum electrode as an electrode and applying a voltage of 3 V to two ends of the electrode, and reacting for 13 minutes, to obtain a mixed liquid IV.
    • (5) The mixed liquid IV obtained in step (4) was heated with stirring, another mixed liquid II was taken and dripped into the mixed liquid IV obtained in step (4) at the speed of one drop per second. The mass ratio of the mixed liquid II to the mixed liquid IV is 1.05:1.25; and after the dripping is completed, the temperature was decreased to the room temperature under stirring, so as to obtain a mixed liquid V.
    • (6) A high-speed shearing treatment was performed on the mixed liquid V obtained in step (5) by using a high-speed shear mulser at the speed of 20000 revolutions per minute for one hour, so as to obtain a mixed liquid VI.
    • (7) Lyophilization treatment was performed on the mixed liquid VI to obtain a mixture I;
    • (8) The mixture I obtained in step (7) and absolute ethyl alcohol were mixed at a mass ratio of 1:2 and uniformly stirred, and were sealed at a temperature of 210° C. for performing solvent thermal treatment for 18 hours. The reaction was cooled to the room temperature, the obtained powder was collected by centrifugation, washed with deionized water and absolute ethyl alcohol eight times respectively, and dried to obtain a powder I.
    • (9) The powder I obtained in step (8) and ammonium persulfate was uniformly mixed at a mass ratio of 10:1, and sealed and heated to 165° C. The temperature was maintained for 13 hours. The reaction was cooled to the room temperature, the obtained mixed powder was washed with deionized water ten times, and dried to obtain a powder II.
    • (10) The powder II obtained in step (4) was placed into a crucible, heated to a temperature of 1500° C. at a speed of 3° C. per minute. The temperature was maintained for 7 hours. The reaction was cooled to the room temperature, to obtain an A-site high-entropy nanometer metal oxide (Gd0.4Er0.3La0.4Nd0.5Y0.4)(Zr0.7, Sn0.8, V0.5)O7 with high conductivity.

As observed via an electron microscope, the obtained A-site high-entropy nanometer metal oxide with high conductivity is a powder, and has microstructure of a square namometer sheet with a side length of about 4 nm and a thickness of about 1 nm.

The product powder was taken and compressed by using a powder sheeter at a pressure of 550 MPa into a sheet. Conductivity of the sheet is measured by using the four-probe method, and the conductivity of the product is 2.1×108 S/m.

A commercially available ITO (indium tin oxide) powder is taken and compressed by using a powder sheeter at a pressure of 550 MPa into a sheet, and the conductivity of the sheet is measured by using the four-probe method.

As measured, the conductivity of the commercially available ITO (indium tin oxide) is 1.6×106 S/m.

US11866343B2. A-site high-entropy nanometer metal oxide with high conductivity, and preparation method thereof (2024-01-09). Zhejiang University [CN]. Inventors: Lingjie Zhang [CN], Weiwei Cai [CN], Ningzhong Bao [CN].
Patent 2024
1-Propanol 4-phenylenediamine Absolute Alcohol ammonium peroxydisulfate Cells Centrifugation Electric Conductivity Electrolytes Electron Microscopy Entropy Ethanol ethyl acetate Freeze Drying indium tin oxide Metals Molar Oxides Platinum Powder Pressure propyl acetate Solvents Sorbitol tetrahydrofuran Ultrasonography
2
Lyophilized Silk Powder Formulations
Not available on PMC !

Example 19

TABLE 37
Embodiments of lyophilized silk powders
Silk SolutionTreatmentSoluble
~60 kDa silk, 6% silk, pH = 7-8lyopholize and cut withno
blender
~60 kDa silk, 6% silk, pH = 10lyopholize and cut withno
blender
~25 kDa silk, 6% silk, pH = 7-8lyopholize and cut withyes
blender
~25 kDa silk, 6% silk, pH = 10lyopholize and cut withyes
blender

The above silk solutions were transformed to a silk powder through lyophilization to remove bulk water and chopping to small pieces with a blender. pH was adjusted with sodium hydroxide. Low molecular weight silk (−25 kDa) was soluble while high molecular weight silk (−60 kDa) was not.

The lyophilized silk powder can be advantageous for enhanced storage control ranging from 10 days to 10 years depending on storage and shipment conditions. The lyophilized silk powder can also be used as a raw ingredient in the pharmaceutical, medical, consumer, and electronic markets. Additionally, lyophilized silk powder can be re-suspended in water, HFIP, or an organic solution following storage to create silk solutions of varying concentrations, including higher concentration solutions than those produced initially.

In an embodiment, aqueous pure silk fibroin-based protein fragment solutions of the present disclosure comprising 1%, 3%, and 5% silk by weight were each dispensed into a 1.8 L Lyoguard trays, respectively. All 3 trays were placed in a 12 ft2 lyophilizer and a single run performed. The product was frozen with a shelf temperature of ≤−40° C. and held for 2 hours. The compositions were then lyophilized at a shelf temperature of −20° C., with a 3 hour ramp and held for 20 hours, and subsequently dried at a temperature of 30° C., with a 5 hour ramp and held for about 34 hours. Trays were removed and stored at ambient conditions until further processing. Each of the resultant lyophilized silk fragment compositions were able to dissolve in aqueous solvent and organic solvent to reconstitute silk fragment solutions between 0.1 wt % and 8 wt %. Heating and mixing were not required but were used to accelerate the dissolving rate. All solutions were shelf-stable at ambient conditions.

In an embodiment, an aqueous pure silk fibroin-based protein fragment solution of the present disclosure, fabricated using a method of the present disclosure with a 30 minute boil, has a molecular weight of about 57 kDa, a polydispersity of about 1.6, inorganic and organic residuals of less than 500 ppm, and a light amber color.

In an embodiment, an aqueous pure silk fibroin-based protein fragment solution of the present disclosure, fabricated using a method of the present disclosure with a 60 minute boil, has a molecular weight of about 25 kDa, a polydispersity of about 2.4, inorganic and organic residuals of less than 500 ppm, and a light amber color.

US11878070B2. Silk-based moisturizer compositions and methods thereof (2024-01-23). Evolved By Nature, Inc. [US]. Inventors: Gregory H. Altman [US], Dylan S. Haas [US], Kevin T. Healy [US].
Patent 2024
Amber ARID1A protein, human Dietary Fiber Fibroins Freeze Drying Freezing Furuncles Light Pharmaceutical Preparations Powder Proteins Silk Sodium Hydroxide Solvents
3
Synthesis of Quinolinylated Diazepan Acetate
Not available on PMC !

Example 62

[Figure (not displayed)]

Step 1: tert-butyl 2-(4-(7-chloro-4-(1H-imidazol-1-yl)quinolin-2-yl)-2-oxo-1,4-diazepan-1-yl)acetate. To a solution of 4-(7-chloro-4-(1H-imidazol-1-yl)quinolin-2-yl)-1,4-diazepan-2-one (20 mg) and tert-butyl 2-bromoacetate (30 mg) in anhydrous DMF was added NaH (10 mg, 65% in mineral oil). After stirring 3 hours, the reaction mixture was diluted with EtOAc (10 mL) and carefully quenched with water (5 mL). Isolation of the organic layer and a column chromatography eluting with a gradient of hexanes and EtOAc afforded the desired intermediate tert-butyl 2-(4-(7-chloro-4-(1H-imidazol-1-yl)quinolin-2-yl)-2-oxo-1,4-diazepan-1-yl)acetate (20 mg) (MS: [M+1]+ 456).

Step 2: 2-(4-(7-chloro-4-(1H-imidazol-1-yl)quinolin-2-yl)-2-oxo-1,4-diazepan-1-yl)acetic acid. tert-butyl 2-(4-(7-chloro-4-(1H-imidazol-1-yl)quinolin-2-yl)-2-oxo-1,4-diazepan-1-yl)acetate was further treated with TFA (0.4 mL) in DCM (0.8 mL). Removal of DCM and TFA under reduced pressure and lyophilization afforded the desired product (10 mg)-2-(4-(7-chloro-4-(1H-imidazol-1-yl)quinolin-2-yl)-2-oxo-1,4-diazepan-1-yl)acetic acid (MS: [M+1]+ 400).

US11873291B2. Quinoline cGAS antagonist compounds (2024-01-16). ImmuneSensor Therapeutics, Inc. [US], The Board of Regents of the University of Texas System [US]. Inventors: Jian Qiu [US], Qi Wei [US], Matt Tschantz [US], Heping Shi [US], Youtong Wu [US], Hulling Tan [US], Lijun Sun [US], Chuo Chen [US], Zhijian Chen [US].
Patent 2024
Acetate Acetic Acids Anabolism bromoacetate Chromatography Freeze Drying Hexanes imidazole isolation Oil, Mineral Pressure TERT protein, human
4
Synthesis of Quinoline-Piperazine Derivatives
Not available on PMC !

Example 56

[Figure (not displayed)]

Step 1: 1-(tert-Butyl) 2-methyl 4-(7,8-dichloro-4-(1H-imidazol-1-yl)quinolin-2-yl)piperazine-1,2-dicarboxylate. A solution of 2,7,8-trichloro-4-(1H-imidazol-1-yl) quinoline (120 mg), 1-(tert-butyl) 2-methyl piperazine-1,2-dicarboxylate (230 mg), and DIPEA (0.1 mL) in DMF (0.6 mL) was heated at 90° C. overnight until the starting material was consumed. Aqueous work-up with EtOAc (25 mL)/water (10 mL) and a column chromatography eluting with a gradient of hexanes and EtOAc afforded the title compound (85 mg) (MS: [M+1]+ 506).

Step 2: 4-(7,8-Dichloro-4-(1H-imidazol-1-yl)quinolin-2-yl)piperazine-2-carboxylic acid. To a solution of 1-(tert-butyl) 2-methyl 4-(7,8-dichloro-4-(1H-imidazol-1-yl)quinolin-2-yl)piperazine-1,2-dicarboxylate (85 mg) in dioxane (2 mL) was added 2 N HCl (2 mL). The resultant mixture was heated at 80° C. over 4 hours until the Boc protecting group and the methyl ester were removed. Evaporation under reduced pressure and lyophilization afforded the title compound (80 mg) as a di-HCl salt (MS: [M+1]+392).

US11873291B2. Quinoline cGAS antagonist compounds (2024-01-16). ImmuneSensor Therapeutics, Inc. [US], The Board of Regents of the University of Texas System [US]. Inventors: Jian Qiu [US], Qi Wei [US], Matt Tschantz [US], Heping Shi [US], Youtong Wu [US], Hulling Tan [US], Lijun Sun [US], Chuo Chen [US], Zhijian Chen [US].
Patent 2024
2-methyl piperazine Anabolism Chromatography Dioxanes DIPEA Esters Freeze Drying Hexanes imidazole Piperazine piperazine-2-carboxylic acid Pressure quinoline Sodium Chloride t-butyloxycarbonyl group TERT protein, human
5
Synthesis of Reagent 48 by Coupling Compound 13 and Suberic Acid Bis(N-Hydroxysuccinimide Ester)
Not available on PMC !

Example 18

[Figure (not displayed)]

To a stirred solution of compound 13 (21.8 mg) in anhydrous DMF (500 μL) was added NMM (7.8 μL). This solution was then added dropwise over a period of 20 min to a stirred solution of suberic acid bis(N-hydroxysuccinimide ester) (43.8 mg) in anhydrous DMF (1.5 mL) at room temperature under an argon atmosphere. The reaction mixture was then stirred at room temperature for 20 h before the solution was concentrated in vacuo and purified by reverse phase C18-column chromatography, eluting with buffer A (v/v): water:0.05% trifluoroacetic acid and buffer B (v/v): acetonitrile:0.05% trifluoroacetic acid (90:10 v/v to 0:100 v/v). The organic solvent was removed in vacuo and the aqueous solvent removed by lyophilisation to give reagent 48 as a white solid (15.2 mg). m/z [M+Na]+ (2126, 10%), [M+H]+ (2104, 20%), [M+2Na]2+ (1074, 50%), [M+Na+H]2+ (1063, 50%) [M+2H]2+ (1052, 100%).

US11865183B2. Conjugates and conjugating reagents comprising a linker that includes at least two (−CH2—CH2—O—) units in a ring (2024-01-09). POLYTHERICS LIMITED [GB]. Inventors: Antony Godwin [GB], Andrew Kyle [GB], Nicholas Evans [GB].
Patent 2024
acetonitrile Anabolism Argon Atmosphere auristatin Buffers Chromatography, Reverse-Phase Esters Freeze Drying N-hydroxysuccinimide Solvents suberic acid Trifluoroacetic Acid

Top products related to «Freeze Drying»

1
Alpha 1 2 ld plus by Martin Christ
Sourced in Germany, Switzerland, United Kingdom
The Alpha 1-2 LD plus is a benchtop lyophilizer (freeze dryer) designed for laboratory use. It is capable of processing samples with a loading capacity of up to 6 kg. The unit features a temperature range of -55°C to +60°C and a vacuum range of 0.001 mbar to 1 mbar.
2
Trypsin by Promega
Sourced in United States, Germany, United Kingdom, China, Japan, France, Switzerland, Sweden, Italy, Netherlands, Spain, Canada, Brazil, Australia, Macao
Trypsin is a serine protease enzyme that is commonly used in cell culture and molecular biology applications. It functions by cleaving peptide bonds at the carboxyl side of arginine and lysine residues, which facilitates the dissociation of adherent cells from cell culture surfaces and the digestion of proteins.
3
Zetasizer nano z by Malvern Panalytical
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The Zetasizer Nano ZS is a dynamic light scattering (DLS) instrument designed to measure the size and zeta potential of particles and molecules in a sample. The instrument uses laser light to measure the Brownian motion of the particles, which is then used to calculate their size and zeta potential.
4
Freeze dryer by Labconco
Sourced in United States, Japan, Macao
A freeze dryer is a laboratory equipment used to remove water from materials through the process of lyophilization. It operates by freezing the material and then reducing the surrounding pressure to allow the frozen water in the material to sublime directly from the solid phase to the gas phase.
5
Whatman no 1 filter paper by Cytiva
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Whatman No. 1 filter paper is a general-purpose cellulose-based filter paper used for a variety of laboratory filtration applications. It is designed to provide reliable and consistent filtration performance.
6
S 4800 by Hitachi
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The S-4800 is a high-resolution scanning electron microscope (SEM) manufactured by Hitachi. It provides a range of imaging and analytical capabilities for various applications. The S-4800 utilizes a field emission electron gun to generate high-quality, high-resolution images of samples.
7
Dimethyl sulfoxide (dmso) by Merck Group
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DMSO is a versatile organic solvent commonly used in laboratory settings. It has a high boiling point, low viscosity, and the ability to dissolve a wide range of polar and non-polar compounds. DMSO's core function is as a solvent, allowing for the effective dissolution and handling of various chemical substances during research and experimentation.
8
Freezone 4 by Labconco
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The FreeZone 4.5 is a lyophilizer, or freeze dryer, designed for laboratory use. It features a 4.5-liter capacity and can operate at temperatures as low as -50°C. The unit is capable of freeze drying a variety of samples.
9
Methacrylic anhydride by Merck Group
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Methacrylic anhydride is a colorless, pungent-smelling liquid used as a chemical intermediate in the production of various compounds. It is a reactive compound that can be used in the synthesis of other chemicals and materials.

More about "Freeze Drying"

Freeze drying, also known as lyophilization or cryodesiccation, is a dehydration process that removes water from a substance through the application of low temperature and reduced pressure.
This technique preserves the structure and composition of the original material and is commonly used in the pharmaceutical, food, and biotechnology industries to stabilize and extend the shelf-life of heat-sensitive products.
The process of freeze drying involves several key steps: freezing, primary drying, and secondary drying.
During freezing, the substance is cooled to a temperature below its freezing point, causing the water to solidify.
In the primary drying stage, the low pressure environment causes the frozen water to sublimate, transitioning directly from solid to gas phase.
The secondary drying stage further removes any residual moisture, ensuring the final product is stable and dry.
Freeze drying is often used to preserve a variety of delicate materials, including pharmaceuticals, biologics, and food products.
For example, the process can be used to stabilize Alpha 1-2 LD plus, a therapeutic enzyme, or Trypsin, a digestive enzyme used in cell culture applications.
The Zetasizer Nano ZS is a common instrument used to characterize the size and properties of particles during the freeze drying process.
To optimize freeze drying protocols, researchers and professionals can utilize the PubCompare.ai platform, which leverages AI-driven technology to compare and identify the best methods from literature, preprints, and patents.
This powerful tool enhances reproducibility and research accuracy, allowing users to experience the future of freeze drying optimization.
Other key equipment used in freeze drying includes the Freeze dryer, Whatman No. 1 filter paper, the S-4800 scanning electron microscope, and the FreeZone 4.5 freeze dryer.
The cryoprotectant DMSO is also commonly used to prevent damage during the freezing and drying stages.
By incorporating these insights and related terms, the freeze drying process can be better understood and optimized to meet the needs of various industries and applications.