Organic Solvent Precipitation
Organic Solvent Precipitation - Related Videos
11:12
Organic Solvent-Based Protein Precipitation for Robust Proteome Purification Ahead of Mass Spectrometry
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Cited by 8 •
2022
The present protocol describes solvent-based protein precipitation under controlled conditions for robust and rapid recovery and purification of proteome samples prior to mass spectrometry.
06:30
Efficient Purification of Elastin-Like Polypeptides (ELPs) from E. coli Using an Organic Solvent-based Extraction and Precipitation Method
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2026
This protocol describes a rapid, reproducible organic solvent-based extraction and precipitation method for purifying elastin-like polypeptide (ELP) from Escherichia coli, providing a potentially scalable alternative to conventional ELP purification methods.
00:49
Gravimetry: Inorganic And Organic Precipitating Agents
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2024
In gravimetry, the precipitant is chosen carefully to obtain a pure solid that can be easily filtered. Common inorganic precipitants can be used to determine several cations and anions. In some cases, the formation of the same precipitate can be used to determine the cation and the anion. For example, the reaction of barium and chromate ions to give barium chromate is used to determine both barium and chromate. However, precipitates such as hydroxides, oxalates, and metal ammonium phosphates...
06:43
Rotary Evaporation to Remove Solvent
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2023
Source: Dr. Melanie Pribisko Yen and Grace Tang — California Institute of Technology Rotary evaporation is a technique most commonly used in organic chemistry to remove a solvent from a higher-boiling point compound of interest. The rotary evaporator, or "rotovap", was invented in 1950 by the chemist Lyman C. Craig. The primary use of a rotovap is to dry and purify samples for downstream applications. Its speed and ability to handle large volumes of solvent make rotary evaporation a preferred...
07:47
Staining of Proteins in Gels with Coomassie G-250 without Organic Solvent and Acetic Acid
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Cited by 94 •
2009
A short protocol for protein staining with Coomassie Brilliant Blue (CBB) G-250 in polyacrylamide gels is described without using organic solvents or acetic acid as in the classical staining procedures with CBB.
FAQs
Ethanol and acetone alter the solution’s polarity and dielectric constant, weakening interactions between dissolved biomolecules and the surrounding solvent. As solvation becomes less favorable, biomolecules aggregate rather than remain dispersed, producing a precipitate that can be recovered. This mechanism explains why solvent composition is central to concentrating biological material and separating it from components that remain soluble.
Temperature, the proportion of organic solvent, and ionic strength are key variables. Changing these conditions can alter how readily particular biomolecules lose solubility, so they influence both selectivity and yield. In practice, condition control determines whether the process favors broad recovery of biological material or more selective fractionation within a complex sample.
The solvent proportion controls the extent to which solution polarity and dielectric behavior change. A suitable proportion can promote aggregation of the target biomolecule while leaving some soluble contaminants behind, supporting purification as well as concentration. Because proteins and nucleic acids are used in different biological workflows, adjusting this variable helps match precipitation behavior to the intended sample-processing goal.
A typical workflow begins with a biological solution containing the dissolved material of interest, followed by addition of an organic solvent such as ethanol or acetone. The solvent proportion, temperature, and ionic strength are then considered because they affect precipitation. The resulting aggregated material forms a recoverable precipitate, while remaining soluble components stay in the surrounding solution.
Researchers use the approach when they need to concentrate biomolecules, fractionate proteins, recover nucleic acids, or remove some soluble contaminants before downstream analysis. Its value is greatest when a sample requires a straightforward separation step rather than elaborate equipment. The method therefore fits biochemical research, general sample preparation, and diagnostic workflows.
Its main practical advantage is simplicity: the method uses organic solvents to change solubility and requires relatively little equipment. That accessibility supports use across biochemical research and diagnostic workflows, including situations where sample concentration or cleanup is needed before analysis. The outcome is a recoverable biomolecule fraction, although selectivity and yield still depend on controlled conditions.