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Hydrophobic interaction media:

Hydrophobic interaction media:

Chromatography, short for “chromatographic analysis”, is a method for the separation and determination of multi-component mixtures based on the different physical properties of each component. Through cooperation with Bestchrom (Shanghai) Biosciences Co., Ltd, Jean Standard Biological Technology Co. Ltd provides customers with quality products and services, including gel filtration media, ion exchange media, hydrophobic interaction media, affinity chromatography media, etc.
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Hydrophobic interaction media:

Hydrophobic interaction chromatography is a commonly used method to separate biomacromolecules such as proteins or peptides according to the difference in the hydrophobicity of molecular surface. The key to the selection of hydrophobic chromatography media lies in the appropriate hydrophobic ligands. If the protein is with strong hydrophobicity, then select a medium with weak hydrophobicity, and vice versa. A certain amount of salt (usually ammonium sulfate) should be added to the buffer to enhance the binding of protein to hydrophobic medium. If the protein itself is with strong hydrophobicity, there is no need to add too much salt. Hydrophobic media with smaller particles can be selected to improve the resolution



Factors affecting the hydrophobic effect

(1)Type and Concentration of Salt 

Some ions that form the salt in the buffer have a stabilizing effect on protein conformation, such as SO42-, which can improve the stability of protein structure, decrease the solubility of protein, have a salting out effect on protein, and enhance the hydrophobic effect between protein and ligand. Some ions have an un-stabilizing effect on protein conformation, such as Cl- and Ca2+, which can increase protein solubility, and these ions have a strong elution ability. The properties of salting out and salting in can be used as the basis for choosing the equilibrium and elution conditions of hydrophobic media.  


In the process of hydrophobic chromatography, the temperature goes up, there are conformational changes in biomacromolecules, and the hydrophobic effect is enhanced, which helps to improve the separating degree of column chromatography. However, for bioactive substances, high temperature will cause denaturation and deactivation, so hydrophobic chromatography is often conducted under a normal temperature or low temperature. It is suggested that hydrophobic chromatography should be conducted under the condition of constant temperature to avoid the influence of temperature changes on the tomographic results. 


The mobile phase of hydrophobic chromatography is usually a phosphate buffer with a neutral pH value. The interaction between protein and hydrophobic group decreases with the increase of pH, because the charge of acidic group of protein increases gradually with the increase of pH, and the hydrophilicity increases. However, the hydrophobicity of proteins is usually not changed by adjusting the pH of solution in hydrophobic chromatography.



Product Series Product
High rigidity agarose base frame hydrophobic chromatography medium
Diamond Phenyl(HS)/Diamond Phenyl(LS)
Diamond Octyl
Diamond Butyl
Diamond Mustang
High-resolution rigid agarose-based hydrophobic chromatography medium
Diamond Phenyl Mustang
Diamond Octyl Mustang
Diamond Butyl Mustang
Bestarose FF
Fast-flow agarose-based hydrophobic chromatography medium
Phenyl Bestarose FF (HS)/
Phenyl Bestarose FF (LS)
Butyl Bestarose 4 FF
Octyl Bestarose 4 FF
Butyl-S Bestarose FF
Bestarose High Performance Butyl Bestarose HP
Phenyl Bestarose HP
Octyl Bestarose HP
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