Hydrophobic Interaction Chromatography: A Key Method for Protein Separation
This review's main goal is to increase theoretical knowledge and comprehension of the techniques used to separate important enzymes using chromatography. Protein separation, purification, and analysis frequently involve the use of hydrophobic interaction chromatography (HIC), in which the molecules are separated based on differences in hydrophobicity. It is conducted using a weakly hydrophobic, nonpolar stationary phase to which the proteins bind in an aqueous highsalt solution as the mobile phase. The protein integrity is thereby conserved during the process. HIC is usually used with a gradient from high to low concentrations of salt as an eluent and can be applied in a wide range of biotechnological processes. In this study, after a brief overview of hydrophobic interaction chromatography, we explain the HIC procedure, protein retention mechanism, factors affecting HIC, and applications of HIC.
Hydrophobic interaction chromatography, protein purification.
ISSN 2637-2835 (Print)
International Burch University