The applications of hydrophobic interaction chromatography to the purification of plant proteins

Abstract

Protein separation by hydrophobic interaction chromatography (HIC) depends on the differences in surface hydrophobicity of the constituent proteins and is hence complementary to chromatographic techniques based on the charge or the size of the macromolecule. This review summarises some of the recent developments in HIC supports and discusses the parameters that must be considered in designing an efficient chromatographic system. The application of HIC to the purification of enzymes of secondary compound biosynthesis that cannot be obtained in pure form by size‐exclusion and ion‐exchange techniques alone is exemplified by reference to recent studies on tryptophan decarboxylase, strictosidine synthase and geraniol‐10‐hydroxylase.