PURIFICATION AND CHARACTERIZATION OF ACE INHIBITORY PEPTIDE FROM AQUATIC RESOURCES: A REVIEW
Protein purification is an essential first step for the study of its molecular and biological properties in order to understand its specific biological function. There are several properties such as molecular weight, charge, hydrophobicity, amino acid composition, and etc. that can be exploited to purify or single out a target peptide from a mixture. Base on those properties, several chromatographic and non-chromatographic procedures have become available. The obtained protein hydrolysate from hydrolysis reaction showing inhibitory activity against ACE purified by using different techniques such as non-chromatographic (ultrafiltration; UF), and chromatographic (gel filtration; GF, ion exchange; IE, or reversed phase high performance liquid chromatography; RP-HPLC). After purification step, the potent fraction is indispensable tools for peptide mapping and protein primary structure elucidation by using mass spectrometry (MS) techniques, HPLC separation or protein sequencing for detecting molecular mass, amino acid sequence or amino acid composition. This article is presented the purification and characterization of ACE inhibitory peptides obtained by enzymatic hydrolysis of proteins from aquatic resources. Identification techniques of the peptides are also reviewed. The methods of purification and identification are significant steps that increase purity and efficacy of potent ACE inhibitory peptide (ACEIP).