Structure-informed separation of bioactive peptides

Abstract

The application of proteomic and peptidomic technologies for food-derived bioactive peptides is an emerging field in food sciences. These technologies include the use of separation tools coupled to a high-resolution spectrometric and bioinformatic tools for prediction, identification, sequencing, and characterization of peptides. To a large extent, one-dimensional separation technologies have been extensively used as a continuous tool under different optimized conditions for the identification and analysis of food peptides. However, most one-dimensional separation technologies are fraught with significant bottlenecks such as insufficient sensitivity and specificity limits for complex samples. To address this limitation, separation systems based on orthogonal, multidimensional principles, which allow for the coupling of more than one analytical separation tool with different operational principles, provide a higher separation power than one-dimensional separation tools. This review describes the structure-informed separation and purification of protein hydrolyzates to obtain peptides with desirable bioactivities. Practical applicationsApplication of bioactive peptides in the formulation of functional foods, nutraceuticals, and therapeutic agents have increasingly gained scholarly and industrial attention. The bioactive peptides exist originally in protein sources and are only active after hydrolysis of the parent protein. Currently, several tools can be configured in one-dimensional or multidimensional systems for the separation and purification of protein hydrolyzates. The separations are informed by the structural properties such as the molecular weight, charge, hydrophobicity or hydrophilicity, and the solubility of peptides. This review provides a concise discussion on the commonly used analytical tools, their configurations, advantages and challenges in peptide separation. Emphasis is placed on how the structural properties of peptides assist in the separation and purification processes and the concomitant effect of the separation on peptide bioactivity. K E Y W O R D S bioactive peptides, multidimensional separation, peptide purification, separation systems, structure-property relationships [Correction added on 30 January 2019: this article has been added to the issue after an inadvertent omission.]

Production of angiotensin‐converting enzyme inhibitory peptides in Iranian ultrafiltered white cheese prepared with Lactobacillus brevis KX572382

“…The height and number of peaks also varied in the hydrophobic region (70-80 min) of the two chromatograms. The early peaks in chromatograms are mostly included low molecular weight hydrophilic peptides and amino acids and the peaks that appear later consist of hydrophobic peptides (Acquah et al, 2019). Differences between the two chromatograms showed that M8 was active on secondary proteolysis and the production of low molecular weight hydrophobic and hydrophilic peptides and amino acids in UF white cheese.…”

The antioxidant potential of peptides obtained from the spotted babylon snail (Babylonia areolata) in treating human colon adenocarcinoma (Caco-2) cells

“…Those peptides which offer low hydrophobicity as well as a low molecular weight will usually exhibit a low retention time in the column as a result of their amino acid sequence, and will be the rst to be eluted. 34,35 RP-HPLC was used to separate the MW < 0.65 kDa fraction from the SPH which had been shown to offer the greatest antioxidant activity. A sample solution was prepared which encompassed molecular polarity differences.…”

Peptide–Mineral Complexes: Understanding Their Chemical Interactions, Bioavailability, and Potential Application in Mitigating Micronutrient Deficiency

“…In general, the peptide mixture is subjected to ultrafiltration at a given molecular weight cut-off and the peptides of interest are extracted or captured using immobilized metal affinity chromatography (IMAC). IMAC is the most widely used technique for isolating metal-binding peptides due to its high sensitivity, selectivity, binding capacity and recovery rate [ 18 , 42 ]. Thus, proteins and peptides that form specific reversible complexes with the metal ions of interest are separated by retention in the solid phase of the column as they are non-covalently linked to the metal [ 18 ].…”