A Review on Purification and Characterization of Anti-proliferative Peptides Derived from Fish Protein Hydrolysate

ABSTRACT

Bioactive peptide with anti-proliferative activity is a novel prospect to develop cancer drugs with fewer or no side effects, as well as cost benefits. The current review provides a development strategy for anti-proliferative peptides derived from fish and its discards through fish protein hydrolysate. The study indicates that enzymatic hydrolysates act as a superior anti-proliferative agent through superior enzyme selection. In general, ion-exchange chromatography, RP-HPLC, ultra, and gel filtration methods are used to purify bioactive peptides. Characterization of the purified peptide can be done with the help of cytotoxicity assay, molecular mass, amino acid composition, and sequence. Most studies on anti-proliferative bioactive peptides have been carried out via in vitro analysis. However, very few studies have provided confirmatory results through in vivo analysis.

Graphical Abstract

KEYWORDS:

• Fish protein hydrolysate
• bioactive peptide
• anti-proliferative peptide
• anticancer
• peptide purification
• peptide characterization

Highlights

• Anti-proliferative peptides obtained from purification of fish protein hydrolysate

• Superior anti-proliferative agent derived from its superior enzyme selection of FPH

• Peptide characterization includes molecular mass, amino acid composition, and sequence

• Purified peptides naturally obtained without side effects as its major advantage

• FPH contribute additional income and waste management to fish processing industry

Author contributions

All authors contributed to the final manuscript. Mannur, I.S. collected the literature sources and wrote the manuscript. Sarbon, N.M. conceptualized the idea and performed critical reviews on manuscript.

Competing interests statements

The authors declare no competing financial or non- financial interest.