A review on the processing of functional proteins or peptides derived from fish by-products and their industrial applications.

To understand the production and characteristics of protein hydrolysates pertaining to individual fish species, we selected and analyzed the most important commercial fish species according to the market value based on the Statistics on International Exports of Fishery Commodities by Food and Agriculture Organization. Accordingly, salmon, shrimp, cod, tuna, squid, and herring are marine species with high global value. Peptides obtained from their by-products were predominant in hydrophobic amino acids such as alanine, phenylalanine, methionine, proline, valine, tyrosine, tryptophan, leucine, and isoleucine. Bioactive peptides are short with a length of 2-20 amino acids. They remain inactive when they are within their parent proteins. Low molecular weight (0.3-8 kDa) peptides from hydrolyzed protein are easily digestible, readily absorbed by the body and are water-soluble. The hydrophobic nature contributes to their bioactivity, which facilitates their interactions with the membrane lipid bilayers. Incomplete hydrolysis results in low yields of hydrophobic amino acids. The glycosylation type of the resulting peptide fragment determines the different applications of the hydrolysate. The degree of conservation of the glycosidic residues and the size of the peptides are influenced by the method used to generate these hydrolysates. Therefore, it is crucial to explore inexpensive novel methodologies to generate bioactive peptides. According to the current studies, a unified approach (

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The authors declare no conflict of interest.