The global population has rapidly expanded in the last few decades and is continuing to increase at a rapid pace. To meet this growing food demand fish is considered a balanced food source due to their high nutritious value and low cost. Fish are rich in well-balanced nutrients, a good source of polyunsaturated fatty acids and impose various health benefits. Furthermore, the most commonly used preservation technologies including cooling, freezing, super-chilling and chemical preservatives are discussed, which could prolong the shelf life. Non-thermal technologies such as pulsed electric field (PEF), fluorescence spectroscopy, hyperspectral imaging technique (HSI) and high-pressure processing (HPP) are used over thermal techniques in marine food industries for processing of most economical fish products in such a way as to meet consumer demands with minimal quality damage. Many by-products are produced as a result of processing techniques, which have caused serious environmental pollution. Therefore, highly advanced technologies to utilize these by-products for high-value-added product preparation for various applications are required. This review provides updated information on the nutritional value of fish, focusing on their preservation technologies to inhibit spoilage, improve shelf life, retard microbial and oxidative degradation while extending the new applications of non-thermal technologies, as well as reconsidering the values of by-products to obtain bioactive compounds that can be used as functional ingredients in pharmaceutical, cosmetics and food processing industries.

In this study, angiotensin-converting enzyme inhibitory peptides (ACE–IPs) derived from Muscovy duck (Cairina moschata) plasma hydrolysate (MDPH) were investigated. According to the general research protocol for bioactive peptides, the crude ACE–IPs of Muscovy duck plasma were separated and purified by ultrafiltration, gel chromatography and reversed-phase high-performance liquid chromatography (RP–HPLC). Then the components with the highest ACE inhibition potential were selected for identification. Finally, the inhibition mechanism was explored by molecular docking and in silico simulated digestion. A total of 121 peptides was detected, and five were screened for synthesis verification and molecular docking. The peptide VALSSLRP revealed high ACE inhibitory activity (91.67 ± 0.73%) because this peptide bound tightly to the S1′ pocket and formed 3 hydrogen bonds. Meaningfully, this work provides some new information about the generation of ACE–IPs derived from duck blood plasma.