Bioactive and functional properties of protein hydrolysates from fish frame processing waste using plant proteases

Abstract

Enzymatic conversion of fish frame waste of threadfin breams (Nemipterus japonicus) to protein hydrolysate could be a solution for minimizing the pollution issues related to seafood processing operations and a way for the value addition to processing by-products. Protein hydrolysates from fish frame waste (FW) of thread fin breams (N. japonicus) were prepared and evaluated for bioactive properties such as angiotensin-I-converting enzyme (ACE) inhibitory activity and antioxidant and functional properties as a function of degree of hydrolysis (DH). Two different plant proteases, papain and bromelain, were used to prepare fish protein hydrolysates (FPH) and designated as HP (hydrolysates prepared using papain) and HB (hydrolysates prepared using bromelain). The ACE inhibitory activity of HP samples was higher at 5 and 10 % DH than that of the HB samples at DH 15 %, and there was no significant difference (p < 0.05). Antioxidant properties (2, 2 diphenyl-1-picrylhydrazyl [DPPH] radical scavenging activity, ferric reducing power and lipid peroxidation inhibition) of hydrolysates increased with increase in DH. The HB samples at DH 15 % had significantly higher antioxidant properties than HP samples (p < 0.05). The solubility of HP and HB samples was high in a wide range of pH and increased with DH. The functional properties of HP and HB samples decreased significantly with increase in DH (p < 0.05). The fractionation of the HB-DH 15 % sample yielded three peptide fractions with the approximate molecular weight of peptides in the range of 7562-812 Da. Relatively, bromelain enzyme is more effective in producing the FPH with desirable bioactive and functional properties.

Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity, Antioxidant Properties, Phenolic Content and Amino Acid Profiles of Fucus spiralis L. Protein Hydrolysate Fractions

“…Furthermore, this previous report also revealed that bromelain exhibited the highest specificity in the generation of ACE-inhibitory peptides from Ulva rigida protein. Other studies on other marine resources, such as different kinds of fish, also showed that bromelain is the most efficient protease tested for the production of protein hydrolysates with higher bioactivities (ACE-inhibitory and/or antioxidant activities) [ 30 , 31 , 32 ]. On the other hand, a molecular weight cut-off (MWCO) dialysis of FSPH was further used as means of enhancing its bioactivities, as well as to provide insights into the molecular weight distribution of the bioactive compounds presented in the hydrolysate.…”

Production of Fish Protein Hydrolysates from Scyliorhinus canicula Discards with Antihypertensive and Antioxidant Activities by Enzymatic Hydrolysis and Mathematical Optimization Using Response Surface Methodology

“…DPPH and ABTS maximum values varied among 12.4% and 5.1% for Alcalase hydrolysates and 16% and 7.3% for Esperase hydrolysates. These antioxidant activities are lower than those addressed for FPH formulated with different materials and using several enzymes: horse mackerel and subtilisin [ 10 ], red scorpionfish and Flavourzyme [ 32 ], or threadfin bream and Papain [ 33 ].…”

Marine Fish Proteins and Peptides for Cosmeceuticals: A Review

“…Various types of methods have been used to evaluate the antioxidant activity of fish-derived peptides, including the 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging assay, the 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) radical scavenging assay, hydroxyl radical scavenging activity, Cu 2+ chelating activity, and Fe 2+ chelating activity [99,100,101,102,103,104,105]. …”