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

Gajanan, Phadke Girija; Elavarasan, Krishnamoorthy; Shamasundar, Bangalore Aswathnarayan

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

2016

Gajanan, Phadke Girija | Elavarasan, Krishnamoorthy | Shamasundar, Bangalore Aswathnarayan

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.

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