Fish protein hydrolysates (FPH) from fresh water carps , and were prepared with 5, 10, 15 and 20% degree of hydrolysis (DH) using papain enzyme. FPH were evaluated for antioxidant properties using in vitro assays such as DPPH free radical scavenging activity (at 10 mg/ml), ferric reducing antioxidant power assay (at 20 mg/ml) and linoleic acid peroxidation inhibition activity (at 10 mg/ml). Antioxidant properties of FPH varied with species and DH.
View Article and Find Full Text PDFFish protein hydrolysates (FPHs) were prepared from freshwater carps (, , and ) using flavorzyme at different degrees of hydrolysis (DHs) ranging from 5 to 20%. The 2,2-diphenyl-1-picrylhydrazyl (DPPH) free-radical-scavenging activity of the FPHs prepared from the three species were in the range of 50-82%; the ferric reducing power of the FPHs prepared from catla was the highest. The linoleic acid peroxidation inhibition activity of the prepared FPHs varied from 71 to 91%.
View Article and Find Full Text PDFEnzymatic 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).
View Article and Find Full Text PDFFish protein hydrolysate (FPH) was prepared from fresh water fish Cirrhinus mrigala using papain and dried in oven (OD-FPH) and freeze dryer (FD-FPH). The electron micrographs of FD-FPH samples showed porous structure. The browning intensity of OD-FPH samples was higher than the FD-FPH samples.
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