Vol. 11, Special Issue 2 (2022)

Author(s):
E Vimalraj, R Ramani, V Appa Rao, M Parthiban and R Narendrababu

Abstract:
Chicken intestine was hydrolysed by protease P food grade fungal enzyme. The protein hydrolysate solution was filtered and separated into small molecular weight fractions by ultrafiltration at 4 °C using 10kDa molecular weight cut-off and 3kDa molecular weight cut-off to enrich specific hydrolysate fractions. This permeate was defined as small peptides with molecular weight less than 10,000 Da and 3000 Da. The filtrate thus obtained was assessed for antioxidant in vitro DPPH radical scavenging assay. Parameters like filterate, concentrate, and total recovery of hydrolysate was studied after ultrafilteration. The filtrate recovery of protein hydrolysate was 47.01 ± 0.2 per cent, concentrate recovery of protein hydrolysate was 5.12 ± 0.45 per cent, total recovery of protein hydrolysate was 52.14 ± 0.2 per cent. The inhibitory concentration IC₅₀ value by DPPH radical scavenging assay of hydrolysate was 1.45 ± 00 mg/ml, bioactive peptides (< 10 kDa) was 0.15 ± 00 mg/ml and bioactive peptides (<3kDa) was 1.90 ± 0.8 mg/ml. Then it was compared with the standard butylated hydroxyl toluene whose IC₅₀ value 0.23 ± 0.3 mg/ml. The bioactive peptides was having lower IC₅₀ value than hydrolysate. So, lower IC₅₀ value indicate higher potency of the extracted peptides when compared to the standard butylated hydroxyl toluene. Antioxidant bioactive peptides extracted from chicken intestine had the molecular weight between 9.4 kDa to 9.8 kDa. Thus the byproduct from chicken industry i.e chicken intestine can be utilized by transforming in to antioxidant bioactive peptides as alternatives to synthetic antioxidants used in pet food.