Vol. 11, Special Issue 2 (2022)

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

Abstract:
Antidiabetic activity of peptides in Chicken intestine hydrolysate was assessed by α- amylase inhibitory activity assay. protease P food grade fungal enzyme was used to hydrolyse the chicken intestine. 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 invitro α- amylase inhibitory activity 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 IC₅₀ value of protein hydrolysate was 273.04 ± 20 mg/ml, bioactive peptides (< 10 kDa) was 959 ± 8.1 mg/ml and bioactive peptides (<3kDa) was 362.86 ± 23mg/ml. Then it was compared with the standard Acarbose whose IC₅₀ value was 158.42 ± 10 mg/ml. The test of significance revealed that the alpha amylase inhibitory activity between protein hydrolysate and bioactive peptides was highly significant (P<0.01). However, the bioactive peptides was having higher IC₅₀ value than hydrolysate and standard Acarbose. It indicates lower potency of the extracted peptides when compared to the standard acarbose. But Peptides from chicken intestine hydrolysate have antidiabetic activity and offer a promising approach to prevent, control diabetes through regulated diet in animals.