Antioxidant properties of pancreatic hydrolysates from various protein sources

Abstract

Antioxidant activity of pancreatic hydrolysates of casein, spent brewer's yeast, bovine liver and tendon was evaluated in comparison to unhydrolised substrates by ABTS assay. In the result of enzymic treatment ABTS cation radical scavenging activity of spent brewer's yeast, bovine liver and bovine tendon was increased in 4.8, 3.3, and 2.3 times respectively, except casein. The IC 50 values of ABTS cation radical scavenging for casein and it's hydrolysate were similar. The IC 50 values of DPPH radical scavenging activity for pancreatic hydrolysates of casein, spent brewer's yeast, bovine liver and tendon were 1.8±0.1 mg/ml, 1.3±0.1 mg/ml, 1.7±0.1 mg/ml, and 6.2±0.1 mg/ml respectively. Above mentioned hydrolysates of various origin were produced at the same conditions (temperature 50 o C, pH 7.5-8.9, duration 5 hours) using fresh bovine pancreatic tissue as an enzyme source. The extent of hydrolysis expressed as AN/TN (amino nitrogen/ total nitrogen) for hydrolysates had values from 0.36±0.02 to 0.46±0.04.

In vitro α-amylase inhibitory and antioxidant properties of pancreatin-derived <em>Polyalthia longifolia</em> seed protein hydrolysate

“…Lorenzo et al (2018) chronicled quite thoroughly the role of protein hydrolysates and isolated bioactive peptides in scavenging ABTS + radical. In particular, pancreatin-derived protein hydrolysates have shown great effectiveness in this regard (Bayarjargal et al, 2014;Karamac et al, 2014;Liao et al, 2020). In this study, ascorbate yielded considerable ABTS + radical scavenging capacity at lower concentrations than the hydrolysate (Figure 3).…”