Evaluation of Preparation, in Vitro and in Vivo Activity of Antioxidant Peptides from Silkworm Pupae
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Abstract:
This study sought to optimize the process of the enzymatic hydrolysis of silkworm pupa protein by alkaline protease by increasing the response value in response surface method. DPPH and ABTS free radical scavenging rates were employed as the evaluation indices of hydrolyzed peptides. This allowed for the screening and identification of enzymatic hydrolysis processes exhibiting strong antioxidant activity. As a result, the optimal enzyme was identified as alkaline protease with pH value 9.0, a temperature of 48 ℃, a substrate mass fraction of 4.1%, a reaction time of 2 h, and an enzyme mass fraction of 3.0%. Compared with the existing process, the reaction time and temperature were reduced, and the antioxidant activity in vitro was improved, reaching 89.10% of Vc. On this basis, the antioxidant activity of the silkworm pupa peptide in vivo was evaluated using an oxidative stress mouse model induced by D-galactose. The low-dose group of silkworm pupa peptide was able to restore the CK, SOD, T-AOC and GSH-PX factors in serum to 0.31, 105.44, 3.51 and 308.36 U/mL, respectively. In addition, the MDA and SOD factors in the liver were restored to 0.71 nmol/mL and 77.40 U/mL, respectively, which were significantly different from the model group (P<0.05). In summary, silkworm pupa peptide prepared using the double response surface method optimized the process flow and improved the antioxidant activity, enhancing antioxidant activity both in vitro and in vivo. This provides an experimental basis for the development and utilization of silkworm pupa protein peptides.
