Enzymatic Hydrolysis of Defatted Antheraea pernyi (Lepidoptera: Saturniidae) Pupa Protein by Combined Neutral Protease Yield Peptides With Antioxidant Activity

J Insect Sci. 2021 Mar 1;21(2):5. doi: 10.1093/jisesa/ieab013.

Abstract

In this study, peptides were prepared from defatted Antheraea pernyi (Lepidoptera: Saturniidae) pupa protein via hydrolysis with combined neutral proteases. Single-factor tests and response surface methodology (RSM) were used to determine the optimal hydrolysis condition suitable for industrial application. Optimal hydrolysis of the defatted pupa protein was found to occur at an enzyme concentration of 4.85 g/liter, a substrate concentration of 41 g/liter, a hydrolysis temperature of 55°C, and a hydrolysis time of 10 h and 40 min. Under these conditions, the predicted and actual rates of hydrolysis were 45.82% and 45.75%, respectively. Peptides with a molecular weight of less than 2,000 Da accounted for 90.5% of the total peptides generated. Some of the peptides were antioxidant peptides as revealed by sequencing and functional analysis. The antioxidant activity of the mixed peptides was subsequently confirmed by an antioxidant activity assay. The results showed that peptides with high antioxidant activity could be obtained from the hydrolysis of A. pernyi pupa protein.

Keywords: antioxidant activity; combined neutral protease; defatted Antheraea pernyi pupa protein; peptides; response surface methodology.

MeSH terms

  • Animals
  • Antioxidants / isolation & purification
  • Antioxidants / metabolism
  • Hydrolysis*
  • Moths / metabolism*
  • Peptide Hydrolases
  • Peptides / isolation & purification*
  • Peptides / metabolism
  • Pupa / metabolism

Substances

  • Antioxidants
  • Peptides
  • Peptide Hydrolases