Purification of chicken breast protein hydrolysate and analysis of its antioxidant activity

Food Chem Toxicol. 2012 Oct;50(10):3397-404. doi: 10.1016/j.fct.2012.07.047. Epub 2012 Aug 1.

Abstract

Chicken breast protein was hydrolyzed by papain under optimal conditions. The antioxidant activity of the chicken breast protein hydrolysate was then evaluated in vitro and in vivo using different measurements, including reducing power and DPPH radical scavenging assays. The reducing power of the hydrolysate was 0.5 at 2.37 mg/mL. The DPPH radical scavenging assay showed that the EC50 value of the hydrolysate was 1.28 mg/mL. In antioxidant assays in vivo, d-galactose-induced aging mice administrated the fraction peptides of chicken breast protein hydrolysate showed significantly increased antioxidant enzyme activities, while malondialdehyde levels decreased both in serums and livers. Under a transmission electron microscope (TEM), the ultramicrostructure of hepatic tissue was observed and we found that the hydrolysate may play a part in inhibiting oxidative stress in hepatocytes in vivo. Therefore, we concluded that chicken breast protein hydrolysate exhibits significant antioxidant activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino-Acid N-Acetyltransferase / chemistry
  • Animals
  • Antioxidants / chemistry
  • Antioxidants / pharmacology*
  • Biphenyl Compounds
  • Chickens*
  • Hydrolysis
  • Liver / drug effects
  • Liver / ultrastructure
  • Male
  • Mice
  • Mice, Inbred ICR
  • Muscle Proteins / chemistry*
  • Muscle, Skeletal / chemistry*
  • Papain
  • Picrates

Substances

  • Antioxidants
  • Biphenyl Compounds
  • Muscle Proteins
  • Picrates
  • 1,1-diphenyl-2-picrylhydrazyl
  • Amino-Acid N-Acetyltransferase
  • Papain