Antioxidant Stability of Fermented Sour Meat Peptides
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Abstract:
Extraction of fermented sour meat peptides was performed via alkaline protease hydrolysis, and the effects of different pHs, temperatures, metal ions, food raw materials, lighting and simulated gastrointestinal environment on the OH radical scavenging rate, DPPH clearance rate, metal ion chelating ability and reducing power of sour meat peptide were examined. In the pH range of 3~11, the antioxidant activity of the sour meat peptide increased first and then decreased with an increase of pH. When pH=7, DPPH radical scavenging rate, Fe2+ chelating ability and reducing power of Fe2+ were the highest (85.56%, 93.21% and 85.61% respectively). In the temperature range of 20~100 ℃, the antioxidant activity of the sour meat peptide first increased and then decreased with an increase of temperature. When temperature was 40 ℃, the scavenging rates of OH radical and DPPH radical, and the chelating ability and reducing power of Fe2+ were the highest (90.88%, 91.64%, 74.54% and 72.58% respectively). The antioxidant activity of sour meat peptide was lower in the environment with Cu2+ or Zn2+ ion, but the rate of bioactivity retention was higher in the environment with K+ or Ca2+ ion. The presence of environmental glucose or NaCl exhibited a certain inhibitory or destructive effect on the sour meat peptide. The antioxidant activity of the sour meat peptide decreased with an extension of storage time, and a dark environment was more beneficial to the antioxidant stability for sour meat peptide. Under simulated gastrointestinal conditions, the order of the antioxidant stability of the sour meat peptide was gastric juice digestion > gastrointestinal digestion. In summary, in order to maintain a higher antioxidant activity of the fermented sour meat peptide, it is necessary to avoid strong acid, strong alkali, high temperature, contacts with Cu2+ and Zn2+ ions, high sugar, high NaCl , and light during storage.