Antioxidant Activity of Peptides Derived from Enzymatic Digestion of Spirulina platensis Protein Extract by Different Proteases Antioxidant activity of protein digests of S. platensis
Trends in Peptide and Protein Sciences,
Vol. 7 (2022),
Page 1-7 (e6)
One of the attractive sources of bioactive compounds is cyanobacteria and in particular, Chlorella vulgaris and Spirulina platensis. Enzymatic digestion of the Spirulina protein extract can result in bioactive peptides with diverse activities, including antioxidant function. This study aims to produce peptides with antioxidant properties after the enzymatic digestion of Spirulina platensis protein extract using three enzymes: bacterial protease, pepsin, and papain. The protein extract from Spirulina platensis was subjected to enzyme hydrolysis for 3 hours at 37°C (pH 7.4 for papain and bacterial protease and pH 5 for pepsin). The concentration of peptide fragments was evaluated to determine the yield of protein digestion. In order to measure the level of anti-oxidative potential of the hydrolysates, the DPPH assay was run. The results indicated that the bacterial protease led to the highest concentration of peptide fragments, while the hydrolysate obtained from pepsin digestion showed the most antioxidant activity (80%), mainly the peptides that have molecular weights less than 14 KDa. Consequently, pepsin can be a proper enzyme to produce antioxidant peptides from the protein extract of S. platensis. In conclusion, the results of the study confirmed that the products of enzymatic digestion by different enzymes have distinct features.
- Spirulina platensis protein extract was digested with three types of protease.
- Digestion of protein extract by pepsin resulted in higher antioxidant activity.
- Digestion by bacterial protease from Bacillus licheniformis resulted in higher yield of peptide formation.
- Spirulina platensis
- Protein extraction
- Protease digestion
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