Amino acid, structure and antioxidant properties of Haematococcus pluvialis protein hydrolysates produced by different proteases

The impact of different protease hydrolysis on the amino acid, structure and antioxidant properties of H. pluvialis protein (HP) was investigated. Results showed that the hydrolysate obtained by Alcalase exhibited the highest degree of hydrolysis (20.59%) and peptide yield (92.64%). The essential amino acid, hydrophobic, sulphur and aromatic amino acid contents of enzyme hydrolysates were significantly higher than HP (P < 0.05). FTIR spectra showed that the beta-sheet proportion of HP hydrolysates were higher compared with HP, the proportion of random coil structure was lower. The alpha-helix content of the hydrolysate obtained by Alcalase was the highest, while the turn proportion was the lowest. The Trypsin derived hydrolysate presented the best DPPH and ABTS scavenging ability, and ferric reducing antioxidant power than other HPHs. These results suggested that HP hydrolysates have a great potential as natural functional ingredients in food manufacture.

Automated summary

The impact of different protease hydrolysis on H. pluvialis protein was studied, showing that enzyme hydrolysates had higher essential amino acid, hydrophobic, sulphur, and aromatic amino acid contents compared to HP. Alcalase hydrolysate had the highest degree of hydrolysis and peptide yield, with higher alpha-helix content. Trypsin-derived hydrolysate exhibited the best antioxidant properties among all hydrolysates. This suggests the potential of HP hydrolysates as natural functional ingredients in food production.