| Affiliation: | 1. Beijing Advanced Innovation Center for Food Nutrition and Human Health, Beijing Technology and Business University (BTBU), 11 Fucheng Road, 100048 Beijing, China Yunping Zhu and Xiaoyan Zhao contributed equally to this work.;2. Department of Food Science and Nutrition, Culinary Institute, University of Jinan, No. 13 Shungeng Road, 250022 Jinan, China;3. Department of Tissue Engineering, China Medical University, 77 Puhe Road, 110122 Shenyang, China |
| Abstract: | 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 β-sheet proportion of HP hydrolysates were higher compared with HP, the proportion of random coil structure was lower. The α-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. |
