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Amino acid, structure and antioxidant properties of Haematococcus pluvialis protein hydrolysates produced by different proteases
Author(s) -
Zhu Yunping,
Zhao Xiaoyan,
Zhang Xiaowei,
Liu Hongkai,
Ao Qiang
Publication year - 2021
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.14618
Subject(s) - hydrolysate , chemistry , abts , dpph , hydrolysis , haematococcus pluvialis , antioxidant , amino acid , trypsin , food science , biochemistry , enzyme , carotenoid , astaxanthin
Summary 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.