Separation and Characterization of Antioxidative and Angiotensin Converting Enzyme Inhibitory Peptide from Jellyfish Gonad Hydrolysate

• Published in: Molecules (Basel, Switzerland) Vol. 23; no. 1; p. 94
• Main Authors: Zhang, Qin, Song, Chengcheng, Zhao, Jun, Shi, Xiaomei, Sun, Meiling, Liu, Jing, Fu, Yinghuan, Jin, Wengang, Zhu, Beiwei
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 05.01.2018; MDPI
• Subjects: ACE inhibitory activity; Amino Acid Sequence; Angiotensin-Converting Enzyme Inhibitors - chemistry; Angiotensin-Converting Enzyme Inhibitors - isolation & purification; Animals; antioxidant activity; Binding sites; Biphenyl Compounds - chemistry; Catalytic Domain; Chromatography, Gel; Dipeptides - chemistry; Dipeptides - isolation & purification; Free Radical Scavengers - chemistry; Free Radical Scavengers - isolation & purification; Gonads - chemistry; Hydrolysis; jellyfish gonad protein hydrolysate; Molecular Docking Simulation; Peptides; Peptidyl-Dipeptidase A - chemistry; Picrates - chemistry; Protein Binding; Proteins; Scyphozoa - chemistry; Superoxides - chemistry; peptides; ACE inhibitory activity; antioxidant activity; jellyfish gonad protein hydrolysate

The gonad of jellyfish (Rhopilema esculentum Kishinouye), containing high protein content with a rich amino acid composition, is suitable for the preparation of bioactive peptides. Jellyfish gonad was hydrolysed with neutral protease to obtain jellyfish gonad protein hydrolysate (JGPH), which was th...