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Characterisation of Bioactive Peptides from Red Alga Gracilariopsis chorda
Title: | Characterisation of Bioactive Peptides from Red Alga Gracilariopsis chorda |
Authors: | Mune Mune, Martin Alain Browse this author | Miyabe, Yoshikatsu Browse this author | Shimizu, Takeshi Browse this author | Matsui, Wataru Browse this author | Kumagai, Yuya Browse this author →KAKEN DB | Kishimura, Hideki Browse this author →KAKEN DB |
Keywords: | red alga | Gracilariopsis chorda | bioactive peptides | ACE inhibitory activity | DPP-IV inhibitory activity | DPPH scavenging activity |
Issue Date: | Jan-2023 |
Publisher: | MDPI |
Journal Title: | Marine drugs |
Volume: | 21 |
Issue: | 1 |
Start Page: | 49 |
Publisher DOI: | 10.3390/md21010049 |
Abstract: | In this study, we studied the bioactive peptides produced by thermolysin hydrolysis of a water-soluble protein (WSP) from the red alga Gracilariopsis chorda, whose major components are phycobiliproteins and Ribulose-1,5-bisphosphate carboxylase-oxygenase (RuBisCo). The results showed that WSP hydrolysate exhibited significantly higher ACE inhibitory activity (92% inhibition) compared to DPP-IV inhibitory activity and DPPH scavenging activity. The phycobiliproteins and RuBisCo of G. chorda contain a high proportion of hydrophobic (31.0-46.5%) and aromatic (5.1-46.5%) amino acid residues, which was considered suitable for the formation of peptides with strong ACE inhibitory activity. Therefore, we searched for peptides with strong ACE inhibitory activity and identified two novel peptides (IDHY and LVVER). Then, their interaction with human ACE was evaluated by molecular docking, and IDHY was found to be a promising inhibitor. In silico analysis was then performed on the structural factors affecting ACE inhibitory peptide release, using the predicted 3D structures of phycobiliproteins and RuBisCo. The results showed that most of the ACE inhibitory peptides are located in the highly solvent accessible alpha-helix. Therefore, it was suggested that G. chorda is a good source of bioactive peptides, especially ACE-inhibitory peptides. |
Type: | article |
URI: | http://hdl.handle.net/2115/88100 |
Appears in Collections: | 水産科学院・水産科学研究院 (Graduate School of Fisheries Sciences / Faculty of Fisheries Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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