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Characterisation of Bioactive Peptides from Red Alga Gracilariopsis chorda
by
Shimizu, Takeshi
, Matsui, Wataru
, Mune Mune, Martin Alain
, Kumagai, Yuya
, Kishimura, Hideki
, Miyabe, Yoshikatsu
in
ACE inhibitory activity
/ Algae
/ Amino acids
/ Antioxidants
/ Aromatic compounds
/ bioactive peptides
/ Biological activity
/ Chloroplasts
/ computer simulation
/ DPP-IV inhibitory activity
/ DPPH scavenging activity
/ Food
/ Functional foods & nutraceuticals
/ Gracilariopsis
/ Gracilariopsis chorda
/ Humans
/ Hydrolysates
/ hydrolysis
/ Hydrophobicity
/ Hypertension
/ Mass spectrometry
/ Molecular docking
/ Molecular Docking Simulation
/ Oxygenase
/ Peptides
/ Peptides - chemistry
/ Peptidyl-Dipeptidase A - chemistry
/ phycobiliprotein
/ Phycobiliproteins
/ Proteins
/ red alga
/ Rhodophyta - metabolism
/ Ribulose-1,5-bisphosphate
/ Ribulose-Bisphosphate Carboxylase
/ Scavenging
/ Scientific imaging
/ solvents
/ Thermolysin
/ water solubility
2023
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Characterisation of Bioactive Peptides from Red Alga Gracilariopsis chorda
by
Shimizu, Takeshi
, Matsui, Wataru
, Mune Mune, Martin Alain
, Kumagai, Yuya
, Kishimura, Hideki
, Miyabe, Yoshikatsu
in
ACE inhibitory activity
/ Algae
/ Amino acids
/ Antioxidants
/ Aromatic compounds
/ bioactive peptides
/ Biological activity
/ Chloroplasts
/ computer simulation
/ DPP-IV inhibitory activity
/ DPPH scavenging activity
/ Food
/ Functional foods & nutraceuticals
/ Gracilariopsis
/ Gracilariopsis chorda
/ Humans
/ Hydrolysates
/ hydrolysis
/ Hydrophobicity
/ Hypertension
/ Mass spectrometry
/ Molecular docking
/ Molecular Docking Simulation
/ Oxygenase
/ Peptides
/ Peptides - chemistry
/ Peptidyl-Dipeptidase A - chemistry
/ phycobiliprotein
/ Phycobiliproteins
/ Proteins
/ red alga
/ Rhodophyta - metabolism
/ Ribulose-1,5-bisphosphate
/ Ribulose-Bisphosphate Carboxylase
/ Scavenging
/ Scientific imaging
/ solvents
/ Thermolysin
/ water solubility
2023
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Characterisation of Bioactive Peptides from Red Alga Gracilariopsis chorda
by
Shimizu, Takeshi
, Matsui, Wataru
, Mune Mune, Martin Alain
, Kumagai, Yuya
, Kishimura, Hideki
, Miyabe, Yoshikatsu
in
ACE inhibitory activity
/ Algae
/ Amino acids
/ Antioxidants
/ Aromatic compounds
/ bioactive peptides
/ Biological activity
/ Chloroplasts
/ computer simulation
/ DPP-IV inhibitory activity
/ DPPH scavenging activity
/ Food
/ Functional foods & nutraceuticals
/ Gracilariopsis
/ Gracilariopsis chorda
/ Humans
/ Hydrolysates
/ hydrolysis
/ Hydrophobicity
/ Hypertension
/ Mass spectrometry
/ Molecular docking
/ Molecular Docking Simulation
/ Oxygenase
/ Peptides
/ Peptides - chemistry
/ Peptidyl-Dipeptidase A - chemistry
/ phycobiliprotein
/ Phycobiliproteins
/ Proteins
/ red alga
/ Rhodophyta - metabolism
/ Ribulose-1,5-bisphosphate
/ Ribulose-Bisphosphate Carboxylase
/ Scavenging
/ Scientific imaging
/ solvents
/ Thermolysin
/ water solubility
2023
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Characterisation of Bioactive Peptides from Red Alga Gracilariopsis chorda
Journal Article
Characterisation of Bioactive Peptides from Red Alga Gracilariopsis chorda
2023
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Overview
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 α-helix. Therefore, it was suggested that G. chorda is a good source of bioactive peptides, especially ACE-inhibitory peptides.
Publisher
MDPI AG,MDPI
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