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Hokkaido University Collection of Scholarly and Academic Papers >
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Angiotensin I Converting Enzyme Inhibitory Peptides Derived from Phycobiliproteins of Dulse Palmaria palmata
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| Title: | Angiotensin I Converting Enzyme Inhibitory Peptides Derived from Phycobiliproteins of Dulse Palmaria palmata |
| Authors: | Furuta, Tomoe Browse this author | | Miyabe, Yoshikatsu Browse this author | | Yasui, Hajime Browse this author →KAKEN DB | | Kinoshita, Yasunori Browse this author | | Kishimura, Hideki Browse this author →KAKEN DB |
| Keywords: | ACE inhibitory activity | | antihypertension | | dulse | | Palmaria palmata | | phycobiliprotein | | primary structure | | recombinant protein | | red algae |
| Issue Date: | Feb-2016 |
| Publisher: | MDPI |
| Journal Title: | Marine Drugs |
| Volume: | 14 |
| Issue: | 2 |
| Start Page: | UNSP 32 |
| Publisher DOI: | 10.3390/md14020032 |
| Abstract: | We examined the inhibitory activity of angiotensin I converting enzyme (ACE) in protein hydrolysates from dulse, Palmaria palmata. The proteins extracted from dulse were mainly composed of phycoerythrin (PE) followed by phycocyanin (PC) and allophycocyanin (APC). The dulse proteins showed slight ACE inhibitory activity, whereas the inhibitory activity was extremely enhanced by thermolysin hydrolysis. The ACE inhibitory activity of hydrolysates was hardly affected by additional pepsin, trypsin and chymotrypsin treatments. Nine ACE inhibitory peptides (YRD, AGGEY, VYRT, VDHY, IKGHY, LKNPG, LDY, LRY, FEQDWAS) were isolated from the hydrolysates by reversed-phase high-performance liquid chromatography (HPLC), and it was demonstrated that the synthetic peptide LRY (IC50: 0.044 mol) has remarkably high ACE inhibitory activity. Then, we investigated the structural properties of dulse phycobiliproteins to discuss the origin of dulse ACE inhibitory peptides. Each dulse phycobiliprotein possesses -subunit (Mw: 17,477-17,638) and -subunit (Mw: 17,455-18,407). The sequences of YRD, AGGEY, VYRT, VDHY, LKNPG and LDY were detected in the primary structure of PE -subunit, and the LDY also exists in the APC - and -subunits. In addition, the LRY sequence was found in the -subunits of PE, PC and APC. From these results, it was suggested that the dulse ACE inhibitory peptides were derived from phycobiliproteins, especially PE. To make sure the deduction, we carried out additional experiment by using recombinant PE. We expressed the recombinant - and -subunits of PE (rPE and rPE, respectively), and then prepared their peptides by thermolysin hydrolysis. As a result, these peptides showed high ACE inhibitory activities (rPE: 94.4%; rPE: 87.0%). Therefore, we concluded that the original proteins of dulse ACE inhibitory peptides were phycobiliproteins. |
| Rights: | http://creativecommons.org/licenses/by/4.0/ |
| Type: | article |
| URI: | http://hdl.handle.net/2115/61395 |
| 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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Submitter: 岸村 栄毅
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