Angiotensin I Converting Enzyme Inhibitory Peptides Derived from Phycobiliproteins of Dulse Palmaria palmata

Furuta, Tomoe; Miyabe, Yoshikatsu; Yasui, Hajime; Kinoshita, Yasunori; Kishimura, Hideki

Angiotensin I Converting Enzyme Inhibitory Peptides Derived from Phycobiliproteins of Dulse Palmaria palmata

Furuta, Tomoe; Miyabe, Yoshikatsu; Yasui, Hajime et al.

Marine Drugs, 2016, 14(2), UNSP 32

Permalink : https://hdl.handle.net/2115/61395

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アクセス権	open access
URI	https://hdl.handle.net/2115/61395
タイトル	Angiotensin I Converting Enzyme Inhibitory Peptides Derived from Phycobiliproteins of Dulse Palmaria palmata
著者	Furuta, Tomoe ; Miyabe, Yoshikatsu ; Yasui, Hajime ; Kinoshita, Yasunori ; Kishimura, Hideki
著者名 Furuta, Tomoe
著者名 Miyabe, Yoshikatsu
e-Rad_Researcher 00200494 著者名 Yasui, Hajime
著者名 Kinoshita, Yasunori
e-Rad_Researcher 50204855 著者名 Kishimura, Hideki
言語	英語
キーワード	ACE inhibitory activity
	antihypertension
	dulse
	Palmaria palmata
	phycobiliprotein
	primary structure
	recombinant protein
	red algae
発行日	2016-02
出版者	MDPI
収録物名	Marine Drugs
巻(号)	14(2)
ページ	UNSP 32
抄録	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.
資源タイプ	学術雑誌論文
出版タイプ	Version of Record
権利情報	Creative Commons Attribution 4.0 International
PISSN	1660-3397
NCID	AA1203626X
関連情報 (isIdenticalTo)	出版社版DOI https://doi.org/10.3390/md14020032