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STRUCTURAL PROPERTIES OF PHYCOERYTHRIN FROM DULSE PALMARIA PALMATA

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Title: STRUCTURAL PROPERTIES OF PHYCOERYTHRIN FROM DULSE PALMARIA PALMATA
Authors: Miyabe, Yoshikatsu Browse this author
Furuta, Tomoe Browse this author
Takeda, Tomoyuki Browse this author
Kanno, Gaku Browse this author
Shimizu, Takeshi Browse this author
Tanaka, Yoshikazu Browse this author
Gai, Zuoqi Browse this author
Yasui, Hajime Browse this author
Kishimura, Hideki Browse this author
Keywords: Red alga
Dulse
Palmaria palmata
ACE inhibitory activity
phycoerythrin
Primary structure
3-D structure
Issue Date: Feb-2017
Publisher: John Wiley & Sons
Journal Title: Journal of food biochemistry
Volume: 41
Issue: 1
Start Page: UNSP e12301
Publisher DOI: 10.1111/jfbc.12301
Abstract: We found that the red alga dulse (Palmaria palmata) contains a lot of proteins, which is mainly composed of phycoerythrin (PE) and the protein hydrolysates showed high angiotensin I converting enzyme (ACE) inhibitory activities. Therefore, we investigated the structure of dulse PE to discuss its structure-function relationship. We prepared the chloroplast DNA and analyzed the nucleotide sequences encoding PE by cDNA cloning method. It was clarified that dulse PE has alpha- and beta-subunits and they are composed by 164 amino acids (MW: 17,638) and 177 amino acids (MW: 18,407), respectively. The dulse PE contained conserved cysteine residues for chromophore attachment site. On the alignment of amino acid sequences of dulse PE with those of other red algal PE, the sequence identities were very high (81-92%). In addition, we purified and crystallized the dulse PE, and its crystal structure was determined at 2.09 angstrom resolution by molecular replacement method. The revealed 3D structure of dulse PE which forms an (alpha beta)(6) hexamer was similar to other red algal PEs. Conversely, it was clarified that the dulse PE proteins are rich in hydrophobic amino acid residues (51.0%), especially aromatic amino acid and proline residues. The data imply that the high ACE inhibitory activity of dulse protein hydrolysates would be caused by the specific amino acid composition and sequence of dulse PE.
Rights: This is the peer reviewed version of the following article: UNSP e12301-Journal of food biochemistry, 2017-02, 41(1) UNSP e12301-, which has been published in final form at DOI: 10.1111/jfbc.12301. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.
Type: article (author version)
URI: http://hdl.handle.net/2115/68247
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)

Submitter: 岸村 栄毅

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