open access

https://hdl.handle.net/2115/68247

STRUCTURAL PROPERTIES OF PHYCOERYTHRIN FROM DULSE PALMARIA PALMATA

英語

3-D structure

2017-02

John Wiley & Sons

Journal of food biochemistry

41(1)

UNSP e12301

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.

学術雑誌論文

Accepted Manuscript

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.

0145-8884

1745-4514

AA00698223