Premium
Structural characteristics of phycobiliproteins from red alga Mazzaella japonica
Author(s) -
Kitade Yumi,
Miyabe Yoshikatsu,
Yamamoto Yohei,
Takeda Hirohumi,
Shimizu Takeshi,
Yasui Hajime,
Kishimura Hideki
Publication year - 2018
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/jfbc.12436
Subject(s) - phycobiliprotein , allophycocyanin , phycocyanin , japonica , biochemistry , hydrolysate , chemistry , phycoerythrin , algae , cyanobacteria , biology , botany , microbiology and biotechnology , hydrolysis , bacteria , flow cytometry , genetics
We determined the primary structures of phycoerythrin (PE), phycocyanin (PC), and allophycocyanin (APC) from red alga Mazzaella japonica . The phycobiliproteins consist of α‐ and β‐subunits like other red algae. M. japonica phycobiliproteins all conserved Cys residues for chromophore attachment site. The amino acid sequences of M. japonica phycobiliproteins showed considerably high identities with those of other red algae (81–100%). In addition, the sequences (YRD, LDY, LRY, VY, LF, and FY), which were angiotensin I converting enzyme (ACE) inhibitory peptides from other algae were detected in the primary structures of M. japonica phycobiliproteins. Then, we prepared the protein hydrolysates from M. japonica and measured its ACE inhibitory activity. Consequently, M. japonica protein hydrolysates indicated considerably high ACE inhibitory activity. Practical applications M. japonica is an abundant resource in Japan, which contains a lot of phycobiliproteins. Then, M. japonica protein hydrolysates strongly inhibited the activity of ACE. Therefore, it has the potential to be an ingredient of functional food.