Structural characteristics of phycobiliproteins from red alga <italic>Mazzaella japonica</italic>.

Abstract: We determined the primary structures of phycoerythrin (PE), phycocyanin (PC), and allophycocyanin (APC) from red alga <italic>Mazzaella japonica</italic>. The phycobiliproteins consist of α‐ and β‐subunits like other red algae. <italic>M. japonica</italic> phycobiliproteins all conserved Cys residues for chromophore attachment site. The amino acid sequences of <italic>M. japonica</italic> 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 <italic>M. japonica</italic> phycobiliproteins. Then, we prepared the protein hydrolysates from <italic>M. japonica</italic> and measured its ACE inhibitory activity. Consequently, <italic>M. japonica</italic> protein hydrolysates indicated considerably high ACE inhibitory activity. Practical applications: <italic>M. japonica</italic> is an abundant resource in Japan, which contains a lot of phycobiliproteins. Then, <italic>M. japonica</italic> protein hydrolysates strongly inhibited the activity of ACE. Therefore, it has the potential to be an ingredient of functional food. [ABSTRACT FROM AUTHOR]