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Purification and characterization of two novel angiotensin I-converting enzyme inhibitory peptides derived from R-phycoerythrin of red algae (Bangia fusco-purpurea)

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Abstract

R-phycoerythrin prepared from red algae (Bangia fusco-purpurea) was hydrolyzed by pepsin followed by trypsin to produce angiotensin I-converting enzyme (ACE) inhibitory peptides. The IC50 of the hydrolysate of R-phycoerythrin (HRPE) was 191.1 ± 4.1 μg/mL, and the molecular weight of most products (89.9 %) was below 2 kDa. After sequential gel permeation and reversed-phase chromatography steps to purify the hydrolysate, two peptides with the sequences of ALLAGDPSVLEDR and VVGGTGPVDEWGIAGAR were obtained and their IC50 values were 57.2 ± 5.0 and 66.2 ± 4.2 μg/mL, respectively. The ALLAGDPSVLEDR and VVGGTGPVDEWGIAGAR peptides were derived from the β- and α-subunit of R-phycoerythrin from Polysiphonia urceolata, with a 92.3 % (12/13) and 94.1 % (16/17) match, respectively. Both peptides were resistant to digestion by proteinases common in the gastrointestinal tract. Therefore, the identified novel peptides derived from R-phycoerythrin may be used as potential nutraceuticals for development of functional foods.

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Acknowledgments

This study was sponsored by the National Natural Scientific Foundation of China (Nos. 31271838, 31471640), the Key Project of the Ministry of Science and Technology of China (2012BAD38B09), the Public Science and Technology Research Fund Project of Ocean (201305015-3), and the Science and Technology Bureau of Xiamen (3502Z20133020). We thank Professor Qi-Xin Zhong in the University of Tennessee for critical reviewing of the manuscript.

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Correspondence to Min-Jie Cao.

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Wu, Q., Cai, QF., Yoshida, A. et al. Purification and characterization of two novel angiotensin I-converting enzyme inhibitory peptides derived from R-phycoerythrin of red algae (Bangia fusco-purpurea). Eur Food Res Technol 243, 779–789 (2017). https://doi.org/10.1007/s00217-016-2792-z

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