Related Experiment Video
Updated: May 7, 2026

Evaluation of the Effect of Growth Factors on Chlorophylls a and b Production from Microalgae
Published on: October 25, 2024
Chlorella is an effective dietary source of lutein for human erythrocytes
Taiki Miyazawa1, Kiyotaka Nakagawa, Fumiko Kimura
1Food and Biodynamic Chemistry Laboratory, Graduate School of Agricultural Science, Tohoku University.
Abstract:
Chlorella contains a high amount of carotenoids, especially lutein, and has received attention as a possible dietary source for improving carotenoid levels in human blood. In the present study, we performed a 2-month single arm human study, and investigated the efficacy of Chlorella supplementation (9 g Chlorella/day; equivalent to 32 mg lutein/day) on lutein and other carotenoid concentrations in plasma as well as erythrocytes of 12 healthy subjects. Following Chlorella supplementation, lutein was the predominant carotenoid in erythrocytes, showing a 4-fold increase (from 14 to 54 pmol/mL packed cells). After the one month without Chlorella ingestion, erythrocyte lutein then decreased to a basal level (17 pmol/mL packed cells). Erythrocyte carotenoid (lutein, zeaxanthin, α-carotene, and β-carotene) levels were proportional to plasma carotenoid levels. The results suggest the transfer of Chlorella carotenoids, especially lutein, from plasma lipoprotein particles to the erythrocyte membrane. Chlorella intake would be effective for improving and maintaining lutein concentrations in human erythrocytes.
Related Concept Videos
Erythropoiesis
Channel Rhodopsins
Rhodopsins belong to the family of cell surface proteins called G-protein coupled receptors,...
Protein Transport to the Stroma
Protein complexes called the translocon of the outer chloroplast membrane or TOC complex, and the translocon of the inner chloroplast membrane or TIC complex mediate the...
Protein Transport to the Outer Chloroplast Membrane
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
Diversity of Protists I
Protein Transport to the Thylakoids

