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<p>C-phycocyanin (C-PC), a blue protein pigment found in cyanobacteria, has potential properties for use in food and medical applications, including antioxidants, antimicrobial, and anti-inflammatory. Generally, C-PC is extracted from mesophilic cyanobacteria, such as <i>Arthrospira platensis</i>, which is unstable under high-temperature conditions. Therefore, thermophilic cyanobacteria represent potential sources of thermostable C-PC. This study aimed to produce a holo-C-PC alpha subunit (holo-CpcA) from the thermophilic cyanobacterium <i>Thermosynechococcus</i> sp. TUBT-T01 by reconstituting the pathway in <i>Escherichia coli</i>. The constructed expression plasmid was designed with a polycistronic transcription unit containing <i>ho1</i>, <i>pcyA</i>, <i>cpcE</i>, and <i>cpcF</i> inserted into pET3a. Together with the pET28a carrying <i>cpcA</i> gene, two plasmids were co-transformed and co-expressed in <i>E. coli</i> Rosetta (DE3). Following induction, the cell pellet exhibited a visible color change, suggesting successful expression of the C-PC alpha subunit. The antioxidant activity of crude holo-CpcA was analyzed; it showed higher antioxidant activity compared to crude apo-CpcA in both the ABTS radical cation decolorization assay and the ORAC-Fluorescein Assay. This study reported the successful heterologous production of holo-CpcA from <i>Thermosynechococcus</i> sp. in <i>E. coli</i>, and the protein also demonstrated antioxidant activities.</p>

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Heterologous Reconstitution of the Biosynthesis Pathway for Producing Holo-C-Phycocyanin Alpha Subunit (CpcA) from Thermosynechococcus sp. TUBT-T01

  • 期刊论文

  • 发表日期：

    2025年10月30日

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  • Wipawee Sritusnee,
  • Sichon Kachayangyuen,
  • Khanittha Kumnueng,
  • Preeyaphat Sukdaeng,
  • Theppanya Charoenrat,
  • Supenya Chittapun,
  • Plaipol Dedvisitsakul,
  • Chanitchote Piyapittayanun

摘要

C-phycocyanin (C-PC), a blue protein pigment found in cyanobacteria, has potential properties for use in food and medical applications, including antioxidants, antimicrobial, and anti-inflammatory. Generally, C-PC is extracted from mesophilic cyanobacteria, such as Arthrospira platensis, which is unstable under high-temperature conditions. Therefore, thermophilic cyanobacteria represent potential sources of thermostable C-PC. This study aimed to produce a holo-C-PC alpha subunit (holo-CpcA) from the thermophilic cyanobacterium Thermosynechococcus sp. TUBT-T01 by reconstituting the pathway in Escherichia coli. The constructed expression plasmid was designed with a polycistronic transcription unit containing ho1, pcyA, cpcE, and cpcF inserted into pET3a. Together with the pET28a carrying cpcA gene, two plasmids were co-transformed and co-expressed in E. coli Rosetta (DE3). Following induction, the cell pellet exhibited a visible color change, suggesting successful expression of the C-PC alpha subunit. The antioxidant activity of crude holo-CpcA was analyzed; it showed higher antioxidant activity compared to crude apo-CpcA in both the ABTS radical cation decolorization assay and the ORAC-Fluorescein Assay. This study reported the successful heterologous production of holo-CpcA from Thermosynechococcus sp. in E. coli, and the protein also demonstrated antioxidant activities.