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<p>Zeaxanthin, a vital carotenoid, is synthesized through a series of enzymatic reactions, with β-carotene hydroxylase serving as a key rate-limiting enzyme facilitating the conversion of β-carotene to zeaxanthin. This study aimed to investigate the feasibility of cloning and transferring the β-carotene hydroxylase gene (<i>LpcrtR</i>) from <i>Limnospira platensis</i> into <i>Escherichia coli</i> for the efficient production of zeaxanthin. Firstly, the <i>LpcrtR</i> gene was successfully extracted from the <i>L. platensis</i> genome, which contains 906 base pairs and encodes 301 amino acids. Through comparison, it was found that the LpCRTR protein shares high amino acid sequence homology with β-carotene hydroxylases from different species and possesses the "HXXXXH" and "HXXHH" motif structures. After constructing the gene expression vector pGEX-6p-1-<i>LpcrtR</i>, the recombinant plasmid was transformed into <i>E. coli</i>. The results of SDS-PAGE and Western blotting validated the expression of the <i>LpcrtR</i> protein (LpCRTR) in the bacterial system. Additionally, HPLC results revealed that LpCRTR can partially catalyze the conversion of β-carotene to zeaxanthin within <i>E. coli</i>. Notably, the zeaxanthin and β-carotene yield in recombinant <i>E. coli</i> were 81.7 ± 0.4% and 14.7 ± 0.6%, respectively. Therefore, this study has successfully identified a novel β-carotene hydroxylase gene, providing an efficient pathway for achieving high zeaxanthin accumulation in genetically engineered bacteria.</p>

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Identification of β-carotene hydroxylase gene from Limnospira platensis: expression in Escherichia coli for the production of zeaxanthin

  • 期刊论文

  • 发表日期：

    2026年4月2日

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  • Zhen-Wei Shi,
  • Liu-Yu Jian,
  • Jun Ma,
  • Xue-Fu Li,
  • Li-Jie Peng,
  • Di-Feng Ren

摘要

Zeaxanthin, a vital carotenoid, is synthesized through a series of enzymatic reactions, with β-carotene hydroxylase serving as a key rate-limiting enzyme facilitating the conversion of β-carotene to zeaxanthin. This study aimed to investigate the feasibility of cloning and transferring the β-carotene hydroxylase gene (LpcrtR) from Limnospira platensis into Escherichia coli for the efficient production of zeaxanthin. Firstly, the LpcrtR gene was successfully extracted from the L. platensis genome, which contains 906 base pairs and encodes 301 amino acids. Through comparison, it was found that the LpCRTR protein shares high amino acid sequence homology with β-carotene hydroxylases from different species and possesses the "HXXXXH" and "HXXHH" motif structures. After constructing the gene expression vector pGEX-6p-1-LpcrtR, the recombinant plasmid was transformed into E. coli. The results of SDS-PAGE and Western blotting validated the expression of the LpcrtR protein (LpCRTR) in the bacterial system. Additionally, HPLC results revealed that LpCRTR can partially catalyze the conversion of β-carotene to zeaxanthin within E. coli. Notably, the zeaxanthin and β-carotene yield in recombinant E. coli were 81.7 ± 0.4% and 14.7 ± 0.6%, respectively. Therefore, this study has successfully identified a novel β-carotene hydroxylase gene, providing an efficient pathway for achieving high zeaxanthin accumulation in genetically engineered bacteria.