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Background <p>Phenolic acid decarboxylase (PAD) is an enzyme capable of catalyzing the nonoxidative decarboxylation of phenolic acids, yielding the corresponding 4-vinyl derivatives. This enzymatic process holds considerable promise for converting naturally abundant phenolic acid substrates into high-value compounds.</p> Results <p>The PAD gene from <i>Bacillus subtilis</i> J6 was cloned to yield the BJ6PAD enzyme, and its mutant BJ6PAD-N was generated by introducing an N-terminal substitution. Compared with BJ6PAD, BJ6PAD-N demonstrated not only higher specific enzyme activity but also increased alkaline resistance. The N-terminal region of BJ6PAD-N exhibited increased flexibility, leading to a looser structure. This change improved the catalytic efficiency for sinapic acid (SA) with bulky side chains. After its immobilization, the application potential of BJ6PAD-N was significantly enhanced, demonstrating reusability and storage stability that were superior to those of BJ6PAD. After 10 repeated uses, the residual enzyme activity remained above 80%. When stored at 4&#xa0;°C for 60 days, 61.15% of the enzyme activity was retained. These characteristics are crucial for facilitating the industrial application of enzymes.</p> Conclusions <p>Replacing the N-terminal of phenolic acid decarboxylase BJ6PAD (resulting in BJ6PAD-N) made the enzyme structure more flexible. While this reduced substrate binding stability, it increased specific enzyme activity. Notably, the enzyme showed improved catalytic efficiency for sinapic acid, which has a bulky side chain. After being immobilized, the performance stability of the enzyme has been further enhanced.</p>

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Enhancing the characteristics of phenolic acid decarboxylase via N-terminal substitution and investigating its immobilization

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年11月28日

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  • Qin Li,
  • Yinzhu Chen,
  • Hongmei Zhao,
  • Yu Cheng,
  • Kaidi Hu,
  • Jianlong Li,
  • Aiping Liu,
  • Ning Zhao,
  • Li He,
  • Yong Yang,
  • Shuliang Liu

摘要

Background

Phenolic acid decarboxylase (PAD) is an enzyme capable of catalyzing the nonoxidative decarboxylation of phenolic acids, yielding the corresponding 4-vinyl derivatives. This enzymatic process holds considerable promise for converting naturally abundant phenolic acid substrates into high-value compounds.

Results

The PAD gene from Bacillus subtilis J6 was cloned to yield the BJ6PAD enzyme, and its mutant BJ6PAD-N was generated by introducing an N-terminal substitution. Compared with BJ6PAD, BJ6PAD-N demonstrated not only higher specific enzyme activity but also increased alkaline resistance. The N-terminal region of BJ6PAD-N exhibited increased flexibility, leading to a looser structure. This change improved the catalytic efficiency for sinapic acid (SA) with bulky side chains. After its immobilization, the application potential of BJ6PAD-N was significantly enhanced, demonstrating reusability and storage stability that were superior to those of BJ6PAD. After 10 repeated uses, the residual enzyme activity remained above 80%. When stored at 4 °C for 60 days, 61.15% of the enzyme activity was retained. These characteristics are crucial for facilitating the industrial application of enzymes.

Conclusions

Replacing the N-terminal of phenolic acid decarboxylase BJ6PAD (resulting in BJ6PAD-N) made the enzyme structure more flexible. While this reduced substrate binding stability, it increased specific enzyme activity. Notably, the enzyme showed improved catalytic efficiency for sinapic acid, which has a bulky side chain. After being immobilized, the performance stability of the enzyme has been further enhanced.