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Background <p>The 4-vinyl derivatives of various hydroxycinnamic acids are highly valued for their substantial application in the food and other industries. With growing demand for natural spice flavors, the nonoxidative decarboxylation of phenolic acid decarboxylase has attracted significant attention as a method for biosynthesizing 4-vinyl derivatives. This approach offers several advantages, such as mild reaction conditions, excellent substrate affinity, and high reaction efficiency.</p> Results <p>In this study, we successfully screened a new strain, <i>Bacillus sp</i>. QCS58, from among 40 marine bacteria for the first time. This strain harbors the phenolic acid decarboxylase gene. Subsequently, we cloned and overexpressed the phenolic acid decarboxylase BaPAD-Q58 from strain QCS58 in <i>Escherichia coli</i>. Enzymatic property assays revealed that BaPAD-Q58 exhibited enhanced stability in organic solvents and displayed optimal catalytic activity at pH 6.0 and 35&#xa0;°C. To improve the substrate affinity of BaPAD-Q58, we conducted tertiary structure prediction and molecular docking analysis to guide site-directed mutagenesis. Importantly, site-directed mutagenesis significantly improved the binding affinity between the phenolic acid decarboxylase and its substrate, as evidenced by a Km value of 0.51 ± 0.14 mM for the variant BaPAD-Q58<sub>F87Y</sub> with p-coumaric acid. Furthermore, within biphasic organic/aqueous reaction systems, the mutant BaPAD-Q58<sub>F87Y</sub> efficiently converted all available ferulic acids (100 mM) within a remarkably short period of 35&#xa0;min.</p> Conclusion <p>The mutant BsPAD-Q58<sub>F87Y</sub> demonstrates remarkable potential as an efficient catalyst for the bioconversion of hydroxycinnamic acids into vinyl phenol derivatives, underscoring its significance and applicability in biocatalysis.</p>

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Characterization and modification of phenolic acid decarboxylase from marine bacteria for the synthesis of 4-vinyl phenol derivatives

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年12月9日

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  • Liying Zhang,
  • Jihui Shen,
  • Mingjie Ren,
  • Yongbin Xu,
  • Shaolong Lin,
  • Surina Bao,
  • Lulu Wang,
  • Ruochen Fan,
  • Liming Jin,
  • Chunshan Quan

摘要

Background

The 4-vinyl derivatives of various hydroxycinnamic acids are highly valued for their substantial application in the food and other industries. With growing demand for natural spice flavors, the nonoxidative decarboxylation of phenolic acid decarboxylase has attracted significant attention as a method for biosynthesizing 4-vinyl derivatives. This approach offers several advantages, such as mild reaction conditions, excellent substrate affinity, and high reaction efficiency.

Results

In this study, we successfully screened a new strain, Bacillus sp. QCS58, from among 40 marine bacteria for the first time. This strain harbors the phenolic acid decarboxylase gene. Subsequently, we cloned and overexpressed the phenolic acid decarboxylase BaPAD-Q58 from strain QCS58 in Escherichia coli. Enzymatic property assays revealed that BaPAD-Q58 exhibited enhanced stability in organic solvents and displayed optimal catalytic activity at pH 6.0 and 35 °C. To improve the substrate affinity of BaPAD-Q58, we conducted tertiary structure prediction and molecular docking analysis to guide site-directed mutagenesis. Importantly, site-directed mutagenesis significantly improved the binding affinity between the phenolic acid decarboxylase and its substrate, as evidenced by a Km value of 0.51 ± 0.14 mM for the variant BaPAD-Q58F87Y with p-coumaric acid. Furthermore, within biphasic organic/aqueous reaction systems, the mutant BaPAD-Q58F87Y efficiently converted all available ferulic acids (100 mM) within a remarkably short period of 35 min.

Conclusion

The mutant BsPAD-Q58F87Y demonstrates remarkable potential as an efficient catalyst for the bioconversion of hydroxycinnamic acids into vinyl phenol derivatives, underscoring its significance and applicability in biocatalysis.