ArticleBMC biotechnology2025
Enhancing the characteristics of phenolic acid decarboxylase via N-terminal substitution and investigating its immobilization.
Article in BMC biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
backgroundPhenolic 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.
resultsThe 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.
conclusionsReplacing 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.
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