Journal
ENZYME AND MICROBIAL TECHNOLOGY
Volume 113, Issue -, Pages 37-43Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.enzmictec.2018.02.008
Keywords
Benzoic acid decarboxylase; Enzymatic decarboxylation; Enzymatic carboxylation; Substrate profile
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Funding
- National Natural Science Foundation of China [21472232]
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Reversible benzoic acid decarboxylases are versatile biocatalysts by taking advantage of both decarboxylation and carboxylation reactions, especially for the biocatalytic Kolbe-Schmitt reaction. In the course of developing a benzoic acid decarboxylase tool-box, a putative benzoic acid decarboxylase gene from Fusarium oxysporum was heterologously over-expressed in Escherichia coli, the recombinant protein was purified and characterized. The purified enzyme exhibited relatively high catalytic efficiencies for the decarboxylation of 2, 3-dihydroxybenzoic acid and carboxylation of catechol (k(cat)/K-m. = 2.03 x 102 and 1.88 mM(-1) min(-1), respectively), and thus characterized as 2, 3-dihydroxybenzoic acid decarboxylase (2, 3-DHBD_Fo). The enzyme also catalyzed the decarboxylation of various substituted salicylic acids with different groups at varied positions except 5-position and the carboxylation of phenol and the substituted phenols. In a preparative reaction, catechol was carboxylated into 2, 3-dihydroxybenoic acid with 95% conversion by adding dodecyldimethylbenzylammonium chloride into the reaction system, and the product was isolated in 72% yield. These results demonstrate that 2, 3DHBD_Fo is a valuable addition to the benzoic acid decarboxylase tool-box with potential practical applications.
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