Enzymatic Kolbe–Schmitt reaction to form salicylic acid from phenol: Enzymatic characterization and gene identification of a novel enzyme, Trichosporon moniliiforme salicylic acid decarboxylase

• Published in: Biochemical and biophysical research communications 2010-04, Vol.394 (2), p.279-284
• Main Authors: Kirimura, Kohtaro, Gunji, Hiroaki, Wakayama, Rumiko, Hattori, Takasumi, Ishii, Yoshitaka
• Format: Article
• Language: English
• Subjects: Carboxy-Lyases - chemistry; Carboxy-Lyases - genetics; Carboxy-Lyases - isolation & purification; Enzymatic Kolbe–Schmitt reaction; Escherichia coli; Escherichia coli - enzymology; Escherichia coli - genetics; Oxygen - chemistry; Phenol - chemistry; Phenol - metabolism; Reversible decarboxylase; Salicylic Acid - chemical synthesis; Salicylic Acid - metabolism; Salicylic acid decarboxylase; Selective production; Trichosporon; Trichosporon - enzymology; Trichosporon - genetics; Trichosporon moniliiforme
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2010.02.154

Salicylic acid decarboxylase (Sdc) can produce salicylic acid from phenol; it was found in the yeast Trichosporon moniliiforme WU-0401 and was for the first time enzymatically characterized, with the sdc gene heterologously expressed. Sdc catalyzed both reactions: decarboxylation of salicylic acid to phenol and the carboxylation of phenol to form salicylic acid without any byproducts. Both reactions were detected without the addition of any cofactors and occurred even in the presence of oxygen, suggesting that this Sdc is reversible, nonoxidative, and oxygen insensitive. Therefore, it is readily applicable in the selective production of salicylic acid from phenol, the enzymatic Kolbe–Schmitt reaction. The deduced amino acid sequence of the gene, sdc, encoding Sdc comprises 350 amino acid residues corresponding to a 40-kDa protein. The recombinant Escherichia coli BL21(DE3) expressing sdc converted phenol to salicylic acid with a 27% (mol/mol) yield at 30 °C for 9 h.