Decarboxylation of Sorbic Acid by Spoilage Yeasts Is Associated with the PAD1 Gene

Abstract

The spoilage yeast Saccharomyces cerevisiae degraded the food preservative sorbic acid (2,4-hexadienoic acid) to a volatile hydrocarbon, identified by gas chromatography mass spectrometry as 1,3-pentadiene. The gene responsible was identified as PAD1, previously associated with the decarboxylation of the aromatic carboxylic acids cinnamic acid, ferulic acid, and coumaric acid to styrene, 4-vinylguaiacol, and 4-vinylphenol, respectively. The loss of PAD1 resulted in the simultaneous loss of decarboxylation activity against both sorbic and cinnamic acids. Pad1p is therefore an unusual decarboxylase capable of accepting both aromatic and aliphatic carboxylic acids as substrates. All members of the Saccharomyces genus (sensu stricto) were found to decarboxylate both sorbic and cinnamic acids. PAD1 homologues and decarboxylation activity were found also in Candida albicans, Candida dubliniensis, Debaryomyces hansenii, and Pichia anomala. The decarboxylation of sorbic acid was assessed as a possible mechanism of resistance in spoilage yeasts. The decarboxylation of either sorbic or cinnamic acid was not detected for Zygosaccharomyces, Kazachstania (Saccharomyces sensu lato), Zygotorulaspora, or Torulaspora, the genera containing the most notorious spoilage yeasts. Scatter plots showed no correlation between the extent of sorbic acid decarboxylation and resistance to sorbic acid in spoilage yeasts. Inhibitory concentrations of sorbic acid were almost identical for S. cerevisiae wild-type and ⌬pad1 strains. We concluded that Pad1p-mediated sorbic acid decarboxylation did not constitute a significant mechanism of resistance to weak-acid preservatives by spoilage yeasts, even if the decarboxylation contributed to spoilage through the generation of unpleasant odors.

Requirement of a Functional Flavin Mononucleotide Prenyltransferase for the Activity of a Bacterial Decarboxylase in a Heterologous Muconic Acid Pathway in Saccharomyces cerevisiae

“…For this reason, many loss-of-function mutations were acquired in PAD1 or FDC1 in strains used for wine or beer production during their domestication (17,25). In a variety of other yeast species (e.g., Kluyveromyces marxianus or Yarrowia lipolytica), no Pad1 homologues can be found and, consistently, these species are not able to decarboxylate phenylacrylic acids (26). However, in most laboratory strains of S. cerevisiae, intact copies of FDC1 and PAD1 are present (25).…”

Adaptive Response and Tolerance to Weak Acids inSaccharomyces cerevisiae: A Genome-Wide View

“…and sorbic acid) was related with its ability to use these weak acids as carbon sources, even in the presence of glucose Sousa et al, 1998;Stratford et al, 2007). Interestingly, no induction of a Pdr12p-like protein was observed in Z. bailii cells challenged with sorbic acid (Papadimitriou et al, 2007), strongly indicating that the key role played by the Pdr12p-War1p axis in S. cerevisiae resistance is not operating in this species.…”

The Weak-Acid Preservative Sorbic Acid Is Decarboxylated and Detoxified by a Phenylacrylic Acid Decarboxylase, PadA1, in the Spoilage Mold Aspergillus niger

“…We have shown recently that S. cerevisiae Pad1p, an enzyme that has been shown previously to decarboxylate cinnamic acid to styrene (5), facilitates the decarboxylation of sorbic acid to the volatile compound 1,3-pentadiene (17). Although several mold species have been shown to degrade sorbic acid to 1,3-pentadiene, the gene(s) and the enzyme(s) that facilitate this degradation were unknown.…”