Factors affecting 2‐hydroxypropiophenone formation by benzoylformate decarboxylase from Pseudomonas putida

Benzoylformate (100 m M ) was quantitatively converted to the acyloin compound, 2‐hydroxypropiophenone (61.76 m M ) and benzaldehyde (38.2 m M ) by an enzyme extract from Pseudomonas putida ATCC 12633 in the presence of 1.6 M acetaldehyde. Biotransformations were carried out at pH 6.0 and 30°C with an incubation time of 60 min. Activity of the acyloin forming enzyme, benzoylformate decarboxylase, was 1.23 units/mL in the biotransformation mixture. Acyloin formation increased dramatically with pH in the range 4–5 and had a broad activity plateau in the pH range 5–8. A broad temperature optimum for acyloin formation was also observed in the range 20–40°C.