Premium
Factors affecting 2‐hydroxypropiophenone formation by benzoylformate decarboxylase from Pseudomonas putida
Author(s) -
Wilcocks R.,
Ward O. P.
Publication year - 1992
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260391010
Subject(s) - pseudomonas putida , biotransformation , chemistry , acetaldehyde , benzaldehyde , enzyme , chromatography , organic chemistry , catalysis , ethanol
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.