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- Title
Efficient enzymatic production of benzaldehyde from l-phenylalanine with a mutant form of 4-hydroxymandelate synthase.
- Authors
Yasuaki Takakura; Takuto Ono; Keiko Danjo; Hiroyuki Nozaki
- Abstract
Benzaldehyde is an organic compound with an almond-like aroma and one of the most important and widely used flavorings in the food industry. To develop an enzymatic process for the production of benzaldehyde from l-phenylalanine, four enzymes were expressed in Escherichia coli; l-amino acid deaminase, 4-hydroxymandelate synthase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase. Although each E. coli strain could be used to synthesize benzaldehyde from l-phenylalanine, the yield was low due to the accumulation of an intermediate, phenylpyruvic acid. We developed a second reaction step by engineering 4-hydroxymandelate synthase of Actinoplanes teichomyceticus. A quadruple mutant of 4-hydroxymandelate synthase (A199V/Q206R/I217V/K337Q) obtained by random and site-directed mutagenesis demonstrated 2.4-fold higher activity than wild type. Furthermore, the mutant-expressing strain was able to produce benzaldehyde from 100 mm l-phenylalanine at a conversion rate of 84% (wild type, 37%). We report the development of an efficient process for benzaldehyde production using l-phenylalanine as a substrate.
- Subjects
ESCHERICHIA coli; PHENYLALANINE; BENZALDEHYDE; SITE-specific mutagenesis; ORGANIC compounds; MANUFACTURING processes
- Publication
Bioscience, Biotechnology & Biochemistry, 2022, Vol 86, Issue 12, p1718
- ISSN
0916-8451
- Publication type
Article
- DOI
10.1093/bbb/zbac162