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ALD5, PAD1, ATF1 and ATF2 facilitate the catabolism of coniferyl aldehyde, ferulic acid and p-coumaric acid in Saccharomyces cerevisiae

Peter Temitope Adeboye (Institutionen för biologi och bioteknik, Industriell bioteknik) ; Maurizio Bettiga (Institutionen för biologi och bioteknik, Industriell bioteknik) ; Lisbeth Olsson (Institutionen för biologi och bioteknik, Industriell bioteknik)
Scientific Reports (2045-2322). Vol. 7 (2017),
[Artikel, refereegranskad vetenskaplig]

The ability of Saccharomyces cerevisiae to catabolize phenolic compounds remains to be fully elucidated. Conversion of coniferyl aldehyde, ferulic acid and p-coumaric acid by S. cerevisiae under aerobic conditions was previously reported. A conversion pathway was also proposed. In the present study, possible enzymes involved in the reported conversion were investigated. Aldehyde dehydrogenase Ald5, phenylacrylic acid decarboxylase Pad1, and alcohol acetyltransferases Atf1 and Atf2, were hypothesised to be involved. Corresponding genes for the four enzymes were overexpressed in a S. cerevisiae strain named APT_1. The ability of APT_1 to tolerate and convert the three phenolic compounds was tested. APT_1 was also compared to strains B_CALD heterologously expressing coniferyl aldehyde dehydrogenase from Pseudomonas, and an ald5 Delta strain, all previously reported. APT_1 exhibited the fastest conversion of coniferyl aldehyde, ferulic acid and p-coumaric acid. Using the intermediates and conversion products of each compound, the catabolic route of coniferyl aldehyde, ferulic acid and p-coumaric acid in S. cerevisiae was studied in greater detail.



Denna post skapades 2017-03-22. Senast ändrad 2017-06-12.
CPL Pubid: 248641

 

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Institutioner (Chalmers)

Institutionen för biologi och bioteknik, Industriell bioteknik

Ämnesområden

Organisk kemi
Mikrobiologi

Chalmers infrastruktur