A coniferyl aldehyde dehydrogenase gene from Pseudomonas sp. strain HR199 enhances the conversion of coniferyl aldehyde by Saccharomyces cerevisiae

Bioresour Technol. 2016 Jul;212:11-19. doi: 10.1016/j.biortech.2016.04.003. Epub 2016 Apr 5.


The conversion of coniferyl aldehyde to cinnamic acids by Saccharomyces cerevisiae under aerobic growth conditions was previously observed. Bacteria such as Pseudomonas have been shown to harbor specialized enzymes for converting coniferyl aldehyde but no comparable enzymes have been identified in S. cerevisiae. CALDH from Pseudomonas was expressed in S. cerevisiae. An acetaldehyde dehydrogenase (Ald5) was also hypothesized to be actively involved in the conversion of coniferyl aldehyde under aerobic growth conditions in S. cerevisiae. In a second S. cerevisiae strain, the acetaldehyde dehydrogenase (ALD5) was deleted. A prototrophic control strain was also engineered. The engineered S. cerevisiae strains were cultivated in the presence of 1.1mM coniferyl aldehyde under aerobic condition in bioreactors. The results confirmed that expression of CALDH increased endogenous conversion of coniferyl aldehyde in S. cerevisiae and ALD5 is actively involved with the conversion of coniferyl aldehyde in S. cerevisiae.

Keywords: Coniferyl aldehyde; Lignocellulose conversion; Phenolics conversion; Phenolics tolerance; Saccharomyces cerevisiae.

MeSH terms

  • Acrolein / analogs & derivatives*
  • Acrolein / metabolism
  • Aldehyde Oxidoreductases / genetics*
  • Aldehyde Oxidoreductases / metabolism
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism
  • Organisms, Genetically Modified / metabolism
  • Pseudomonas / enzymology
  • Pseudomonas / genetics*
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism*


  • Bacterial Proteins
  • coniferaldehyde
  • Acrolein
  • Aldehyde Oxidoreductases
  • coniferyl aldehyde dehydrogenase
  • aldehyde dehydrogenase (NAD(P)+)