Horst Priefert
University of Münster
32 Papers
94 Citations
Horst Priefert is an academic researcher from University of Münster. The author has contributed to research in topics: Ferulic acid & Vanillin. The author has an hindex of 17, co-authored 32 publications. Previous affiliations of Horst Priefert include University of Göttingen & Massachusetts Institute of Technology.
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Papers
Highly Efficient Biotransformation of Eugenol to Ferulic Acid and Further Conversion to Vanillin in Recombinant Strains of Escherichia coli
TL;DR: The genes ehyAB, encoding eugenol hydroxylase of Pseudomonas sp.
131
Potential of Rhodococcus strains for biotechnological vanillin production from ferulic acid and eugenol
Rainer Plaggenborg,Jörg Overhage,Andrea Loos,John A. C. Archer,Philip A. Lessard,Anthony J. Sinskey,Alexander Steinbüchel,Horst Priefert +7 more
TL;DR: Investigation of two Rhodococcus strains for biotechnological vanillin production from ferulic acid and eugenol suggested that genetically engineered strains of I24 and PD630 are suitable candidates for vanillinProduction from Eugenol.
119
Identification and molecular characterization of the Alcaligenes eutrophus H16 aco operon genes involved in acetoin catabolism.
TL;DR: The occurrence of a new enzyme type for the degradation of acetoin is discussed, and significant homologies to the primary structures of the dehydrogenase components of various 2-oxo acid dehydrogenases complexes are exhibited.
66
Harnessing eugenol as a substrate for production of aromatic compounds with recombinant strains of Amycolatopsis sp. HR167.
TL;DR: To harness eugenol as cheap substrate for the biotechnological production of aromatic compounds, the vanillyl alcohol oxidase gene (vaoA) from Penicillium simplicissimum CBS 170.90 was cloned in an expression vector suitable for Gram- positive bacteria and expressed in the vanillin-tolerant Gram-positive strain Amycolatopsis sp.
59
Identification and molecular characterization of the gene coding for acetaldehyde dehydrogenase II (acoD) of Alcaligenes eutrophus.
TL;DR: The N-terminal amino acid sequence of purified acetaldehyde dehydrogenase II from ethanol-grown cells of Alcaligenes eutrophus was determined and was identified and was preceded by a sequence which exhibited a striking homology to the enterobacterial sigma 54-dependent promoter consensus sequence.
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