A system for the production of high value chemicals includes (a) an input selected from the group consisting of ethylene glycol, glycerol, ethanol methanol or a combination thereof. In addition, the system includes (b) an oxidation biocatalyst including an alcohol oxidase, a copper radical oxidase, a glycerol oxidase, an alditol oxidase or a combination thereof. Further, the system includes (c) an oxidized intermediate. The system also includes (d) a finishing catalyst including a supported metal catalyst, a carboligating catalyst, an amine oxidase, a glyoxalase, an acid catalyst, a base catalyst, an isomerization catalyst or a combination thereof. Still further, the system includes (e) an output.

The present invention relates to new methylglyoxal reductase (MGR) enzymes which are useful for efficiently converting methylglyoxal into hydroxyacetone. The invention more particularly relates to a method for efficiently converting methylglyoxal into hydroxyacetone using said enzymes, to a method for producing 1,2-propanediol using a microorganism overexpressing said enzymes, and to said microorganism.

The present invention relates to new lactaldehyde reductase (LAR) enzymes useful for the production of 1,2-propanediol and to microorganisms overexpressing said enzymes. The invention also relates to a method for producing 1,2-propanediol by converting lactaldehyde into 1,2-propanediol with said enzymes.

The present invention relates to new methylglyoxal reductase (MGR) enzymes which are useful for efficiently converting methylglyoxal into hydroxyacetone. The invention more particularly relates to a method for efficiently converting methylglyoxal into hydroxyacetone using said enzymes, to a method for producing 1,2-propanediol using a microorganism overexpressing said enzymes, and to said microorganism.

The invention relates to a cell capable of converting one or more pentose sugar and one or more hexose sugar into fermentation product constitutively expressing one or more heterologous or homologous polypeptide having the amino acid sequence set out in SEQ ID NO: 20, or a variant polypeptide thereof having at least 45% identity to SEQ ID NO 20. In an embodiment the heterologous polypeptide has glyoxalase activity.

The invention relates to a cell capable of converting one or more pentose sugar and one or more hexose sugar into fermentation product constitutively expressing one or more heterologous or homologous polypeptide having the amino acid sequence set out in SEQ ID NO: 20, or a variant polypeptide thereof having at least 45% identity to SEQ ID NO 20. In an embodiment the heterologous polypeptide has glyoxalase activity.

The invention relates to a cell capable of converting one or more pentose sugar and one or more hexose sugar into fermentation product constitutively expressing one or more heterologous or homologous polypeptide having the amino acid sequence set out in SEQ ID NO: 20, or a variant polypeptide thereof having at least 45% identity to SEQ ID NO 20. In an embodiment the heterologous polypeptide has glyoxalase activity.

The invention relates to a cell capable of converting one or more pentose sugar and one or more hexose sugar into fermentation product constitutively expressing one or more heterologous or homologous polypeptide having the amino acid sequence set out in SEQ ID NO: 20, or a variant polypeptide thereof having at least 45% identity to SEQ ID NO 20. In an embodiment the heterologous polypeptide has glyoxalase activity.

The present invention relates to new lactaldehyde reductase (LAR) enzymes useful for the production of 1,2-propane-diol and to microorganisms overexpressing said enzymes. The invention also relates to a method for producing 1,2-propanediol by converting lactaldehyde into 1,2-propanediol with said enzymes.

The present invention relates to the use of GLO1 to modulate acetic acid tolerance in yeast. More specifically, it relates to the use of a specific GLO1 allele to confer tolerance to acetic acid, and to improve the fermentation performance of yeast in the presence of acetic acid.