The invention provides a method for producing a terpene or a precursor thereof by microbial fermentation. Typically, the method involves culturing a recombinant bacterium in the presence of a gaseous substrate whereby the bacterium produces a terpene or a precursor thereof, such as mevalonic acid, isopentenyl pyrophosphate, dimethylallyl pyrophosphate, isoprene, geranyl pyrophosphate, farnesyl pyrophosphate, and/or farnesene. The bacterium may comprise one or more exogenous enzymes, such as enzymes in mevalonate, DXS, or terpene biosynthesis pathways.

The invention relates to the production of one or more terpenoids through microbial engineering, and relates to the manufacture of products comprising terpenoids.

The invention relates to the production of one or more terpenoids through microbial engineering, and relates to the manufacture of products comprising terpenoids.

Provided are a D-amino acid oxidase and use thereof in the preparation of L-phosphinothricin or an intermediate thereof. Provided is a D-amino acid oxidase having an amino acid sequence comprising an amino acid residue difference as compared to SEQ ID NO: 1, the amino acid residue difference being selected from one or a plurality of: K29G/H/I/N/Q/W/Y/C/L; V42C/D/E/H/Y; E195N/Y/Q; C234L; and V326W. The activity and/or thermal stability of the D-amino acid oxidase is not lower than that of a D-amino acid oxidase having an amino acid sequence as set forth in SEQ ID NO: 1. Provided is a D-amino acid oxidase with higher thermal stability. The operating temperature range of the enzyme is expanded while the activity of the enzyme is improved. The enzyme can have a prolonged service life when used at a relatively low temperature, and can have an improved catalytic efficiency when used at a relatively high temperature.

Provided are a D-amino acid oxidase and use thereof in the preparation of L-phosphinothricin or an intermediate thereof. Provided is a D-amino acid oxidase having an amino acid sequence comprising an amino acid residue difference as compared to SEQ ID NO: 1, the amino acid residue difference being selected from one or a plurality of: K29G/H/I/N/Q/W/Y/C/L; V42C/D/E/H/Y; E195N/Y/Q; C234L; and V326W. The activity and/or thermal stability of the D-amino acid oxidase is not lower than that of a D-amino acid oxidase having an amino acid sequence as set forth in SEQ ID NO: 1. Provided is a D-amino acid oxidase with higher thermal stability. The operating temperature range of the enzyme is expanded while the activity of the enzyme is improved. The enzyme can have a prolonged service life when used at a relatively low temperature, and can have an improved catalytic efficiency when used at a relatively high temperature.

Methods for the production of L-glufosinate (also known as phosphinothricin or (S)-2-amino-4-(hydroxy(methyl)phosphonoyl)butanoic acid) are provided. The methods comprise a two-step process. The first step involves the oxidative deamination of D-glufosinate to PPO (2-oxo-4-(hydroxy(methyl)phosphinoyl)butyric acid). The second step involves the specific amination of PPO to L-glufosinate, using an amine group from one or more amine donors. By combining these two reactions, the proportion of L-glufosinate in a mixture of L-glufosinate and D-glufosinate can be substantially increased.

Methods for the production of L-glufosinate (also known as phosphinothricin or (S)-2-amino-4-(hydroxy(methyl)phosphonoyl)butanoic acid) are provided. The methods comprise a two-step process. The first step involves the oxidative deamination of D-glufosinate to PPO (2-oxo-4-(hydroxy(methyl)phosphinoyl)butyric acid). The second step involves the specific amination of PPO to L-glufosinate, using an amine group from one or more amine donors. By combining these two reactions, the proportion of L-glufosinate in a mixture of L-glufosinate and D-glufosinate can be substantially increased.

Methods for the production of L-glufosinate (also known as phosphinothricin or (S)-2-amino-4-(hydroxy(methyl)phosphonoyl)butanoic acid) are provided. The methods comprise a two-step process. The first step involves the oxidative deamination of D-glufosinate to PPO (2-oxo-4-(hydroxy(methyl)phosphinoyl)butyric acid). The second step involves the specific amination of PPO to L-glufosinate, using an amine group from one or more amine donors. By combining these two reactions, the proportion of L-glufosinate in a mixture of L-glufosinate and D-glufosinate can be substantially increased.

Methods for the production of L-glufosinate (also known as phosphinothricin or (S)-2-amino-4-(hydroxy(methyl)phosphonoyl)butanoic acid) are provided. The methods comprise a two-step process. The first step involves the oxidative deamination of D-glufosinate to PPO (2-oxo-4-(hydroxy(methyl)phosphinoyl)butyric acid). The second step involves the specific amination of PPO to L-glufosinate, using an amine group from one or more amine donors. By combining these two reactions, the proportion of L-glufosinate in a mixture of L-glufosinate and D-glufosinate can be substantially increased.

Geranyl pyrophosphate (GPP) is a key intermediate molecule in the bioproduction of thousands of natural products. Currently, natural products are either cultivated from plants, synthesized via complex chemical synthesis strategies, or through cell-based factories also known as biofoundries. However, in order to replicate the process in a cell free environment, numerous enzymes and cofactors must be utilized making this approach costly and unviable. In order to make this process viable, a new approach was needed that uses fewer enzymes and cofactors. As described herein, the present invention demonstrates that it is possible to create GPP from glycerol through a short and concise biosynthetic pathway outside of the cell.