This document describes biochemical pathways for producing 7-hydroxyheptanoate methyl ester and heptanoic acid heptyl ester using one or more of a fatty acid O-methyltransferase, an alcohol O-acetyltransferase, and a monooxygenase, as well as recombinant hosts expressing one or more of such exogenous enzymes. 7-hydroxyheptanoate methyl esters and heptanoic acid heptyl esters can be enzymatically converted to pimelic acid, 7-aminoheptanoate, 7-hydroxyheptanoate, heptamethylenediamine, or 1,7-heptanediol.

This document describes biochemical pathways for producing 7-hydroxyheptanoate methyl ester and heptanoic acid heptyl ester using one or more of a fatty acid O-methyltransferase, an alcohol O-acetyltransferase, and a monooxygenase, as well as recombinant hosts expressing one or more of such exogenous enzymes. 7-hydroxyheptanoate methyl esters and heptanoic acid heptyl esters can be enzymatically converted to pimelic acid, 7-aminoheptanoate, 7-hydroxyheptanoate, heptamethylenediamine, or 1,7-heptanediol.

There is described a method for producing 3-hydroxypropanal, the method comprising: culturing an Acetobacter lovaniensis bacterium in a growth medium containing phosphate at a level which is more than 1 g/litre and nitrate at a level which is more than 0.1 g/litre, wherein culturing of the bacterium produces the 3-hydroxypropanal. The 3-hydroxypropanal can be separated from the growth medium or, when the microorganism has converted some or all of the 3-hydroxypropanal to 3-hydroxypropionic acid and/or a 3-hydroxypropionate ester, it may be separated as 3-hydroxypropionic acid or a 3-hydroxypropionate ester. The separated product can be converted into other chemicals such as an ester of 3-hydroxypropionic acid, 3-hydroxypropionic acid, 3-hydroxypropionate salts (including ammonium, sodium and calcium 3-hydroxypropionate), acrylic acid, acrylates, acrylamide, acrylonitrile, acrolein and 1,3 propanediol.

There is described a method for producing 3-hydroxypropanal, the method comprising: culturing an Acetobacter lovaniensis bacterium in a growth medium containing phosphate at a level which is more than 1 g/litre and nitrate at a level which is more than 0.1 g/litre, wherein culturing of the bacterium produces the 3-hydroxypropanal. The 3-hydroxypropanal can be separated from the growth medium or, when the microorganism has converted some or all of the 3-hydroxypropanal to 3-hydroxypropionic acid and/or a 3-hydroxypropionate ester, it may be separated as 3-hydroxypropionic acid or a 3-hydroxypropionate ester. The separated product can be converted into other chemicals such as an ester of 3-hydroxypropionic acid, 3-hydroxypropionic acid, 3-hydroxypropionate salts (including ammonium, sodium and calcium 3-hydroxypropionate), acrylic acid, acrylates, acrylamide, acrylonitrile, acrolein and 1,3 propanediol.

Methods and processes for producing aerobic digestion products, such as organic acids, from a low-rank coal substrate are provided. Also provided are multistage bioreactor systems for carrying out the described methods and processes. In another aspect, product compositions comprising organic acids produced by the described methods and processes are provided, as well as methods for their use, including for the improvement of soil quality and/or plant growth.

Disclosed is a method that includes use of a catalyst in a method of reducing a substrate, the method including contacting a substrate with a catalyst, optionally in the presence of a co-substrate, thereby to generate a reduced substrate. The catalyst is a polypeptide including an amino acid sequence having at least 70% identity to SEQ ID NO: 1, SEQ ID NO: 7 or SEQ ID NO: 9. In the method the substrate concentration is at least

The present invention relates to natural vanillin compositions comprising at least one compound chosen from 4-((4-hydroxy-3-methoxybenzyl)oxy)-3-methoxybenzaldehyde and 4-hydroxy-3-(4-hydroxy-3-methoxybenzyl)-5-methoxybenzaldehyde. The invention also relates to a process for obtaining natural vanillin compositions according to the invention.

The invention relates to ketoreductases and the use thereof. The ketoreductases of the invention are particularly useful for enzymatically catalyzing the reduction of ketones to chiral secondary alcohols.

The invention relates to ketoreductases and the use thereof. The ketoreductases of the invention are particularly useful for enzymatically catalyzing the reduction of ketones to chiral secondary alcohols.

Genetically modified LeuCD′ enzyme complexes, processes for preparing a C.sub.7-C.sub.11 2-ketoacid utilizing genetically modified LeuCD′ enzyme complexes, and microbial organisms including modified LeuCD enzyme complexes are described. The instantly-disclosed genetically modified LeuCD′ enzyme complexes, processes for preparing a C.sub.7-C.sub.11 2-ketoacid, and microbial organisms including modified LeuCD′ enzyme complexes can be particularly useful for producing C.sub.6-C.sub.10 aldehydes, alkanes, alcohols, and carboxylic acids, both in vivo and in vitro.