Disclosed are methods for producing optically active amino acids and amines. According to the methods, α-keto acids are generated as reaction intermediates, and as a result, ω-transaminase-catalyzed kinetic resolution of racemic amino acids or amines as racemic amine compounds enables the production of optically active amine compounds without the need to use expensive α-keto acids as starting materials. Therefore, the optically active amine compounds are produced at greatly reduced costs. In addition, the optically active amine compounds have high enantiomeric excess.

Recombinant microorganisms comprising DNA molecules in a deregulated form which improve the production of cadaverine or N-acetylcadaverine, as well as recombinant DNA molecules and polypeptides used to produce the microorganisms are provided. Said microorganisms comprise an intracellular lysine decarboxylase activity and a deregulated cadaverine export activity, or comprise a decreased cadaverine export activity and an enhanced N-acetylcadaverine forming activity. Processes for the production of cadaverine N-acetylcadaverine using the recombinant microorganisms are also provided.

The present invention relates to a transformant which is transformed to express Baeyer-Villiger monooxygenase (BVMO), a method for producing C5-C14 medium-chain ω-hydroxy fatty acids, α,ω-dicarboxylic acids, ω-amino fatty acids, or alcohols from C16-C20 long-chain fatty acids by biotransformation using the transformant, a method for producing a fatty acid derivative having an ester group which is introduced into the chain thereof from keto fatty acid using the BVMO, and novel ω-hydroxy fatty acids which are prepared by the method. Degradation products such as C5 to C14 ω-hydroxy fatty acids, α,ω-dicarboxylic acids, ω-amino fatty acids, alcohols can be produced in a large amount from C16 to C20 long-chain fatty acids contained in a medium by biotransformation using a transformant capable of expressing BVMO of the present invention. Therefore, it can be widely used to produce ω-hydroxy fatty acids, α,ω-dicarboxylic acids, ω-amino fatty acids or alcohols in a more safe and economic manner.

This document describes biochemical pathways for producing 2-aminopimelate from 2,6-diaminopimelate, and methods for converting 2-aminopimelate to one or more of adipic acid, adipate semialdehyde, caprolactam, 6-aminohexanoic acid, 6-hexanoic acid, hexamethylenediamine, or 1,6-hexanediol by decarboxylating 2-aminopimelate into a six carbon chain aliphatic backbone and enzymatically forming one or two terminal functional groups, comprised of carboxyl, amine or hydroxyl group, in the backbone.

The present invention relates to a process for preparing a compound having the formula (I), said process comprising the following steps: a) the addition of an oxygen source into a solution of a compound of formula (II), in a water-miscible solvent, b) the addition of a laccase in the solution obtained after step a); and c) the possible recovering of the compound of formula (I) thus obtained.

##STR00001##

The present disclosure describes biocatalytic processes for producing a product, comprising providing an aqueous stream (AS) comprising at least one fermentable substrate and a gaseous stream (GS) comprising at least one of CO.sub.2/H.sub.2, H.sub.2, methane, and/or CO to a fermentation zone, wherein the GS and AS stream are optionally contacted and/or mixed; the fermentation zone comprising at least one organism capable of metabolizing an AS substrate and a GS substrate, wherein the fermentation operates at conditions to mixotrophically metabolize at least one gaseous substrate in the GS and at least one substrate in the AS, producing the product. The present disclosure also describes compositions comprising an AS, a GS, and an organism, wherein the organism or an equivalent or engineered equivalent thereof is a methanotroph or a hydrogen-metabolizing or CO-metabolizing chemolithotrophic organism, and wherein the organism is capable of mixotrophic metabolism of at least one gaseous substrate in the GS and at least one substrate in the AS. The present disclosure also describes a process wherein said fermentation operates at conditions to mixotrophically metabolize at least H.sub.2 in the gaseous stream and glycerol and lactic acid in the aqueous stream. The present disclosure also describes a system for producing a fermentation or bio-derived product.

The present disclosure describes biocatalytic processes for producing a product, comprising providing an aqueous stream (AS) comprising at least one fermentable substrate and a gaseous stream (GS) comprising at least one of CO.sub.2/H.sub.2, H.sub.2, methane, and/or CO to a fermentation zone, wherein the GS and AS stream are optionally contacted and/or mixed; the fermentation zone comprising at least one organism capable of metabolizing an AS substrate and a GS substrate, wherein the fermentation operates at conditions to mixotrophically metabolize at least one gaseous substrate in the GS and at least one substrate in the AS, producing the product. The present disclosure also describes compositions comprising an AS, a GS, and an organism, wherein the organism or an equivalent or engineered equivalent thereof is a methanotroph or a hydrogen-metabolizing or CO-metabolizing chemolithotrophic organism, and wherein the organism is capable of mixotrophic metabolism of at least one gaseous substrate in the GS and at least one substrate in the AS. The present disclosure also describes a process wherein said fermentation operates at conditions to mixotrophically metabolize at least H.sub.2 in the gaseous stream and glycerol and lactic acid in the aqueous stream. The present disclosure also describes a system for producing a fermentation or bio-derived product.

This document describes biochemical pathways for producing one or more of pimelic acid, 7-aminoheptanoic acid, 7-hydroxyheptanoic acid, heptamethylenediamine and 1,7-heptanediol by forming one or two terminal functional groups, comprised of carboxyl, amine or hydroxyl groups, in a C7 aliphatic backbone substrate produced from succinate semialdehyde or pyruvate. These pathways, metabolic engineering and cultivation strategies described herein rely on the aldol condensation of succinate semialdehyde and pyruvate.

A novel process is provided for the efficient preparation of an asymmetric compound of structural formula I: ##STR00001##
employing dynamic kinetic resolution (DKR). The DKR process involves an enzymatic enantioselective amination reaction catalyzed by transaminases. The process can be used to manufacture key intermediates in the preparation of poly (ADP-ribose) polymerase (PARP) inhibitors which may be useful for the treatment of cancer.

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.