A method of producing lipids, containing the steps of: culturing a transformant into which a gene encoding at least one protein selected from the group consisting of the following proteins (A) to (C) is introduced; and producing fatty acids or lipids containing the same as components: (A) a protein consisting of an amino acid sequence having at least one amino acid substitution selected from the group consisting of the following (A-1) to (A-11) in the amino acid sequence set forth in SEQ ID NO: 1, and having acyl-ACP thioesterase activity; (B) a protein consisting of an amino acid sequence having at least one amino acid substitution selected from the group consisting of the following (B-1) to (B-11) in an amino acid sequence having 85% or more identity with the amino acid sequence set forth in SEQ ID NO: 1, and having acyl-ACP thioesterase activity; and (C) a protein containing the amino acid sequence of the protein (A) or (B), and having acyl-ACP thioesterase activity: (A-1) substitution of isoleucine for leucine at position 257 of the amino acid sequence set forth in SEQ ID NO: 1; (A-2) substitution of arginine for threonine at position 251 of the amino acid sequence set forth in SEQ ID NO: 1; (A-3) substitution of lysine for threonine at position 251 of the amino acid sequence set forth in SEQ ID NO: 1; (A-4) substitution of histidine for threonine at position 251 of the amino acid sequence set forth in SEQ ID NO: 1; (A-5) substitution of isoleucine for tryptophan at position 254 of the amino acid sequence set forth in SEQ ID NO: 1; (A-6) substitution of tyrosine for tryptophan at position 254 of the amino acid sequence set forth in SEQ ID NO: 1; (A-7) substitution of methionine for leucine at position 257 of the amino acid sequence set forth in SEQ ID NO: 1; (A-8) substitution of valine for leucine at position 257 of the amino acid sequence set forth in SEQ ID NO: 1; (A-9) substitution of phenylalanine for leucine at position 257 of the amino acid sequence set forth in SEQ ID NO: 1; (A-10) substitution of cysteine for valine at position 266 of the amino acid sequence set forth in SEQ ID NO: 1; (A-11) substitution of tyrosine for tryptophan at position 271 of the amino acid sequence set forth in SEQ ID NO: 1; (B-1) substitution of isoleucine for an amino acid at a position corresponding to position 257 of the amino acid sequence set forth in SEQ ID NO: 1; (B-2) substitution of arginine for an amino acid at a position corresponding to position 251 of the amino acid sequence set forth in SEQ ID NO: 1; (B-3) substitution of lysine for an amino acid at a position corresponding to position 251 of the amino acid sequence set forth in SEQ ID NO: 1; (B-4) subst

Provided is a method for construction of recombinant bacteria for producing 3-hydroxypropionic acid. The method includes: knocking out fadR, fabF and fabH genes of recipient bacteria, introducing acc genes or gene clusters, alKL and Mcr genes, and enhancing the expression of fadL, fadD, sthA genes and atoSC gene clusters in the recipient bacteria. Also provided is a method for producing 3-hydroxypropionic acid by using the recombinant bacteria.

Recombinant microbial cells are provided which have been engineered to produce fatty acid derivatives having linear chains containing an odd number of carbon atoms by the fatty acid biosynthetic pathway. Also provided are methods of making odd chain fatty acid derivatives using the recombinant microbial cells, and compositions comprising odd chain fatty acid derivatives produced by such methods.

This document describes biochemical pathways for producing 7-aminoheptanoic acid using a β-ketoacyl synthase or a β-ketothiolase to form an N-acetyl-5-amino-3-oxopentanoyl-CoA intermediate. 7-aminoheptanoic acid can be enzymatically converted to pimelic acid, 7-hydroxyheptanoic acid, heptamethylenediamine or 1,7-heptanediol or corresponding salts thereof. This document also describes recombinant microorganisms producing 7-aminoheptanoic acid as well as pimelic acid, 7-hydroxyheptanoic acid, heptamethylenediamine and 1,7-heptanediol or corresponding salts thereof.

An object of the present invention is to provide a microorganism that efficiently produces a PUFA and a method for producing a PUFA using the microorganism. The present invention relates to a microorganism capable of producing a polyunsaturated fatty acid (PUFA), in which a gene encoding an exogenous polyketide synthase dehydratase (PS-DH) domain having a higher activity against 3-hydroxyhexanoyl acyl carrier protein (3-hydroxyhexanoyl ACP) than an endogenous FabA-like β-hydroxyacyl-ACP dehydratase (FabA-DH) domain has been introduced into a microorganism having a PUFA metabolic pathway, and the like.

The invention relates to compositions and methods, including polynucleotide sequences, amino acid sequences, recombinant host cells and recombinant host cell cultures engineered to produce fatty acid derivative compositions comprising fatty acids, fatty alcohols, fatty aldehydes, fatty esters, alkanes, terminal olefins, internal olefins or ketones. The fatty acid derivative composition is produced extracellularly with a higher titer, yield or productivity than the corresponding wild type or non-engineered host cell.

The present disclosure provides processes for producing alkylated fatty acids and derivatives thereof. In at least one embodiment, a process includes introducing a terminal alkyl transferase and a fatty acid into a bioreactor. The process includes introducing an internal methyl transferase and internal methyl reductase into the bioreactor or a second bioreactor. The process includes obtaining an alkylated fatty acid having a methyl substituent located at an internal carbon atom of the fatty acid and a methyl substituent or ethyl substituent located at a carbon atom alpha to the terminal carbon atom of the fatty acid.

The disclosure relates to variant carboxylic acid reductase (CAR) enzymes for the improved production of fatty alcohols in recombinant host cells.

The disclosure relates to the field of specialty chemicals and methods for their synthesis. In embodiments, the disclosure provides viable bacterial cells which comprise heterologous dual 3-hydroxy-acyl-ACP dehydratase/isomerases, etc. The disclosure further provides monounsaturated fatty acid derivative molecules produced by the viable bacterial cells which are non-native to the bacterial cells. The disclosure further provides methods for the preparation and production of non-native monounsaturated fatty acid derivative molecules such as e.g., an ω3-monounsaturated fatty acid derivative, an ω5-monounsaturated fatty acid derivative, an ω9-monounsaturated fatty acid derivative, an ω11-monounsaturated fatty acid fatty acid derivative, etc.

Recombinant DNA techniques are used to produce oleaginous recombinant cells that produce triglyceride oils having desired fatty acid profiles and regiospecific or stereospecific profiles. Genes manipulated include those encoding stearoyl-ACP desaturase, delta 12 fatty acid desaturase, acyl-ACP thioesterase, ketoacyl-ACP synthase, and lysophosphatidic acid acyltransferase. The oil produced can have enhanced oxidative or thermal stability, or can be useful as a frying oil, shortening, roll-in shortening, tempering fat, cocoa butter replacement, as a lubricant, or as a feedstock for various chemical processes. The fatty acid profile can be enriched in midchain profiles or the oil can be enriched in triglycerides of the saturated-unsaturated-saturated type.