The disclosure relates to omega-hydroxylase-related fusion polypeptides that result in improved omega-hydroxylated fatty acid derivative production when expressed in recombinant host cells. The disclosure further relates to microorganisms for expressing the omega-hydroxylase-related fusion polypeptides for the production of omega-hydroxylated fatty acid derivatives.

Microorganisms are genetically engineered to continuously produce fatty acids, fatty alcohols, cultured protein, or any combination thereof by microbial fermentation, particularly by microbial fermentation of a gaseous substrate. The microorganisms are C1-fixing. The production of fatty acids, fatty alcohols, and cultured proteins can be improved. This can be improved by varying promoters or nutrient limiting means.

The disclosure relates to a recombinant microorganism engineered to express an enzyme which catalyzes the conversion of a primary amine and an acyl thioester to a fatty amide. The disclosure further encompasses a method of producing a fatty amide by culturing the recombinant microorganism in the presence of a carbon source.

The disclosure relates to fatty diols and recombinant microorganisms for producing them. More particularly, the disclosure relates to recombinant microorganisms engineered to produce fatty diols via fermentation. Further encompassed is a process that uses the microorganisms to produce fatty diols from a simple carbon source.

The disclosure relates to a recombinant microorganism engineered to express an enzyme which catalyzes the conversion of a primary amine and an acyl thioester to a fatty amide. The disclosure further encompasses a method of producing a fatty amide by culturing the recombinant microorganism in the presence of a carbon source.

The disclosure relates to fatty diols and recombinant microorganisms for producing them. More particularly, the disclosure relates to recombinant microorganisms engineered to produce fatty diols via fermentation. Further encompassed is a process that uses the microorganisms to produce fatty diols from a simple carbon source.

The present disclosure relates to methods, cells, and compositions for producing a product of interest, e.g., a recombinant protein. In particular, the present disclosure provides improved mammalian cells expressing the product of interest, where the cells (e.g., Chinese Hamster Ovary (CHO) cells) have reduced or eliminated activity, e.g., expression, of certain host cell proteins, e.g., enzymes including, but not limited to, certain lipases, esterases, and/or hydrolases.

Provided is a mutated lysophospholipase. Further provided are a gene encoding the lysophospholipase, and a vector and a host cell comprising the gene. In addition, further provided is a use of the lysophospholipase. The present invention also provides a mutated Aspergillus niger strain and a use thereof. Specifically, the present invention provides a mutated Aspergillus niger strain, which is an orotate phosphoribosyltransferase auxotrophic strain, and has improved production capacity of endogenous enzymes, preferably lysophospholipase, with respect to an unmutated strain. The present invention further provides uses of the strain. For example, the strain can be used for expressing the mutated lysophospholipase of the present invention.

Disclosed in the present invention is a fluoroacetate dehalogenase mutant, a sequence of the fluoroacetate dehalogenase mutant comprising a mutated sequence having an amino acid residue H at position 155 and/or an amino acid residue W at position 156, as shown in SEQ ID NO: 1; the fluoroacetate dehalogenase mutant has activity catalyzing bromination of a substrate, particularly a 2-bromobutyric acid substrate. Also provided in the present invention is an application of said fluoroacetate dehalogenase mutant in the preparation of (R)-2-bromobutyric acid and/or (R)-2-hydroxybutyric acid. When using the fluoroacetate dehalogenase mutant of the present invention to prepare (R)-2-bromobutyric acid, production costs are low and stereoselectivity is high, facilitating industrialized production.