C12Y101/03013

MATERIALS AND METHODS FOR PROTEIN PRODUCTION
20250066951 · 2025-02-27 ·

This document relates to materials and methods for the production of protein. In one aspect, this document provides a nucleic acid construct including a first alcohol oxidase promoter element, wherein the first alcohol oxidase promoter element includes a mutation at one or more nucleotide positions corresponding to any of nucleotide positions 668-734 relative to SEQ ID NO: 28.

Production of non-native monounsaturated fatty acids in bacteria

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 3-monounsaturated fatty acid derivative, an 5-monounsaturated fatty acid derivative, an 9-monounsaturated fatty acid derivative, an 11-monounsaturated fatty acid fatty acid derivative, etc.

PRODUCTION OF CHIRAL 1,2-AMINO ALCOHOLS AND ALPHA-AMINO ACIDS FROM ALKENES BY CASCADE BIOCATALYSIS
20170067084 · 2017-03-09 ·

Disclosed herein are methods of forming chiral 1,2-aminoalcohols and -aminoacids from alkene starting materials by way of an enzymatic cascade reaction sequence that may be accomplished in a single reaction vessel without the need to isolate any intermediates. Also disclosed herein are recombinant nucleic acids, vectors and host cells for use in the methods of the invention.

Enzyme Catalyzed Oxidation of Hydrocarbons

The present disclosure provides a method of generating electricity from a long chain hydrocarbon, said method comprising contacting the liquid non-polar substrate with a plurality of enzymes, wherein at least one enzyme is non-electric current/potential enzyme that functions as a catalyst for chemical reaction transforming a first substrate or byproduct to a second substance that can be used with an additional electric current/potential generating enzyme.

Mut- methylotrophic yeast

A recombinant methanol utilization pathway deficient methylotrophic yeast (Mut) host cell which is engineered: a) by one or more genetic modifications to reduce expression of a first and a second endogenous gene compared to the host cell prior to said one or more genetic modifications, wherein i. the first endogenous gene encodes alcohol oxidase 1 (AOX1) comprising the amino acid sequence identified as SEQ ID NO:1 or a homologue thereof, and ii. the second endogenous gene encodes alcohol oxidase 2 (AOX2) comprising the amino acid sequence identified as SEQ ID NO:3 or a homologue thereof, and b) by one or more genetic modifications to increase expression of an alcohol dehydrogenase (ADH2) gene compared to the host cell prior to said one or more genetic modifications, wherein the ADH2 gene encodes an alcohol dehydrogenase (ADH2).

SYNTHETIC METHANOTROPHIC AND METHYLOTROPHIC MICROORGANISMS

Provided herein are non-naturally occurring microbial organisms comprising a methane-oxidizing metabolic pathway. The invention additionally comprises non-naturally occurring microbial organisms comprising pathways for the production of chemicals. The invention additionally provides methods for using said organisms for the production of chemicals.

Method of producing glycolipids
09540672 · 2017-01-10 · ·

A protein selected from the following (a) to (c), a gene encoding the protein, a transformant in which the gene is subjected to deletion, mutation or repression of gene expression, and a method of producing a glycolipid using the transformant are provided, wherein: (a) is a protein consisting of an amino acid sequence set forth in SEQ ID NO: 1; (b) is a protein consisting of an amino acid sequence having 50% or more identity with the amino acid sequence set forth in SEQ ID NO: 1, and having alcohol oxidase activity; and (c) is a protein consisting of an amino acid sequence in which one to several amino acids are subjected to deletion, substitution, insertion or addition in the amino acid sequence set forth in SEQ ID NO: 1, and having alcohol oxidase activity.

Production Of Non-Native Monounsaturated Fatty Acids In Bacteria

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 3-monounsaturated fatty acid derivative, an 5-monounsaturated fatty acid derivative, an 9-monounsaturated fatty acid derivative, an 11-monounsaturated fatty acid fatty acid derivative, etc.

COMPOSITIONS AND METHODS FOR PRODUCTION OF HIGH VALUE CHEMICALS FROM ETHANOL

A chemoenzymatic manufacturing process for the preparation of high value chemicals includes the enzymatic oxidation of ethanol using an oxidizing biocatalyst to form an acetaldehyde intermediate. In addition, the process includes contacting of the acetaldehyde intermediate with a carboligating biocatalyst to form pyruvic acid. Further, the process includes reacting pyruvic acid with ethanol to form ethyl pyruvate. Still further, the process includes contacting the ethyl pyruvate with a metal catalyst and hydrogen to form ethyl lactate. The process also includes hydrolyzing the ethyl lactate to produce lactic acid. Moreover, the process includes contacting at least a portion of the lactic acid with a dehydrating catalyst to form acrylic acid. In addition, the process includes contacting at least a portion of the lactic acid with a metal catalyst and hydrogen to form propylene glycol and n-propanol.