Embodiments provide a modified microbe capable of growing in or fermenting a solution, or lignocellulosic hydrolysate, comprising ferulic acid and/or coniferyl aldehyde. The microbe has one or more modifications to provide: (a) a decrease in copy number or expression of a BNA7 gene; (b) an increase in copy number or expression of one or more pentose phosphate pathway genes; and/or (c) localization of one or more products of the pentose phosphate pathway genes to the mitochondria or endoplasmic reticulum. Also provided is a microbe having modified expression or copy number of BNA7 and/or one or more of the pentose phosphate pathway genes. The pentose phosphate pathway genes may in certain embodiments be selected from at least one of ZWF1, TKL1, RPE1 and GND1. Also provided is a method for fermenting a substrate comprising ferulic acid and/or coniferyl aldehyde to produce a fermentation product.

The present disclosure is related to genetically engineered microbial strains and related bioprocesses for the production of pyruvate and related products. Specifically, the use of dynamically controlled synthetic metabolic valves to reduce the activity of enzymes known to contribute to pyruvate synthesis, leads to increased pyruvate production in a two-stage process rather than a decrease in production.

The present disclosure concerns recombinant yeast host cells having a first genetic modification for downregulating a first metabolic pathway that converts NADP.sup.+ to NADPH, as well as a second genetic modification for upregulating a second metabolic pathway that converts NADP.sup.+ to NADPH. The second genetic modification allows the expression of a glyceraldehyde-3-phosphate dehydrogenase lacking phosphorylating activity, which can, in some embodiments, be from enzyme commission 1.2.1.9 or 1.2.1.90. The second pathway is distinct from the first metabolic pathway. The present disclosure also concerns a process for making and improving the yield of a fermented product, such as ethanol, using the recombinant yeast host cell.

This invention relates to metabolically engineered microorganisms, such as bacterial and or fungal strains, and bioprocesses utilizing such strains. These strains enable the dynamic control of metabolic pathways, which can be used to optimize production. Dynamic control over metabolism is accomplished via a combination of methodologies including but not limited to transcriptional silencing and controlled enzyme proteolysis. These microbial strains are utilized in a multi-stage bioprocess encompassing at least two stages, the first stage in which organisms are grown and metabolism can be optimized for microbial growth and at least one other stage in which growth can be slowed or stopped, and dynamic changes can be made to metabolism to improve the production of desired product, such as a chemical or fuel.

The present application relates to methods to improve biomass or lipid production in a microorganism from one or more fatty acid and one or more simple carbon co-substrates. Produced lipids may include unsaturated C.sub.6-C.sub.24 fatty acids, alcohols, aldehydes, and acetates which may be useful as final products or precursors to insect pheromones, fragrances, flavors, and polymer intermediates. The application further relates to recombinant microorganisms modified for improved production of biomass or lipid, or improved lipid selectivity. Also provided are methods of producing one or more lipid using the recombinant microorganisms, as well as compositions comprising the recombinant microorganisms and/or optionally one or more of the product lipid.

The present disclosure describes the engineering of microbial cells for fermentative production of histamine and provides novel engineered microbial cells and cultures, as well as related histamine production methods.

Metabolites produced by a microorganism using more particularly oxaloacetate as substrate or co-substrate upstream in the biosynthesis pathway. There is indeed a need in the art for transformed, in particular recombinant, microorganisms having at least an increased ability to produce oxaloacetate, thus allowing an increased capacity to produce oxaloacetate-derived amino acids and amino acid derivatives, the oxaloacetate-derived amino acids and amino acid derivatives being termed oxaloacetate derivatives. The solution is the use of a genetically modified yeast including many modifications as described in the present text.

Disclosed is a glucose-6-phosphate dehydrogenase mutant and a use thereof in preparing a detection reagent. Compared with a wild-type glucose-6-phosphate dehydrogenase mutant, the glucose-6-phosphate dehydrogenase mutant contains a combination of the following mutations: 56C, 306C, and 454C. A detection kit prepared by using the glucose-6-phosphate dehydrogenase has strong specificity, high sensitivity, convenient operation, a short detection time, accurate quantification, and is suitable for high-throughput detection.

This disclosure relates to methods and kits for determining the presence and/or amount of one or more analytes in a keratinized structure (e.g., hair) sample.

The present disclosure provides recombinant Pichia pastoris, a construction method thereof, and use thereof in the efficient preparation of 15α-D-ethylgonendione, and belongs to the technical field of fermentation engineering. In the present disclosure, with Pichia pastoris as a host, 15α-steroid hydroxylase and glucose-6-phosphate dehydrogenase (G6PD) are simultaneously induced in a manner of intracellular enzyme production for the first time, and the Pichia pastoris whole-cell induction and catalysis mode is used to achieve the conversion of D-ethylgonendione with high substrate loading and high conversion rate.