C12Y401/01031

ENZYMES AND METHODS FOR PRODUCTION OF MALONIC ACID AND DERIVATIVES THEREOF

The present disclosure provides an engineered microorganism capable of producing malonic acid, malonate, esters of malonic acid, or mixtures thereof. The engineered microorganism includes a malonate-semialdehyde dehydrogenase that is heterologous to a native form of the engineered microorganism and comprises at least 80% sequence identity to SEQ ID NO: 6, wherein the engineered microorganism is capable of producing about 3 g/L to about 250 g/L of malonic acid, malonate, esters of malonic acid, or mixtures thereof.

ENGINEERED PHOSPHOENOLPYRUVATE CARBOXYLASE ENZYMES

The present disclosure provides plants that express a variant phosphoenolpyruvate carboxylase (PEPC) enzyme. The plants have enhanced resistance to aluminum than comparable plants that lack the variant PEPC enzyme. In addition, the plants more effectively sequester carbon, extract phosphate, and produce oxaloacetate-derived amino acids and glucose than comparable plants that lack the variant PEPC enzyme. The disclosure also provides tools for production of plants that express the variant PEPC enzyme.

Enhanced metabolite-producing yeast

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.

RECOMBINANT HOST CELLS AND METHODS FOR THE PRODUCTION OF ASPARTIC ACID AND B-ALANINE

Methods and materials related to producing aspartic acid, β-alanine and salts of each thereof are disclosed. Specifically, isolated nucleic acids, polypeptides, host cells, methods and materials for producing aspartic acid by direct fermentation from sugars are disclosed.

Microorganisms and methods for production of specific length fatty alcohols and related compounds

The invention provides non-naturally occurring microbial organisms containing a fatty alcohol, fatty aldehyde or fatty acid pathway, wherein the microbial organisms selectively produce a fatty alcohol, fatty aldehyde or fatty acid of a specified length. Also provided are non-naturally occurring microbial organisms having a fatty alcohol, fatty aldehyde or fatty acid pathway, wherein the microbial organisms further include an acetyl-CoA pathway. In some aspects, the microbial organisms of the invention have select gene disruptions or enzyme attenuations that increase production of fatty alcohols, fatty aldehydes or fatty acids. The invention additionally provides methods of using the above microbial organisms to produce a fatty alcohol, a fatty aldehyde or a fatty acid.

Xylose-induced genetically engineered bacteria used for producing ectoine and use thereof

The present disclosure relates to the field of genetic engineering, especially relates to a xylose-induced genetically engineered bacteria used for producing ectoine as well as a construction method and use thereof. The genetically engineered bacteria is constructed by heterologously expressing the ectABC gene cluster from Halomonas elongata on the E. coli chromosome, using the promoter of xylose transporter coding gene xylF to control the RNA polymerase from T7 bacteriophage, reconstructing a synthesis pathway of ectoine and constructing a plasmid-free system, and enhancing the expression of target genes by a strong promoter T7; the yield of ectoine reached 12-16 g/L after 20-28 h fermentation in shake flask, and reached 35-50 g/L after 24-40 h fermentation in a 5 L fermentor.

Genetically engineered bacterium for sarcosine production as well as construction method and application

The disclosure discloses a genetically engineered strain for sarcosine production as well as a construction method and application. The genetically engineered strain is obtained by using Escherichia coli as a host and by integrating a single copy of imine reductase gene dpkA on its genome; singly copying citrate synthase gene gltA; knocking out glyoxylate cycle inhibitor gene iclR; knocking out malate synthase gene aceB; integrating a single copy of isocitrate lyase gene aceA; integrating a single copy of membrane-bound transhydrogenase gene pntAB; knocking out 2-ketate reductase gene ycdW; integrating a single copy of phosphoenolpyruvate carboxylase gene ppc; and knocking out pyruvate kinase gene pykF. After system metabolism transformation, the engineered strain can synthesize sarcosine with glucose and methylamine as main raw materials. The sarcosine titer can reach 10 g/L after fermentation for 30 h in a 5 L fermenter.

Microorganisms and methods for the production of glycolic acid and glycine via reverse glyoxylate shunt

The present invention provides biochemical pathways, glyoxylate producing recombinant microorganisms, and methods for the production and yield improvement of glycolic acid and/or glycine via a reverse glyoxylate shunt. The reverse glyoxylate shunt comprises an enzyme that catalyzes the carboxylation of phosphoenol pyruvate (PEP) to oxaloacetate (OAA), or an enzyme that catalyzes the carboxylation of pyruvate to oxaloacetate (OAA) or an enzyme that catalyzes the carboxylation of pyruvate to malate or a combination of any of the previous reactions; an enzyme that catalyzes the conversion of malate to malyl-CoA; an enzyme that catalyzes the conversion of malyl-CoA to glyoxylate and acetyl-CoA; and optionally an enzyme that catalyzes the conversion of oxaloacetate (OAA) to malate. Glyoxylate is reduced to produce glycolate. Alternatively, glyoxylate is converted to glycine. The reverse glyoxylate shunt pathway of the present invention can be utilized synergistically with other glycolic acid and/or glycine producing pathways to increase product yield.

GENETICALLY ENGINEERED BACTERIUM FOR SARCOSINE PRODUCTION AS WELL AS CONSTRUCTION METHOD AND APPLICATION

The disclosure discloses a genetically engineered strain for sarcosine production as well as a construction method and application. The genetically engineered strain is obtained by using Escherichia coli as a host and by integrating a single copy of imine reductase gene dpkA on its genome; singly copying citrate synthase gene gltA; knocking out glyoxylate cycle inhibitor gene iclR; knocking out malate synthase gene aceB; integrating a single copy of isocitrate lyase gene aceA; integrating a single copy of membrane-bound transhydrogenase gene pntAB; knocking out 2-ketate reductase gene ycdW; integrating a single copy of phosphoenolpyruvate carboxylase gene ppc; and knocking out pyruvate kinase gene pykF. After system metabolism transformation, the engineered strain can synthesize sarcosine with glucose and methylamine as main raw materials. The sarcosine titer can reach 10 g/L after fermentation for 30 h in a 5 L fermenter.

Genetically engineered bacterium of <i>Escherichia coli </i>and method for fermentation production of L-theanine thereof

The present invention belongs to the bioengineering field, and relates to a method for fermentation production of L-theanine by using an Escherichia coli genetically engineered bacterium. The engineered bacterium is obtained by serving a strain as an original strain, wherein the strain is obtained after performing a single copy of T7RNAP, a dual copy of gmas, xylR knockout, and sucCD knockout on an Escherichia coli W3110 genome, and by integrating genes xfp, pta, acs, gltA, and ppc, and knocking out ackA on the genome. The present invention has a high yield, and stable production performance; after 20-25 h, L-theanine has a titer of 75-80 g/L, and the yield is up to 52-55%. The fermentation broth is purified by membrane separation in combination with a cation-anion resin series technique. Moreover, the one-step crystallization yield is 72.3% and the L-theanine final product has a purity of 99%.