E.i. Dupont De Nemours and Company

North Carolina State University

Genencor International, Inc.

Other

E. I. Du Pont Nemours and Co.

Anthony Arthur Gatenby

Sima Sariaslani

Arie Ben-Bassat

Katharine Janet Gibson

Juan Ramos

M Isabel Ramos-Gonzalez

Monica Cattermole

Nigel S Dunn-Coleman

Fernando Valle

Gregory Marshall Whited

Donald Eugene Trimbur

Sharon Loretta Haynie

Amy Kuang-Hua Hsu

Ben A Bulthuis

Mark Scott Payne

Vasantha Nagarajan

Stephen K Picataggio

Andrew C Eliot

Charles Edwin Nakamura

Tina K Van Dyk

Ramesh V Nair

Fateme Sima Sariaslani

Xiao-Song Tang

Wonchul Suh

Ranjan Patnaik

Maria R Diaz-Torres

Wei Wei Qi

Todd M Vannelli

John S Chapman

Francois Baneyx

Richard D Lareau

Richard D La Reau

Cathy E Kalbach

Stephen Kenneth Picataggio

Recombinant microorganisms having an improved ability to co-metabolize in medium both fructose and glucose are described. The recombinant microorganisms comprise a promoter operably linked to a native or non-native nucleotide sequence that encodes a fucose: H+ symporter polypeptide. The recombinant microorganisms are useful for the production of a variety of products including glycerol and glycerol derivatives such as 1,3-propanediol and 3-hydroxypropionic acid.

Co-metabolism of fructose and glucose in microbial production strains

An enteric bacterial strain was engineered to over-produce L-tyrosine using a one-step method. The pheA-tyrA chromosomal region of the bacterial genome was replaced with an engineered chromosomal segment, resulting in inactivation of the pheA coding region and strong expression of the tyrA coding region, resulting in high levels of L-tyrosine production.

Method for producing an L-tyrosine over-producing bacterial strain

Recombinant organisms are provided comprising genes encoding cob(II)alamin reductase, cob(I)alamin adenosyltransferase, glycerol dehydratase and 1,3-propanediol oxidoreductase activities useful for the production of 1,3-propanediol from a variety of carbon substrates.

Method for the production of 1,3-propanediol by recombinant organisms comprising genes for coenzyme B12 synthesis

Bacterial strains transformed with the pcu genes are useful for the production of para-hydroxybenzoate (PHBA). Applicant has provided the p-cresol utilizing (pcu) and tmoX gene sequences fromKR-1, the proteins encoded by these sequences, recombinant plasmids containing such sequences, and bacterial host cells containing such plasmids or integrated sequences. Method for the use of these materials to produce PHBA are also disclosed.

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Recombinant organisms are provided comprising genes encoding aquacobalamin reductase, cob(II)alamin reductase, cob(I)alamin adenosyltransferase, glycerol dehydratase and 1,3-propanediol oxidoreductase activities useful for the production of 1,3-propanediol from a variety of carbon substrates. More specifically the following nucleotide sequences are provided: btuR, encoding thecob(I)alamin adenosyltransferase enzyme; cobA, encoding thecob(I)alamin adenosyltransferase enzyme; cobO, encoding thecob(I)alamin adenosyltransferase enzyme; dhaB1, encoding the &#x3b1; subunit of theglycerol dehydratase enzyme; dhaB2, encoding the &#x3b2; subunit of theglycerol dehydratase enzyme; dhaB3, encoding the &#x3b3; subunit of theglycerol dehydratase enzyme; dhaT, encodingoxidoreductase enzyme; the yciK gene isolated from; the glucose isomerase promoter sequence from; and the N-terminal amino acid sequence for cob(II)alamin reductase from

Bacterial strains transformed with the pcu genes are useful for the production of para-hydroxybenzoate (PHBA). Applicant has provided the p-cresol utilizing (pcu) and tmoX gene sequences from KR-1, the proteins encoded by these sequences, recombinant plasmids containing such sequences, and bacterial host cells containing such plasmids or integrated sequences. Method for the use of these materials to produce PHBA are also disclosed.

Method for the production of &rgr;-Hydroxybenzoate in species of pseudomonas and agrobacterium

Recombinant organisms are provided comprising genes encoding genes encoding glycerol dehydratase, 1,3-propanediol oxidoreductase, a gene encoding vitamin B receptor precursor(BtuB), a gene encoding vitamin B transport system permease protein(BtuC) and a gene encoding vitamin B transport ATP-binding protein (BtuD). The recombinant microorganism is contacted with a carbon substrate and 1,3-propanediol is isolated from the growth media.

Method for the production of 1,3-propanediol by recombinant organisms comprising genes for vitamin B12 transport

The present invention provides several methods for biological production of para-hydroxycinnamic acid (PHCA). The invention is also directed to the discovery of new fungi and bacteria that possess the ability to convert cinnamate to PHCA. The invention relates to developing of a new biocatalyst for conversion of glucose to PHCA by incorporation of the wild type PAL from the yeast into underlining the ability of the wildtype PAL to convert tyrosine to PHCA. The invention is also directed to developing a new biocatalyst for conversion of glucose to PHCA by incorporation of the wildtype PAL from the yeast plus the plant cytochrome P-450 and the cytochrome P-450 reductase into . In yet another embodiment, the present invention provides for the developing of a new biocatalyst through mutagenesis of the wild type yeast PAL which possesses enhanced tyrosine ammonia-lyase (TAL) activity.

Bioproduction of para-hydroxycinnamic acid

Recombinant organisms are provided comprising genes encoding a glycerol-3-phosphate dehydrogenase and/or a glycerol-3-phosphatase activity useful for the production of glycerol from a variety of carbon substrates.

Method for the production of glycerol by recombinant organisms

Recombinant organisms are provided comprising genes encoding glycerol-3-phosphate dehydrogenase, glycerol-3-phosphatase, glycerol dehydratase and 1,3-propanediol oxidoreductase activites useful for the production of 1,3-propanediol from a variety of carbon substrates.

Method for the production of 1,3-propanediol by recombinant

Yield of biologically active foreign proteins from recombinent E. coli has been increased 2-4 fold by a novel use of the dnaK mutation. The presence of the full length dnaK mutant protein results in elevated levels of biologically active foreign proteins.

Process for enchancing the production of heterologous protein in

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Wilmington, DE, United States of America

Anthony Arthur Gatenby