A method for enzymatic sulfurylation of a substrate is provided which includes the steps of reacting the substrate with 3′-phosphoadenosine-5′-phosphosulfate (PAPS) in a medium containing a bacterium belonging to the family Enterobacteriaceae to produce a sulfated derivative of the substrate, and collecting the sulfated derivative from the medium, wherein the bacterium has been modified to produce, at least, a protein having sulfotransferase activity, and to attenuate expression of an aphA gene, a cysQ gene, or a cpdB gene, or a combination of these.

The present invention relates to a method for chondroitin sulfate biosynthesis, belongs to the field of pharmaceuticals. CS was biosynthesized by sulfating the chondroitin with C4ST or C6ST in Tris-HCl buffer assisted with 3′-phosphoadenosine 5′-phophosulfate (PAPS). C4ST and C46ST came from bioengineered Escherichia coli or Pichia pastoris. Chondroitin came from bioengineered Bacillus subtilis 168.

The present invention relates to a novel 3-hydroxypropionate-lactate block copolymer [P(3HP-b-LA)], and a method for preparing same, and more specifically, provides a method for preparing a 3-hydroxypropionate-lactate block copolymer, and a 3-hydroxypropionate-lactate block copolymer produced thereby, the method comprising: a first culture step in which, by using recombinant E. coli improved so as to be incapable of biosynthesizing lactic acid, P(3HP) is biosynthesized at the early stage of culturing by having glycerol as a carbon source and through 3-hydroxypropionate-generating genes and an enhanced PHA synthase; and a second culture step in which P(3HP) production is inhibited by using a carbon catabolic repression system for selectively introducing only glucose into E. coli when glycerol and glucose are supplied together as carbon sources, and in which polylactate is biosynthesized to an interrupted P(3HP) terminus by the enabling of the expression of a lactate synthase and a lactyl-CoA converting enzyme through an IPTG induction system.

A DNA expression construct comprising a polynucleotide encoding an unnatural UstD enzyme, the unnatural enzyme itself, and a method of making gamma-hydroxy amino acids by contacting an aldehyde-containing substrate, an amino acid, and the unnatural, purified UstD enzyme under conditions and for a time sufficient to react at least a portion of the aldehyde-containing substrate with at least a portion of the amino acid, to yield a gamma-hydroxy amino acid product.

The present application relates to recombinant microorganisms useful in the biosynthesis of monoethylene glycol (MEG) and one or more three-carbon compounds such as acetone, isopropanol or propene. The MEG and one or more three-carbon compounds described herein are useful as starting material for production of other compounds or as end products for industrial and household use. The application further relates to recombinant microorganisms co-expressing a C2 branch pathway and a C3 branch pathway for the production of MEG and one or more three-carbon compounds. Also provided are methods of producing MEG and one or more three-carbon compounds using the recombinant microorganisms, as well as compositions comprising the recombinant microorganisms and/or optionally the products MEG and one or more three-carbon compounds.

The present invention relates to a recombinant microorganism to which a gene coding for 2-hydroxyisocaproate-CoA transferase and a gene coding for polyhydroxyalkanoate synthase are introduced and which has a potential of producing polyhydroxyalkanoate bearing an aromatic monomer or a long-chain 2-HA monomer and a method for producing polyhydroxyalkanoate bearing an aromatic monomer or a long-chain 2-HA monomer, using the recombinant microorganism. According to the present invention, a biodegradable polymer bearing an aromatic monomer or a long-chain 2-HA monomer can be produced.

The present invention generally relates to the field of biotechnology as it applies to the production of aryl sulfates using recombinant host cells. More particularly, the present invention pertains to recombinant host cells comprising (e.g., expressing) a polypeptide having aryl sulfotransferase activity, wherein said recombinant host cells have been modified to have an increased uptake of sulfate compared to identical host cells that does not carry said modification. Further provided are processes for the production of aryl sulfates, such as zosteric acid, employing such recombinant host cells.

The invention provides a genetically modified bacterial cell capable of improved iron-sulfur cluster delivery, characterized by a modified gene encoding a mutant Iron Sulfur Cluster Regulator (IscR) as well as one or more transgenes encoding polypeptides that enhance the biosynthesis of either biotin, lipoic acid or thiamine. The invention provides a method for producing either biotin, lipoic acid or thiamine using the genetically modified bacterium of the invention; as well as for the use of the genetically modified bacterial cell for either biotin, lipoic acid or thiamine production.

The present invention provides a 2-OST mutant exhibiting a high activity. Specifically, the present invention provides a 2-O-sulfation enzyme mutant, having a substitution of a leucine residue at position 321 with a basic amino acid residue in any one amino acid sequence of: (a) the amino acid sequence of SEQ ID NO: 2; (b) an amino acid sequence comprising one or several amino acid substitutions, deletions, insertions, or additions in the amino acid sequence of SEQ ID NO: 2; (c) an amino acid sequence having 90% or more identity to the amino acid sequence of SEQ ID NO: 2; (d) the amino acid sequence consisting of amino acid residues at positions 69 to 356 in the amino acid sequence of SEQ ID NO: 2; (e) an amino acid sequence comprising one or several amino acid substitutions, deletions, insertions, or additions in the amino acid sequence consisting of amino acid residues at positions 69 to 356 in the amino acid sequence of SEQ ID NO: 2; (f) an amino acid sequence having 90% or more identity to the amino acid sequence consisting of amino acid residues at positions 69 to 356 in the amino acid sequence of SEQ ID NO: 2; and having a 2-O-sulfate transfer activity.

The present disclosure provides a method for detecting L-serine based on cysteine desulfurase-containing living Escherichia coli cells, and belongs to the technical field of amino acid detection. The method includes the following steps: incubating an unknown sample with the cysteine desulfurase-containing living E. coli cells to produce a red substance, and qualitatively or semi-quantitatively detecting L-serine content in the unknown sample according to color changes of the red substance of the living E. coli cells, or quantitatively detecting L-serine content in the unknown sample by measuring absorbance of a lysate of the living E. coli cells. The detection method provided by the present disclosure is simple and convenient in process, few in reaction steps and stable in enzymatic activity of living cells.