Patent classifications
C12N11/00
Structures and methods of manufacturing structures using biological based materials
A structure for a turbine, the structure comprising a body having a multi-layer construction including an interior layer with substantially uniform concentrations throughout of facultative anaerobic organisms (FAO) that have gene sets capable of producing the enzyme urease and/or the proteins purloin, lustre A and perlustrin, along with glucose, and non-uniform concentrations throughout of a structural composition, the structural composition including a chitin-based component with silk fibronectin and water; an exterior layer of urea, water, calcium ions and facultative anaerobic organisms (FAOs) including urease, aragonite; and a binding layer of conchiolin protein intermediate the interior layer and the exterior layer. The facultative anaeorobic organisms (FAOs) are organisms classified in one of the Saccharomyces, Escherichia and Bacillus genuses.
Structures and methods of manufacturing structures using biological based materials
A structure for a turbine, the structure comprising a body having a multi-layer construction including an interior layer with substantially uniform concentrations throughout of facultative anaerobic organisms (FAO) that have gene sets capable of producing the enzyme urease and/or the proteins purloin, lustre A and perlustrin, along with glucose, and non-uniform concentrations throughout of a structural composition, the structural composition including a chitin-based component with silk fibronectin and water; an exterior layer of urea, water, calcium ions and facultative anaerobic organisms (FAOs) including urease, aragonite; and a binding layer of conchiolin protein intermediate the interior layer and the exterior layer. The facultative anaeorobic organisms (FAOs) are organisms classified in one of the Saccharomyces, Escherichia and Bacillus genuses.
Dephosphorylated lysosomal storage disease proteins and methods of use thereof
Provided are substantially dephosphorylated forms of lysosomal storage disease (LSD) proteins, including dephosphorylated forms of iduronate-2-sulfatase (IDS, or I2D) and iduronidase (IDU), having increased ability to traverse or penetrate the blood brain barrier (BBB) relative to phosphorylated forms of the protein, and p97 conjugates thereof. Also provided are compositions comprising such dephosphorylated LSD proteins and p97 conjugates, and methods of use thereof, for instance, to treat any one or more lysosomal storage diseases, such as Hunter Syndrome (or MPS Type II).
Dephosphorylated lysosomal storage disease proteins and methods of use thereof
Provided are substantially dephosphorylated forms of lysosomal storage disease (LSD) proteins, including dephosphorylated forms of iduronate-2-sulfatase (IDS, or I2D) and iduronidase (IDU), having increased ability to traverse or penetrate the blood brain barrier (BBB) relative to phosphorylated forms of the protein, and p97 conjugates thereof. Also provided are compositions comprising such dephosphorylated LSD proteins and p97 conjugates, and methods of use thereof, for instance, to treat any one or more lysosomal storage diseases, such as Hunter Syndrome (or MPS Type II).
Method for preparing peptide fragments, kit for preparing peptide fragments to be used therein, and analysis method
A method of proteolyzing a protein, including immobilizing a protein in at least one pore of a porous body, and contacting the protein immobilized in the pore and a protease immobilized on a solid surface such that the protease selectively accesses a site of the protein and proteolyzes the protein at the site.
Method for preparing peptide fragments, kit for preparing peptide fragments to be used therein, and analysis method
A method of proteolyzing a protein, including immobilizing a protein in at least one pore of a porous body, and contacting the protein immobilized in the pore and a protease immobilized on a solid surface such that the protease selectively accesses a site of the protein and proteolyzes the protein at the site.
?-1,6-GLUCANASE MUTANT, AND METHOD FOR MEASURING ?-1,6-GLUCAN
A β-1,6-glucanase mutant which is a mutant of β-1,6-glucanase (EC 3.2.1.75), wherein a Glu residue located at a position corresponding to Glu (E)-321 in SEQ ID NO: 1 is substituted by an amino acid residue X or a Glu (E) residue located at a position corresponding to each of Glu (E)-225 and Glu (E)-321 in SEQ ID NO: 1 is substituted by an amino acid residue X, wherein the amino acid residue (X) is selected from the group consisting of Gln (Q), Gly (G), Ala (A), Leu (L), Tyr (Y), Met (M), Ser (S), Asn (N), and His (H); and a method for measuring β-1,6-glucan, including measuring β-1,6-glucan bonded to the mutant.
Cell printing apparatus
A cell printing apparatus according to the present disclosure comprises: a nozzle through which a liquid cell substance is discharged; a container in which the liquid cell substance discharged through the nozzle is laminated into a three-dimensional structure; and a supply unit for supplying the liquid heated to a predetermined temperature to the container.
Cell printing apparatus
A cell printing apparatus according to the present disclosure comprises: a nozzle through which a liquid cell substance is discharged; a container in which the liquid cell substance discharged through the nozzle is laminated into a three-dimensional structure; and a supply unit for supplying the liquid heated to a predetermined temperature to the container.
ENGINEERED DECARBOXYLASE POLYPEPTIDES AND THEIR USES IN PREPARING TYRAMINE AND DOPAMINE
Provided herein are engineered decarboxylase polypeptides that are useful for catalyzing the decarboxylation of amino acids such as L-tyrosine to produce tyramine or catalyzing the decarboxylation of L-DOPA to produce dopamine. Also provided are the preparation process of engineered decarboxylase polypeptides as well as reaction process under industrial-relevant conditions. The disclosure also provides polynucleotide sequences encoding engineered decarboxylase polypeptides, recombinant host cells capable of expressing engineered decarboxylase polypeptides, and methods of producing tyramine or dopamine using the engineered decarboxylase polypeptides. Compared to the wild type decarboxylase, the engineered polypeptide provided by this disclosure has better activity and/or stability. The use of the engineered polypeptides for the preparation of tyramine or dopamine reduces the production cost and has a good industrial application prospect.