The present disclosure relates to methods for detecting brain tumors and assessing the recurrence of such tumors by administering a pharmaceutical composition comprising 5-aminolevulinic acid (5-ALA) and detecting the conversion of 5-ALA to protoporphyrin IX (PPIX) associated with brain-derived microparticles.

The present disclosure relates to methods for detecting brain tumors and assessing the recurrence of such tumors by administering a pharmaceutical composition comprising 5-aminolevulinic acid (5-ALA) and detecting the conversion of 5-ALA to protoporphyrin IX (PPIX) associated with brain-derived microparticles.

The present invention provides a mutated histidine decarboxylase suitable for a practical use. Specifically, the present invention provides a mutated histidine decarboxylase having at least one amino acid residue mutated as compared to a wild-type histidine decarboxylase, and having higher histidine decarboxylase activity and/or stability than the wild-type histidine decarboxylase, and also a use thereof. The mutated histidine decarboxylase has Motifs (1) to (6), and an amino acid residue in at least one motif thereof can be mutated. The mutated histidine decarboxylase can also have a mutation of at least one amino acid residue in an amino acid sequence designated by SEQ ID NO: 3 and in a homologous sequence thereto.

The present invention provides a mutated histidine decarboxylase suitable for a practical use. Specifically, the present invention provides a mutated histidine decarboxylase having at least one amino acid residue mutated as compared to a wild-type histidine decarboxylase, and having higher histidine decarboxylase activity and/or stability than the wild-type histidine decarboxylase, and also a use thereof. The mutated histidine decarboxylase has Motifs (1) to (6), and an amino acid residue in at least one motif thereof can be mutated. The mutated histidine decarboxylase can also have a mutation of at least one amino acid residue in an amino acid sequence designated by SEQ ID NO: 3 and in a homologous sequence thereto.

A method for distinguishing among a first group of microorganisms belonging to a first taxon of Gram negative bacteria, the first group of bacteria exhibiting a mechanism of resistance to a treatment; a second group of microorganisms belonging to a second taxon of Gram negative bacteria, the second taxon of bacteria being different than said first taxon, and exhibiting a mechanism of resistance to a treatment identical to the mechanism of the first group; and a third group of Gram negative bacteria that is not resistant to the treatment.

A method for distinguishing among a first group of microorganisms belonging to a first taxon of Gram negative bacteria, the first group of bacteria exhibiting a mechanism of resistance to a treatment; a second group of microorganisms belonging to a second taxon of Gram negative bacteria, the second taxon of bacteria being different than said first taxon, and exhibiting a mechanism of resistance to a treatment identical to the mechanism of the first group; and a third group of Gram negative bacteria that is not resistant to the treatment.

Lipogenic yeasts bioengineered to overexpress genes for lipid production, and methods of use thereof. The yeasts are modified to express, constitutively express, or overexpress an acetyl-CoA carboxylase, an alpha-amylase, an ATP citrate lyase, a diacylglycerol acyltransferase, a fatty acid synthase, a glycerol kinase, a 6-phosphogluconate dehydrogenase, a glycerol-3-phosphate dehydrogenase, a malic enzyme, a fatty acyl-CoA reductase, a delta-9 acyl-CoA desaturase, a glycerol-3-phosphate acyltransferase, a lysophosphatidate acyltransferase, a glucose-6-phosphate dehydrogenase, a beta-glucosidase, a hexose transporter, a glycerol transporter, a glycoside hydrolase enzyme, an auxiliary activity family 9 enzyme, or combinations thereof. The yeasts in some cases are also modified to reduce or ablate activity of certain proteins. The methods include cultivating the yeast to convert low value soluble organic stillage byproducts into lipids suitable for biodiesel production and other higher value uses.

Lipogenic yeasts bioengineered to overexpress genes for lipid production, and methods of use thereof. The yeasts are modified to express, constitutively express, or overexpress an acetyl-CoA carboxylase, an alpha-amylase, an ATP citrate lyase, a diacylglycerol acyltransferase, a fatty acid synthase, a glycerol kinase, a 6-phosphogluconate dehydrogenase, a glycerol-3-phosphate dehydrogenase, a malic enzyme, a fatty acyl-CoA reductase, a delta-9 acyl-CoA desaturase, a glycerol-3-phosphate acyltransferase, a lysophosphatidate acyltransferase, a glucose-6-phosphate dehydrogenase, a beta-glucosidase, a hexose transporter, a glycerol transporter, a glycoside hydrolase enzyme, an auxiliary activity family 9 enzyme, or combinations thereof. The yeasts in some cases are also modified to reduce or ablate activity of certain proteins. The methods include cultivating the yeast to convert low value soluble organic stillage byproducts into lipids suitable for biodiesel production and other higher value uses.

The present invention provides a mutated histidine decarboxylase suitable for a practical use. Specifically, the present invention provides a mutated histidine decarboxylase having at least one amino acid residue mutated as compared to a wild-type histidine decarboxylase, and having higher histidine decarboxylase activity and/or stability than the wild-type histidine decarboxylase, and also a use thereof. The mutated histidine decarboxylase has Motifs (1) to (6), and an amino acid residue in at least one motif thereof can be mutated. The mutated histidine decarboxylase can also have a mutation of at least one amino acid residue in an amino acid sequence designated by SEQ ID NO: 3 and in a homologous sequence thereto.

The present invention provides a mutated histidine decarboxylase suitable for a practical use. Specifically, the present invention provides a mutated histidine decarboxylase having at least one amino acid residue mutated as compared to a wild-type histidine decarboxylase, and having higher histidine decarboxylase activity and/or stability than the wild-type histidine decarboxylase, and also a use thereof. The mutated histidine decarboxylase has Motifs (1) to (6), and an amino acid residue in at least one motif thereof can be mutated. The mutated histidine decarboxylase can also have a mutation of at least one amino acid residue in an amino acid sequence designated by SEQ ID NO: 3 and in a homologous sequence thereto.