Abstract: The purpose of the present invention is to provide an organism having an ergothioneine productivity that is capable of easily producing ergothioneine within a short period of time at a high yield, as compared with a conventional technology, and, therefore, enables ergothioneine production on an industrial scale. This purpose can be achieved by a transformed fungus into which a gene encoding enzyme (1) or genes encoding enzymes (1) and (2) have been inserted and in which the inserted gene(s) are overexpressed. (1) an enzyme catalyzing a reaction of synthesizing hercynyl cysteine sulfoxide from histidine and cysteine in the presence of S-adenosyl methionine, iron (II) and oxygen. (2) An enzyme catalyzing a reaction of synthesizing ergothioneine from hercynyl cysteine sulfoxide using pyridoxal 5?-phosphate as a coenzyme.

Abstract: The present invention provides a method for allowing a used inert material that has been subjected to a reaction once, which is disposed of in the background art, to be used again as well as a brand-new one. A method of recovering an inert material of the present invention is characterized by in the fixed-bed reactor, the inert material is loaded in an inert material layer provided between a first-stage catalyst layer and a second-stage catalyst layer, the first-stage catalyst layer is loaded with a first-stage catalyst for producing acrolein from propylene, and the second-stage catalyst layer is loaded with a second-stage catalyst for producing acrylic acid from acrolein, the method comprising the steps of: extracting the inert material from the fixed-bed reactor; washing the extracted inert material; and screening the washed inert material.

Abstract: DNA and recombinant DNA that encode a peptide-forming enzyme, a method for producing a peptide-forming enzyme, and a method for producing a dipeptide are disclosed. A method for producing a dipeptide includes producing a dipeptide from a carboxy component and an amine component by using a culture of a microbe belonging to the genus Sphingobacterium and having the ability to form the dipeptide from the carboxy component and the amine component, a microbial cell separated from the culture, treated microbial cell product of the microbe or a peptide-forming enzyme derived from the microbe.

Abstract: A fermented seasoning which does not have the bitterness specific to peptides and can be easily ingested orally, in spite of containing large amount of peptides is provided. Namely, a fermented seasoning obtained by adding salt water to an Aspergillus culture or a mixture of the Aspergillus culture with a plant-derived protein material and by controlling the leucine aminopeptidase-I activity in the moromi to be 1.0 U/ml or less, and also controlling the leucine aminopeptidase-II activity in the moromi to be 0.5 U/ml or less, within 10 days after the preparation.

Abstract: It is an object of the present invention to provide a procedure for realizing inexpensive and simple production of 3-indole-pyruvic acid. A transformant is made using a polynucleotide having a specific nucleotide sequence encoding a protein having an oxidase activity, and oxidase is generated by culturing the transformant in a medium to accumulate the oxidase in the medium and/or the transformant. Further, tryptophan is converted into 3-indole-pyruvic acid in the presence of the transformant and/or a culture thereof to produce 3-indole-pyruvic acid.

Abstract: It is an object of the present invention to provide a procedure for realizing inexpensive and simple production of 3-indole-pyruvic acid. A transformant is made using a polynucleotide having a specific nucleotide sequence encoding a protein having an oxidase activity, and oxidase is generated by culturing the transformant in a medium to accumulate the oxidase in the medium and/or the transformant. Further, tryptophan is converted into 3-indole-pyruvic acid in the presence of the transformant and/or a culture thereof to produce 3-indole-pyruvic acid.

Abstract: It is an object of the present invention to provide a procedure for realizing inexpensive and simple production of 3-indole-pyruvic acid. A transformant is made using a polynucleotide having a specific nucleotide sequence encoding a protein having an oxidase activity, and oxidase is generated by culturing the transformant in a medium to accumulate the oxidase in the medium and/or the transformant. Further, tryptophan is converted into 3-indole-pyruvic acid in the presence of the transformant and/or a culture thereof to produce 3-indole-pyruvic acid.

Abstract: DNA and recombinant DNA that encode a peptide-forming enzyme, a method for producing a peptide-forming enzyme, and a method for producing a dipeptide are disclosed. A method for producing a dipeptide includes producing a dipeptide from a carboxy component and an amine component by using a culture of a microbe belonging to the genus Sphingobacterium and having the ability to form the dipeptide from the carboxy component and the amine component, a microbial cell separated from the culture, treated microbial cell product of the microbe or a peptide-forming enzyme derived from the microbe.

Abstract: A method of producing an ?-L-aspartyl-L-phenylalanine-?-ester by forming the ?-L-aspartyl-L-phenylalanine-?-ester from L-aspartic acid-?,?-diester and L-phenylalanine using an enzyme or enzyme-containing substance that has an ability to selectively link L-phenylalanine to an ?-ester site of the L-aspartic acid-?,?-diester through a peptide bond.

Abstract: A method of producing an ?-L-aspartyl-L-phenylalanine-?-ester by forming the ?-L-aspartyl-L-phenylalanine-?-ester from L-aspartic acid-?,?-diester and L-phenylalanine using an enzyme or enzyme-containing substance that has an ability to selectively link L-phenylalanine to an ?-ester site of the L-aspartic acid-?,?-diester through a peptide bond.

Abstract: DNA and recombinant DNA that encode a peptide-forming enzyme, a method for producing a peptide-forming enzyme, and a method for producing a dipeptide are disclosed. A method for producing a dipeptide includes producing a dipeptide from a carboxy component and an amine component by using a culture of a microbe belonging to the genus Sphingobacterium and having the ability to form the dipeptide from the carboxy component and the amine component, a microbial cell separated from the culture, treated microbial cell product of the microbe or a peptide-forming enzyme derived from the microbe.

Abstract: DNA and recombinant DNA that encode a peptide-forming enzyme, a method for producing a peptide-forming enzyme, and a method for producing a dipeptide are disclosed. A method for producing a dipeptide includes producing a dipeptide from a carboxy component and an amine component by using a culture of a microbe belonging to the genus Sphingobacterium and having the ability to form the dipeptide from the carboxy component and the amine component, a microbial cell separated from the culture, treated microbial cell product of the microbe or a peptide-forming enzyme derived from the microbe.

Abstract: A method of producing an ?-L-aspartyl-L-phenylalanine-?-ester by forming the ?-L-aspartyl-L-phenylalanine-?-ester from L-aspartic acid-?,?-diester and L-phenylalanine using an enzyme or enzyme-containing substance that has an ability to selectively link L-phenylalanine to an ?-ester site of the L-aspartic acid-?,?-diester through a peptide bond.

Abstract: A method of producing an ?-L-aspartyl-L-phenylalanine-?-ester by forming the ?-L-aspartyl-L-phenylalanine-?-ester from L-aspartic acid-?,?-diester and L-phenylalanine using an enzyme or enzyme-containing substance that has an ability to selectively link L-phenylalanine to an ?-ester site of the L-aspartic acid-?,?-diester through a peptide bond.

Abstract: A method of producing an ?-L-aspartyl-L-phenylalanine-?-ester by forming the ?-L-aspartyl-L-phenylalanine-?-ester from L-aspartic acid-?,?-diester and L-phenylalanine using an enzyme or enzyme-containing substance that has an ability to selectively link L-phenylalanine to an ?-ester site of the L-aspartic acid-?,?-diester through a peptide bond.

Abstract: A method of producing an ?-L-aspartyl-L-phenylalanine-?-ester by forming the ?-L-aspartyl-L-phenylalanine-?-ester from L-aspartic acid-?,?-diester and L-phenylalanine using an enzyme or enzyme-containing substance that has an ability to selectively link L-phenylalanine to an ?-ester site of the L-aspartic acid-?,?-diester through a peptide bond.

Abstract: DNA and recombinant DNA that encode a peptide-forming enzyme, a method for producing a peptide-forming enzyme, and a method for producing a dipeptide are disclosed. A method for producing a dipeptide includes producing a dipeptide from a carboxy component and an amine component by using a culture of a microbe belonging to the genus Sphingobacterium and having the ability to form the dipeptide from the carboxy component and the amine component, a microbial cell separated from the culture, treated microbial cell product of the microbe or a peptide-forming enzyme derived from the microbe.

Abstract: The present invention provides a method for producing a dipeptide from starting materials that are available at low costs through a route industrially advantageous and simple. Dipeptides are produced from amino acid esters and amino acids by using a culture of a microbe having an ability to produce a dipeptide from an amino acid ester and an amino acid, microbial cells separated from the culture, or treated microbial cell product.

Abstract: DNA and recombinant DNA that encode a peptide-forming enzyme, a method for producing a peptide-forming enzyme, and a method for producing a dipeptide are disclosed. A method for producing a dipeptide includes producing a dipeptide from a carboxy component and an amine component by using a culture of a microbe belonging to the genus Sphingobacterium and having the ability to form the dipeptide from the carboxy component and the amine component, a microbial cell separated from the culture, treated microbial cell product of the microbe or a peptide-forming enzyme derived from the microbe.

Abstract: A method of producing an ?-L-aspartyl-L-phenylalanine-?-ester by forming the ?-L-aspartyl-L-phenylalanine-?-ester from L-aspartic acid-??-diester and L-phenylalanine using an enzyme or enzyme-containing substance that has an ability to selectively link L-phenylalanine to an ?-ester site of the L-aspartic acid-??-diester through a peptide bond.