Abstract: The invention aims at providing a process for producing coenzyme Q10 efficiently in microorganisms by utilizing a coenzyme Q10 side chain synthesis gene derived from a fungal species belonging to the genus Aspergillus and genus Leucosporidium.

Abstract: The present invention provides a method of producing a long-chain prenyl diphosphate synthase (in particular decaprenyl diphosphate synthase and solanesyl diphosphate synthase) using a gene and a protein which are required for enabling or enhancing the activity expression of a eukaryote-derived long-chain prenyl diphosphate synthase as well as a method of efficiently producing a coenzyme Q having a long-chain isoprenoid in its side chain (in particular coenzyme Q9 or coenzyme Q10) using a microorganism.

Abstract: The present invention has for its object to isolate a gene coding for the enzyme synthesizing the coenzyme Q10 side chain from a fungal strain of the genus Saitoella and exploit it to advantage for the efficient microbial production of coenzyme Q10. The present invention provides; a DNA having the nucleotide sequence shown under SEQ ID NO:1 a DNA having a nucleotide sequence derived from the nucleotide sequence of SEQ ID NO:1 by the deletion, addition, insertion and/or substitution of one or a plurality of nucleotides and coding for a protein having decaprenyl diphosphate synthase activity a DNA which hybridizes with the DNA having the nucleotide sequence of SEQ ID NO:1 under a stringent condition and codes for a protein having decaprenyl diphosphate synthase activity.

Abstract: The invention aims at providing a process for producing coenzyme Q10 efficiently in microorganisms by utilizing a coenzyme Q10 side chain synthesis gene derived from a fungal species belonging to the genus Rhodotorula.

Abstract: Primaiy supernatant liquid collector 1 allows blood A to separate into a primary supernatant liquid B and red blood cells by leaving the blood A stationary for a prescribed period of time, and then it discharges the primary supernatant liquid B and physiological saline W in the same amount into a first treatment container 13 and a first balance container 14, respectively. Centrifuge 61 centrifuges the above primary supernatant liquid B using the first balance container 14 as a balance weight, and a secondary supernatant liquid in the first treatment container 13 is transferred to a second treatment container 109 by take-out device 91 and at the same time the physiological saline W in the same amount as the transferred secondary supernatant liquid is transferred from the first balance container 14 to a second balance container 110.

Abstract: Primary supernatant liquid collecting means 1 allows blood A to separate into a primary supernatant liquid B and red blood cells by leaving the blood A stationary for a prescribed period of time, and then it discharges the primary supernatant liquid B and physiological saline W in the same amount into a first treatment container 13 and a first balance container 14, respectively.

Abstract: A gene of decaprenyl diphosphate synthase, which is the key gene participating in the biosynthesis of coenzyme Q10 was isolated from a bacterium belonging to the family Rhizobiaceae. By transferring this gene into a microorganism such as Escherichia coli and expressing therein, coenzyme Q10 can be effectively produced.

Abstract: A DNA fragment coding for a decarbamylase protein improved in thermostability as the result of replacement of at least one base of a DNA fragment coding for a decarbamylase protein derived from a microorganism with another base and the resultant replacement of at least one of the corresponding amino acids, and its production process; a vector containing the DNA fragment; a transformant obtained by transformation with the vector; as well as a decarbamylase improved in thermostability and its production process. Also disclosed is a process for producing a D-.alpha.-amino acid, which comprises converting an N-carbamoyl-D-.alpha.-amino acid into the corresponding D-.alpha.-amino acid in an aqueous medium by the action of a decarbamylase having a thermostable temperature of 65.degree. C. or higher; and collecting the D-.alpha.-amino acid produced.

Abstract: A process for the efficient production of a D-amino acid from the corresponding DL-5-substituted hydantoin by one-step reaction which comprises using a composite immobilized enzyme at a pH about neutrality, said composite immobilized enzyme being obtained by immobilizing a hydantoinase having its optimal pH within an alkaline range and a D-N-carbamyl-.alpha.-amino acid amidohydrolase having its optimal pH about neutrality in a coexisting state on an immobilizing support, simultaneously, is disclosed.

Abstract: In a process for the production of a D-.alpha.-amino acid, in which an N-carbamyl-D-.alpha.-amino acid corresponding to the general formula: ##STR1## wherein R represents phenyl, hydroxy-substituted phenyl, substituted or unsubstituted alkyl, or thienyl, is converted by a microbial enzyme in an aqueous medium to a D-.alpha.-amino acid corresponding to the general formula: ##STR2## wherein R is the same as defined above, decarbamylase produced by a microorganism of the genus Comamonas, Blastobacter, Alcaligenes, Sporosarcina, Rhizobium, Bradyrhizobium or Arthrobacter is used as the enzyme converting the N-carbamyl-D-.alpha.-amino acid to the D-.alpha.-amino acid.The conversion of the N-carbamyl-D-.alpha.-amino acids to the D-.alpha.-amino acids is carried out in a neutral to alkaline pH range.

Abstract: In a process for the production of a D-.alpha.-amino acid, in which an N-carbamyl-D-.alpha.-amino acid corresponding to the general formula: ##STR1## wherein R represents phenyl, hydroxy-substituted phenyl, substituted or unsubstituted alkyl, or thienyl, is converted by a microbial enzyme in an aqueous medium to a D-.alpha.-amino acid corresponding to the general formula: ##STR2## wherein R is the same as defined above, decarbamylase produced by a microorganism of the genus Comamonas, Blastobacter, Alcaligenes, Sporosarcina, Rhizobium, Bradyrhizobium or Arthrobacter is used as the enzyme converting the N-carbamyl-D-.alpha.-amino acid to the D-.alpha.-amino acid.The conversion of the N-carbamyl-D-.alpha.-amino acids to the D-.alpha.-amino acids is carried out in a neutral to alkaline pH range.

Abstract: Decarbamylases are provided capable of producing D-.alpha.-amino acids by hydrolysis of N-carbamyl-D-.alpha.-amino acids. A source of the decarbamylases is recombinant microorganisms produced by gene manipulation methods. Decarbamylases having improved thermostability can be obtained in which amino acids at a thermostability-related site of a natural decarbamylase have been replaced with other amino acids by mutating a DNA fragment encoding the natural decarbamylase. Recombinant DNA is obtained from a vector DNA and a DNA fragment encoding a natural decarbamylase where the nucleic acid sequence encoding an amino acid at a thermostability-related site is replaced with a nucleic acid sequence encoding another amino acid. The recombinant DNA is used to produce transformants that produce thermostable decarbamylases.

Abstract: The present invention is directed to a gene which is related to a D-N-carbamoyl-.alpha.-amino acid amidohydrolase which is an enzyme capable of converting D-N-carbamoyl-.alpha.-amino acids into D-.alpha.-amino acids; a recombinant plasmid in which a DNA fragment containing the gene is incorporated into a vector; a microorganism belonging to the genus Escherichia, Pseudomonas, Flavobacterium, Bacillus, Serratia, Corynebacterium, or Brevibacterium, which is transformed by incorporating the recombinant plasmid thereinto; a process for the production of D-N-carbamoyl-.alpha.-amino acid amidohydrolases, comprising the steps of cultivating the transformed microorganism and collecting the desired product therefrom; a D-N-carbamoyl-.alpha.-amino acid amidohydrolase obtained by the method; and a process for the production of D-.alpha.-amino acids with the aid of an action of the enzyme.The D-N-carbamoyl-.alpha.-amino acid amidohydrolase can be fixed on a support for immobilization and used as an immobilized enzyme.

Abstract: The present invention is directed to a gene which is related to a D-N-carbamoyl-.alpha.-amino acid amidohydrolase which is an enzyme capable of converting D-N-carbamoyl-.alpha.-amino acids into D-.alpha.-amino acids; a recombinant plasmid in which a DNA fragment containing the gene is incorporated into a vector; a microorganism belonging to the genus Escherichia, Pseudomonas, Flavobacterium, Bacillus, Serratia, Corynebacterium, or Brevibacterium, which is transformed by incorporating the recombinant plasmid thereinto; a process for the production of D-N-carbamoyl-.alpha.-amino acid amidohydrolases, comprising the steps of cultivating the transformed microorganism and collecting the desired product therefrom; a D-N-carbamoyl-.alpha.-amino acid amidohydrolase obtained by the method; and a process for the production of D-.alpha.-amino acids with the aid of an action of the enzyme.The D-N-carbamoyl-.alpha.-amino acid amidohydrolase can be fixed on a support for immobilization and used as an immobilized enzyme.

Abstract: A TPA variant with replacement of amino acids is provided. In a typical embodiment, the variant has an amino acid sequence with replacement of the amino acid group consisting of asparagine at the 37th position, serine at the 38th position, glycine at the 39th position, arginine at the 40th position, alanine at the 41st position, and glutamine at the 42nd position from the N-terminus of the amino acid sequence of mature human tissue plasminogen activator.