Abstract: A DNA fragment which encodes a polypeptide defined in the following (a) or (b), and a polypeptide defined in the following (c) or (d): (a) a polypeptide which has at least the amino acid sequence of the amino acid numbers 50 to 393 in SEQ ID NO: 2 shown in Sequence Listing, (b) a polypeptide which has at least the amino acid sequence of the amino acid numbers 50 to 393 in SEQ ID No: 2 shown in Sequence Listing including substitution, deletion, insertion, addition, or inversion of one or several amino acids, and can constitute a protein having a carbamoyl-phosphate synthetase activity with a large subunit of carbamoyl-phosphate synthetase having the amino acid sequence comprising at least the amino acid numbers 55 to 1113 of SEQ ID NO: 3, (c) a polypeptide which has the amino acid sequence comprising at least the amino acid numbers 55 to 1113 of SEQ ID NO: 3 shown in Sequence Listing, (d) a polypeptide which has the amino acid sequence comprising at least the amino acid numbers 55 to 1113 of SEQ ID NO: 3 s

Abstract: The present invention provides a process for producing an L-amino acid which comprises culturing in a nutrient medium a microorganism which is capable of producing the L-amino acid and which can not grow in a synthetic medium containing said L-amino acid as the sole nitrogen source in an amount of 5 mg/ml or below, allowing the L-amino acid to accumulate in the culture, and recovering the L-amino acid from the culture.

Abstract: 2-Aminopropane is used as the amine donor in the stereoselective synthesis of a chiral amine from a ketone with a transaminase. In a typical embodiment, (S)-1-methoxy-2-aminopropane is prepared by bringing methoxyacetone into contact with a transaminase in the presence of 2-aminopropane as an amine donor until a substantial amount of methoxyacetone is converted to (S)-1-methoxy-2-aminopropane and 2-aminopropane is converted to acetone. In a second embodiment, L-alanine is prepared by bringing pyruvic acid into contact with a transaminase in the presence of 2-aminopropane as an amine donor.

Abstract: Disclosed is a process for preparing acylated amino esters and a process for preparing optically active amino esters from racemic amino esters with a carboxylic ester as acylating agent, whose acid component has a halogen, nitrogen, oxygen or sulfur atom neighboring the carbonyl carbon atom, in the presence of a hydrolase selected from the group of amidase, protease, esterase and lipase, and subsequent separation of the enantioselectively acylated amino ester from the non-acylated other enantiomer of the amino ester.

Abstract: The present invention provides a process for producing an L-amino acid which comprises culturing in a nutrient medium a microorganism which is capable of producing the L-amino acid and which can not grow in a synthetic medium containing said L-amino acid as the sole nitrogen source in an amount of 5 mg/ml or below, allowing the L-amino acid to accumulate in the culture, and recovering the L-amino acid from the culture.

Abstract: A method for determining three-dimensional structural information of a protein which involves producing the protein in a form substantially labeled with .sup.13 C of .sup.15 N or both substantially labeled with .sup.15 N and .sup.13 C and partially labeled with .sup.2 H and subjecting the protein to nuclear magnetic resonance spectroscopic analysis. The isotopically labeled protein is produced by a method which involves producing a substantially labeled microbial protein hydrolysate, subjecting the protein hydrolysate to cation exchange chromatography to produce a partially purified labeled amino acid mixture, subjecting the partially purified labeled amino acid mixture to anion exchange chromatography to produce a purified labeled amino mixture and supplementing the purified labeled amino acid mixture with isotopically labeled cysteine and optionally with isotopically labeled glutamine and asparagine.

Abstract: The present invention relates to materials and methods for production of natural and unnatural D-amino acids. In particular, the present invention relates to a fermentation method for the production of D-amino acids using recombinant host cells.Specifically, the invention relates to a method for producing a D-amino acid in a cell, comprising:(a) incorporating into the cell a D-aminotransferase gene and a L-aminodeaminase gene;(b) culturing the cell in a cell culture medium; and(c) isolating the D-amino acid from the cell culture medium.The invention also relates to a method for producing D-phenylalanine in a cell, comprising:(a) incorporating into the cell a D-aminotransferase gene, a L-aminodeaminase gene and means for increasing production of phenylpyruvate;(b) culturing the cell in a cell culture medium; and(c) isolating the D-phenylalanine from the cell culture medium.The invention also relates to the preparation of recombinant cells for use in the production of enantiomerically pure D-amino acids.

Abstract: DSM 9771 is a mutant of DSM 7330 which was obtained under selective pressure. Its enzymatic activity is higher by a factor of 2.3 than that of its parent organism. In the presence of an inducer, this activity may be farther increased by a factor of 2.7. The reaction catalyzed by this microorganism or enzymes therefrom is the enantioselective conversion of a D-5-monosubstituted hydantoin or an L-5-monosubstituted hydantoin or a D-N-carbamoyl amino acid or an L-N-carbamoyl amino acid to a corresponding L-.alpha.-amino acid.

Abstract: Culturing an L-amino acid producing microorganism belonging to the genus Brevibacterium or Corynebacterium and having a resistance to a peptide containing glutamic acid or aspartic acid gives L-amino acids in high yield.

Abstract: A nutrient medium comprising amino acids and other substrates used by mammalian or insect cells in protein synthesis that are either double-labeled with .sup.2 H and .sup.13 C or triple-labeled with .sup.2 H, .sup.13 C and .sup.15 N is disclosed. The invention is also directed to a method for producing the nutrient medium.

Abstract: D-arginine and L-ornithine are prepared by means of the enzymatic conversion of DL-arginine in the presence of an L-arginase which selectively converts L-arginase to L-ornithine, permitting recovery of both D-arginine and L-ornithine.

Abstract: An arginase batch capable of producing ornithine with reduced consumption of enzyme. The arginase batch is stabilized by the addition of a reducing agent in at least a 10-fold molar amount relative to the arginase.

Abstract: The invention relates to coryneform microorganisms capable of assimilating lactose which carry a recombinant DNA capable of conferring the ability to assimilate lactose on coryneform microorganisms; and to a process for producing L-amino acids which comprises culturing said coryneform microorganism capable of assimilating lactose in a culture medium containing lactose to form an amino acid, and recovering said amino acid accumulated in the culture broth. Further, the invention relates to a method for preparing recombinant plasmids containing a DNA fragment essential to the expression of a gene in coryneform microorganisms.

Abstract: Salts of L-ornithine are prepared by means of the enzymatic conversion of arginine to L-ornithine in the presence of the enzyme L-arginase in an aqueous medium in such a manner that the acid whose salt is to be prepared is used for the adjustment of the pH for the enzymatic conversion and for the subsequent neutralization of the reaction mixture and that the salt formed is isolated directly from the reaction mixture.

Abstract: A basic L-amino acid and an acidic L-amino acid may be concurrently produced by either culturing a basic L-amino acid-producing bacteria under conditions for producing an acidic L-amino acid or mix-culturing a basic L-amino acid-producing bacteria and an acidic L-amino acid-producing bacteria.

Abstract: Culturing an L-amino acid producing microorganism belonging to the genus Brevibacterium or corynebacterium and having a resistance to a dipeptide containing glutamic acid or aspartic acid gives L-amino acids in high yield.

Abstract: L-arginine is produced in high yields by culturing a microorganism of the genus Brevibacterium or the genus Cornyebacterium, which is resistant to a compound of the formula X-guanidine, wherein X is an aliphatic group or derivative thereof. The preferred microorganisms are Brevibacterium flavum FERM BP-2227 and Corynebacterium glutamicum FERM BP-2228.

Abstract: The present invention relates to yeast with a high arginine content which belongs to Kluyveromyces polysporus and has resistance to ethionine.

Abstract: The present invention is directed to a process for producing (-) 2-substituted-ornithines comprising contacting a 2-substituted-piperidone with L-.alpha.-E-aminocaprolactam-hydrolas in the presence of a divalent cation.

Abstract: A basic L-amino acid and an acidic L-amino acid may be concurrently produced by either culturing a basic L-amino acid-producing bacteria under conditions for producing an acidic L-amino acid or mix-culturing a basic L-amino acid-producing bacteria and an acidic L-amino acid-producing bacteria.

Abstract: A process for producing L-ornithine by fermentation which comprises culturing a L-ornithine-producing microorganism is disclosed. The microorganism used belongs to the genus Brevibacterium, Corynebacterium, or Arthrobacter, has auxotrophy for arginine and/or citrulline, and has resistance to microphenolic acid and/or ornithinol.

Abstract: A process is provided for producing an L-amino acid, which entails culturing bacteria producing the L-amino acid in a medium containing cane molasses, sucrose or glucose as a main carbon source and containing at least one substance selected from the group consisting of N-methylglycine, N,N-dimethylglycine, N,N,N-trimethylglycine and (2-hydroxyethyl)trimethyl ammonium in an amount effective to enhance the yield of the L-amino acid; and harvesting the L-amino acid, and wherein the L-amino acid is selected from the group consisting of L-glutamic acid, L-lysine, L-glutamine, L-arginine, L-isoleucine, L-valine, L-threonine, L-histidine, L-phenylalanine, L-tryptophan, L-serine, L-ornithine, L-citrulline, L-tyrosine and L-leucine.

Abstract: Pharmaceutically pure physiologically active N.sup.G -aminoarginine (i.e., the L or D,L form) or pharmaceutically acceptable salt thereof is administered in a nitric oxide synthesis inhibiting amount to a subject in need of such inhibition (e.g. a subject with low blood pressure or needing immunosuppressive effect) or is added to a medium containing isolated organs, intact cells, cell homogenates or tissue homogenates in an amount sufficient to inhibit nitric oxide formation to elucide or control the biosynthesis, metabolism or physiological role of nitric oxide.N.sup.G -amino-L-arginine is prepared and isolated as a pharmaceutically pure compound by reducing N.sup.G -nitro-L-arginine, converting L-arginine by-product to L-ornithine with arginase and separating N.sup.G -amino-L-arginine from the L-ornithine. N.sup.G -amino-D,L-arginine is prepared in similar fashion starting with N.sup.G -nitro-D,L-arginine.

Abstract: The disclosure relates to a process for the preparation of L-amino acids of general Formula I ##STR1## wherein A means the residue of an amino acid molecule, from D,L-aminonitriles of general Formula II ##STR2## wherein A has the meaning given above, characterized by fermenting the .alpha.-aminonitriles with a culture of Actinetobacter calcoaceticus DSM 3875 and reacting the thus-obtained D,L-amino acid amides of general Formula III ##STR3## wherein A has the meaning given above, with a culture of a microorganism containing amino acid amide racemases and L-amino acid amide amidases.

Abstract: Process is described for the production of L-amino acids of general formula I ##STR1## in which R.sub.1 means an alkyl radical with at most 12 carbon atoms optionally substituted by hydroxy groups, mercapto groups, halogen atoms, amino groups, carbonyl groups or guanidino groups and/or interrupted by oxygen atoms, nitrogen atoms or sulfur atoms, and in the case of mercapto compounds of formula I also their dithio compounds, characterized in that the microorganism Nocardia spec. DSM 3306 or its enzymes are allowed to act on a D,L-imidazolidinedione derivative of general formula II ##STR2## in which R.sub.1 has the above-named meaning or, in the case of mercapto compounds of formula II, also in their dithio compounds.

Abstract: Disclosed is a process for producing L-arginine, which comprises culturing in a medium a coryneform glutamic acid-producing bacterium having resistance to cysteine or a cysteine analogue and an ability to produce L-arginine, accumulating L-arginine in the culture and recovering the L-arginine therefrom.

Abstract: A process for recovering a high-purity L-amino acid from a fermentation liquor obtained by fermentation or an enzymic method, which comprises removing the impurities contained in said fermentation liquor by passing said fermentation liquor through an ultrafilter membrane and then through an ion-exchange or adsorbent resin; concentrating or cooling the effluent thus obtained to result in crystallization of said L-amino acid, and isolating said crystalline L-amino acid from said fermentation liquor.

Abstract: L-arginine is produced by constructing a recombinant DNA composed of a vector DNA and a DNA fragment derived from chromosomal DNA of a microorganism belonging to the genus Corynebacterium or Brevibacterium and bearing genetic information relating to the synthesis of L-arginine-biosynthetic enzyme, introducing the recombinant DNA in a microorganism belonging to the genus Corynebacterium or Brevibacterium, culturing the microorganism in a medium, and recovering L-arginine accumulated in the culture broth.

Abstract: A process for recovering a high-purity L-amino acid from a fermentation liquor obtained by fermentation or an enzymic method, which comprises removing the impurities contained in said fermentation liquor by passing said fermentation liquor through an ultrafilter membrane and then through an ion-exchange or adsorbent resin; concentrating or cooling the effluent thus obtained to result in crystallization of said L-amino acid, and isolation said crystalline L-amino acid from said fermentation liquor.

Abstract: A substantial elevation of the space-time yield is achieved in the preparation of D-.alpha.-amino acids by means of the biotransformation of hydantoins which are monosubstituted in the 5-position in an aqueous medium in the presence of cells of the microorganism Agrobacterium radiobacter if the biotransformation is carried out under a elevated pressure at the start of the reaction. A further improvement results if this elevated pressure is maintained for a period of at least 16 hours, then removed and the biotransformation continued at atmospheric pressure.

Abstract: To improve the yield and/or reduce the energy cost in carrying out a microbiological or enzymatic process in a reactor and to make the reaction conditions essentially independent of the size of the reactor, it is proposed to make use, as a reactor, of an endless circulation tube in which the reaction components are circulated essentially according to a plug flow and in this process are fed through one or more in-line mixers fitted inside the tube. This method and reactor are suitable in particular for the preparation by fermentation of polysaccharides, especially xanthan, in which water, a production medium containing one or more sugars and nutrient salts and an inoculating material of a suitable aerobic bacterium are introduced into the said reactor tube and exposed to fermentation with air being supplied.

Abstract: Process for treating a xanthan gum in order to improve the filterability of its aqueous solutions, comprising an enzymatic treatment of an aqueous solution of xanthan gum containing, as dissolved salts, a proportion of alkali and/or alkaline-earth metals of at least 10.sup.-2 equivalent/liter, said treatment being performed by means of two enzyme extracts of different types, a so-called PG enzyme having as main activity a polygalacturonase activity and a so-called P enzyme extract whose main activity is a protease activity, in conditions compatible with the activity of said enzyme extracts. The obtained xanthan gum powder or solution can be used as enhanced oil recovery agent.

Abstract: A biocatalytic method for producing a desired amino acid is disclosed. The method involves contacting a 2-ketoacid corresponding to the desired amino acid with lactic acid, aspartic acid and ammonia, or salts thereof, in the presence of:(a) one or more transaminase enzymes capable of catalyzing the conversion of the 2-ketoacid and L-aspartic acid to the desired amino acid and oxaloacetic acid;(b) a malate-lactate transhydrogenase enzyme capable of catalyzing the conversion of lactic acid and oxaloacetic acid to pyruvic acid and malic acid;(c) a fumarase enzyme capable of catalyzing the conversion of malic acid to fumaric acid; and(d) an aspartate-ammonia lyase enzyme capable of catalyzing the conversion of fumaric acid and ammonia to aspartic acid.

Abstract: Disclosed is a process for producing L-arginine by transforming a host microorganism belonging to the genus Corynebacterium or Brevibacterium with a recombinant DNA of a DNA fragment containing a gene involved in the biosynthesis of L-arginine and a vector DNA, culturing the transformant in a nutrient medium, accumulating L-arginine in the culture medium and recovering L-arginine therefrom.

Abstract: An L-arginine producing microorganism which is constructed by transforming into a recipient strain of the genus Escherichia of a vector having inserted therein an arg A gene derived from a chromosomal DNA of the genus Escherichia, is useful for the production of high levels of L-arginine by fermentation.

Abstract: Mutants of the genus Bervibacterium or Corynebacterium are given resistance to keto-malonic acid, fluoro-malonic acid, monofluoro-acetic acid or aspartate antagonist and used to produce L-arginine by aerobic fermentation.

Abstract: D-.alpha.-amino acids are produced by contacting a 5-substituted hydantoin with an effective amount of an enzyme capable of converting the 5-substituted hydantoin to the D-.alpha.-amino acid produced by a microorganism in an aqueous medium at a pH in the range of 4 to 9, the microorganism being capable of utilizing the D-isomer of the 5-substituted hydantoin as the sole nitrogen source, but substantially incapable of utilizing the L-isomer of the 5-substituted hydantoin as the nitrogen source and the substituent of the 5-position being such that upon reaction with the enzyme, an optically active D-.alpha.-amino acid isomer is produced; and recovering the D-.alpha.-amino acid which accumulates in the aqueous medium.