Abstract: 4-(Indol-3-ylmethyl)-4-hydroxy-2-oxoglutarate, which is useful as an intermediate in the synthesis of monatin, may be synthesized from indole pyruvic acid and pyruvic acid (and/or oxalacetic acid) by using a novel aldolase derived from the genus Pseudomonas, Erwinia, Flavobacterium, or Xanthomonas.

Abstract: A D-aminotransferase can be modified so as to efficiently produce (2R,4R)-monatin having high sweetness intensity from 4-(indol-3-ylmethyl)-4-hydroxy-2-oxoglutaric acid by substituting an amino acid at least at one of positions (positions 100, 180 to 183, 243 and 244) involved in efficiently producing the (2R,4R)-monatin in an amino acid sequence of a wild-type D-aminotransferase represented in SEQ ID NO:2.

Abstract: The present invention relates to a method for producing optically active IHOG, which can in turn be used for the production of monatin. The present invention further relates to a method for producing optically active monatin, and aldolase used for these methods. As such, the present invention enables the synthesis of 4-(Indole-3-ylmethyl)-4-hydroxy-2-oxoglutaric acid with high optical purity, which is useful as an intermediate in the synthesis of optically active monatin, from indole pyruvic acid and pyruvic acid (or oxaloacetic acid).

Abstract: The present invention provides a method for producing a peptide, comprising culturing a transformant introduced with an expression vector to prepare a culture, and mixing the culture with a carboxy component and an amine component to form the peptide. The expression vector comprises a polynucleotide encoding a protein: (A) having selected deletions in the amino acid sequence of SEQ ID NO:2, (B) having a mutation of one or several amino acid residues in any protein selected from said group (A); (C) having 70% or more amino acid sequence identity to any protein selected from said group (A), (D) encoded by a polynucleotide that hybridizes under a stringent condition with a polynucleotide consisting of a nucleotide sequence complementary to a polynucleotide encoding any protein selected from said group (A), and (E) encoded by a polynucleotide having 70% or more nucleotide sequence identity to the polynucleotide encoding any protein selected from the group (A).

Abstract: The present invention is to provide an industrially advantageous method for producing an amino acid derivative. Provided is a method for producing an amino acid derivative including contacting a microorganism and/or an enzyme with a hydroxyimino acid represented by the following general formula (I): wherein R1 represents an optionally substituted predetermined hydrocarbon group; R2 represents a C1 to C3 alkyl group or a hydrogen atom; and n is 0 or 1, to produce an amino acid derivative represented by the following general formula (III): wherein R1 and n have the same meanings as those of R1 and n in the general formula (I), wherein the microorganism and/or the enzyme is capable of catalyzing the reaction.

Abstract: Thickening agents which containing a specific N-acylamino acid (component A) and a specific amideamine (component B) are capable of generating, when used in combination with a wide variety of oily bases including a hydrocarbon oil and silicone, a creamy thickening composition having a practical dissolution temperature and a smooth feeling in use when applied to the skin.

Abstract: Mixing milk with a reaction product, which is prepared by dissolving at a high concentration highly pure milk whey protein having been separated from cow's milk, etc. and concentrated and then treating with transglutaminase, then inoculating with a lactic acid bacterium and fermenting economically affords a yogurt of agitated type, which is enriched in whey protein, shows little water release and has a rich feeling and a highly smooth texture.

Abstract: [Problem] A valine, isoleucine, leucine mixture which is excellent in the reduction of bitter taste and improved dissolution speed is provided. [Solving Means] The above problem is solved by a solid solution composed of three amino acids of valine, isoleucine, leucine, and a solid solution composed of these and at least one of acid selected from the group consisting of neutral aliphatic amino acid, neutral hydroxy amino acid, neutral acid amide amino acid, acidic amino acid, basic amino acid, hydroxy acid.

Abstract: A method is provided for producing hIGF-I with high purity and yield. This is a method for producing human insulin-like growth factor I, having a step of removing modified human insulin-like growth factor I from the human insulin-like growth factor I, the step including: (A) a step of adjusting the pH of a culture liquid of a human insulin-like growth factor I producing bacteria to 8 or more after completion of culture; (B) a step of letting the culture liquid obtained in step (A) stand; and (C) a step of removing the producing bacteria from the culture liquid obtained in step (B).

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: By searching various kinds of compounds having CaSR agonistic activity, the present invention provides CaSR agonistic agents, pharmaceutical compositions, preventive or therapeutic agents for diarrhea and kokumi-imparting agents each of which comprise the compound. More specifically, the present invention provides CaSR agonistic agents, pharmaceutical compositions, preventive or therapeutic agents for diarrhea and kokumi-imparting agents each of which comprise a glutamic acid derivative having CaSR agonistic activity or pharmaceutically acceptable salts thereof.

Abstract: A method is provided for producing a purine nucleoside, such as inosine and guanosine, and a method for producing a 5?-purine nucleotide such as 5?-inosinic acid or 5?-guanylic acid, using a bacterium belonging to the either genus Escherichia or genus Bacillus, wherein purine nucleoside productivity of said bacterium is enhanced by enhancing an activity of a protein encoded by the yeaS (leuE) gene.

Abstract: Crystals of a purine nucleoside compound, particularly crystals of 2?,3?-dideoxyinosine, which have excellent storage stability and have a concentration of phosphate attached to the crystal of 25 ppm or more, may be produce by: (1) preparing an aqueous solution containing phosphate ion (PO43?) and a purine nucleoside compound; and (2) crystallizing the purine nucleoside compound from the aqueous solution.

Abstract: The present invention provides a method of manufacturing a highly pure ammonium succinate solution including the steps of (A) producing calcium succinate trihydrate by crystallization fermentation of a microorganism; (B) converting calcium succinate trihydrate to calcium succinate monohydrate by transition crystallization; (C) separating the calcium succinate monohydrate crystals; (D) substituting the calcium salt in the calcium succinate monohydrate with ammonium salt resulting in an ammonium succinate solution; and (E) removing the solid calcium carbonate from the ammonium succinate solution.

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 bacterium belonging to the genus Escherichia which has an ability to produce L-lysine or L-threonine and which is modified so that a malic enzyme does not function normally in a cell, and a method for producing L-lysine or L-threonine, comprising culturing the bacterium in a medium to produce and cause accumulation of L-lysine or L-threonine, and collecting the L-lysine or L-threonine from the medium.

Abstract: Compounds represented by formula (I) wherein the symbols are as defined in the description, exhibit a lipase inhibitory activity, and are useful for foods, drinks, and the like.

Abstract: Provided is a method whereby a dairy product having a rich and creamy texture can be obtained by reducing or removing a reaction inhibitor of a protein deamidating enzyme contained in a raw material milk having low heat history to thereby more efficiently and more effectively treat the raw material milk having low heat history with a protein deamidating enzyme. A raw material milk having low heat history is treated with a protein deamidating enzyme after or simultaneously with a treatment, such as an addition of a calcium chelating agent, for reducing a protein deamidating enzyme inhibitor.

Abstract: The present invention provides a method for producing L-methionine by culturing a microorganism in a medium to produce and accumulate L-methionine in the medium, and collecting the L-methionine from the medium, where the microorganism is deficient in a repressor of L-methionine biosynthesis system and has L-methionine productivity.

Abstract: A method for production of L-lysine is provided which includes the steps of cultivating a methanol-utilizing bacterium in a culture medium to produce and accumulate L-lysine in the culture medium and collecting the L-lysine from the culture medium, wherein the methanol-utilizing bacterium contains DNA encoding dihydrodipicolinate synthetase which is desensitized to feedback inhibition by L-lysine and DNA encoding a LysE protein that can enhance the excretion of L-lysine out of the methanol-utilizing bacterium, and the bacterium is modified so as to increase the intracellular activities of diaminopimelic acid dehydrogenase, diaminopimelic acid decarboxylase, dihydrodipicolinic acid reductase and aspartate-semialdehyde dehydrogenase.