Abstract: Disclosed is use of ?-nicotinamide mononucleotide in the preparation of anti-aging drugs or health-care products. A single dose of the ?-nicotinamide mononucleotide is 1-500 mg/Kg body weight/day, and the drug or health-care product is in the form of tablets, capsules, granules, aqueous solutions, enteric-coated preparations or injections.

Abstract: A health care product having nicotinamide mononucleotide as the active ingredient, and the use of nicotinamide mononucleotide in preparing health care products for the prevention and treatment of arteriosclerosis and cardiovascular and cerebrovascular diseases caused by arteriosclerosis.

Abstract: A medication having nicotinamide mononucleotide as the active ingredient, and the use of nicotinamide mononucleotide in preparing medications for the prevention and treatment of arteriosclerosis and cardiovascular and cerebrovascular diseases caused by arteriosclerosis.

Abstract: Disclosed is use of nicotinamide adenine dinucleotide (NADH) or a salt thereof in the preparation of drugs or health-care products for treating phenylketonuria (PKU), wherein a single dose of the NADH or a salt thereof is 1-100 mg.

Abstract: Disclosed is use of nicotinamide adenine dinucleotide (NADH) and ?-nicotinamide mononucleotide (NMN) in the preparation of drugs or health-care products for treating Parkinson's disease, in which ?-NADH and ?s-NMN are produced enzymatically.

Abstract: The present invention discloses a method for purifying reduced form of ?-nicotinamide adenine dinucleotide, comprising the steps of: sequentially microfiltrating and nanofiltrating a reaction solution obtained after an enzymatic reaction, to collect a concentrate for use; then adding an ion pair reagent to the concentrate, and purifying by gradient elution using a reverse-phase chromatographic column as a stationary phase, a buffer solution as a phase A, and ethanol as a phase B; changing the cations in the purified filtrate into sodium ions by using a cation exchange resin; and nanofiltrating the filtrate obtained in Step c, and finally freeze drying it in a vacuum freeze drier. In the present invention, the reduced form of ?-nicotinamide adenine dinucleotide is purified by reverse phase high performance liquid chromatography and cation exchange, such that the reduced form of ?-nicotinamide adenine dinucleotide has a high purity and high yield, thus meeting the requirements in industry.

Abstract: The present invention discloses a method for purifying oxidized form of ?-nicotinamide adenine dinucleotide, comprising the steps of: sequentially microfiltrating and nanofiltrating a reaction solution obtained after an enzymatic reaction by using filteration membranes, to collect a concentrate for use; then adding an acid to the concentrated filtrate, to adjust the pH of the concentrate, and purifying by gradient elution using a reverse-phase chromatographic column as a stationary phase, a buffer solution as a phase A, and ethanol as a phase B; and concentrating the purified solution by nanofiltrating it with a filtration membrance, and then freeze drying it in a vacuum freeze drier. In the present invention, the oxidized form of ?-nicotinamide adenine dinucleotide is purified by reverse phase high performance liquid chromatography, such that the oxidized form of ?-nicotinamide adenine dinucleotide has a high purity and high yield, thus meeting the requirements in industry.

Abstract: The present invention discloses an oxidized form of ?-nicotinamide adenine dinucleotide phosphate and a method for purifying the same. The method comprises specifically the steps of: a. sequentially microfiltrating and nanofiltrating a pretreated coenzyme II solution with membrane concentration devices, to obtain a concentrated crude product solution; b. adjusting the obtained crude product solution to pH 2-4, loading it onto a preparative reverse phase high performance liquid chromatographic column, and purifying by gradient elution, to obtain a purified sample solution; and c. nanofiltrating the purified sample solution with a membrane concentration device, and freeze drying it in a vacuum freeze drier, to obtain a purified coenzyme II. The coenzyme II prepared in the present invention has a high purity, a high yield, and thus a promising prospect in the market.

Abstract: The present invention discloses a method for purifying ?-nicotinamide mononucleotide, comprising the steps of: a. sequentially microfiltrating and nanofiltrating a pretreated ?-nicotinamide mononucleotide solution with membrane concentration devices, to collect a concentrated crude product solution; b. adjusting the obtained crude product solution to pH 3-7, loading it onto a preparative reverse phase high performance liquid chromatographic column, and purifying by gradient elution using an octadecylsilane-bonded silica gel as a stationary phase, a hydrochloric acid solution at pH 3-7 as a mobile phase A, and ethanol as a mobile phase B, to obtain a purified sample solution; and c. nanofiltrating the purified sample solution with a membrane concentration device, and freeze drying it in a vacuum freeze drier, to obtain purified ?-nicotinamide mononucleotide.

Abstract: This invention provides a series of recombinant Thermoanaerobacterium saccharolyticum glucose isomerases with improved catalytic activity and thermostability obtained by using recombinant techniques. These recombinant glucose isomerases comprise amino acid variation including phenylalanine (Phe) at position 139, alanine (Ala) at position 182, serine (Ser) at position 187, and glutamine (Gin) at position 299, and carry at least one additional mutated amino acid at position 87, position 217, position 260 or position 276, and possess a higher catalytic activity than that of the wild-type when using D-glucose as substrate. These recombinant glucose isomerases can be used for direct production of high fructose corn syrup containing 55% [wt] or higher concentration of fructose.

Abstract: This invention provides use of a series of recombinant Thermoanaerobacterium saccharolyticum glucose isomerases with improved catalytic activity obtained by using recombinant techniques. These mutants comprise at least one amino acid variation at position 87, position 139, position 182, position 187, position 217, position 260, position 276, or position 299, and can be used in the conversion of hemicellulose to ethanol.

Abstract: This invention provides a series of recombinant Thermoanaerobacterium saccharolyticum glucose isomerases with improved catalytic activity and thermostability obtained by using recombinant techniques. These recombinant glucose isomerases comprise amino acid variation including phenylalanine (Phe) at position 139, alanine (Ala) at position 182, serine (Ser) at position 187, and glutamine (Gin) at position 299, and carry at least one additional mutated amino acid at position 87, position 217, position 260 or position 276, and possess a higher catalytic activity than that of the wild-type when using D-glucose as substrate. These recombinant glucose isomerases can be used for direct production of high fructose corn syrup containing 55% [wt] or higher concentration of fructose.

Abstract: This invention describes a series of recombinant Thermoanaerobacterium saccharolyticum glucose isomerases having improved catalytic activity and thermostability. The recombinant glucose isomerases can be used for direct production of fructose syrup containing 55 wt % or higher concentration of fructose, or used for the production of fructose syrup containing less than 55 wt % fructose.

Abstract: The invention discloses a series of Methanococcus jannaschii S-adenosylmethionine synthetase mutants with improved thermostability and high catalytic activity obtained by using gene mutation technique, characterized in that these mutants refer to an enzyme using Sequence 2 in the Sequence Listing as the reference sequence and contains at least one mutation at position 102, position 93, position 230, and position 357 and has a catalytic activity at least 70% higher than that of the wild-type S-adenosylmethionine synthetase using adenosine triphosphate (ATP) and methionine as substrates. These S-adenosylmethionine synthetase mutants can be used in the production of S-adenosylmethionine.

Abstract: This invention provides a series of recombinant Thermoanaerobacterium saccharolyticum glucose isomerases with improved catalytic activity and thermostability obtained by using recombinant techniques. These recombinant glucose isomerases comprise amino acid variation including phenylalanine (Phe) at position 139, alanine (Ala) at position 182, serine (Ser) at position 187, and glutamine (Gin) at position 299, and carry at least one additional mutated amino acid at position 87, position 217, position 260 or position 276, and possess a higher catalytic activity than that of the wild-type when using D-glucose as substrate. These recombinant glucose isomerases can be used for direct production of high fructose corn syrup containing 55% [wt] or higher concentration of fructose.

Abstract: This invention provides a series of recombinant Thermoanaerobacterium saccharolyticum glucose isomerases with improved catalytic activity and thermostability obtained by using recombinant techniques. These recombinant glucose isomerases comprise amino acid variation including phenylalanine (Phe) at position 139, alanine (Ala) at position 182, serine (Ser) at position 187, and glutamine (Gln) at position 299, and carry at least one additional mutated amino acid at position 87, position 217, position 260 or position 276, and possess a higher catalytic activity than that of the wild-type when using D-glucose as substrate. These recombinant glucose isomerases can be used for direct production of high fructose corn syrup containing 55% [wt] or higher concentration of fructose.

Abstract: This invention provides a series of recombinant Thermoanaerobacterium saccharolyticum glucose isomerases with improved catalytic activity and thermostability obtained by using recombinant techniques. These recombinant glucose isomerases comprise amino acid variation including phenylalanine (Phe) at position 139, alanine (Ala) at position 182, serine (Ser) at position 187, and glutamine (Gln) at position 299, and carry at least one additional mutated amino acid at position 87, position 217, position 260 or position 276, and possess a higher catalytic activity than that of the wild-type when using D-glucose as substrate. These recombinant glucose isomerases can be used for direct production of high fructose corn syrup containing 55.% [wt] or higher concentration of fructose.

Abstract: This invention provides use of a series of recombinant Thermoanaerobacterium saccharolyticum glucose isomerases with improved catalytic activity obtained by using recombinant techniques. These mutants comprise at least one amino acid variation at position 87, position 139, position 182, position 187, position 217, position 260, position 276, or position 299, and can be used in the conversion of hemicellulose to ethanol.

Abstract: The invention discloses a series of Methanococcus jannaschii S-adenosylmethionine synthetase mutants with improved thermostability and high catalytic activity obtained by using gene mutation technique, characterized in that these mutants refer to an enzyme using Sequence 2 in the Sequence Listing as the reference sequence and contains at least one mutation at position 102, position 93, position 230, and position 357 and has a catalytic activity at least 70% higher than that of the wild-type S-adenosylmethionine synthetase using adenosine triphosphate (ATP) and methionine as substrates. These S-adenosylmethionine synthetase mutants can be used in the production of S-adenosylmethionine.

Abstract: This invention provides a series of recombinant Thermoanaerobacterium saccharolyticum glucose isomerases with improved catalytic activity and thermostability obtained by using recombinant techniques. These recombinant glucose isomerases comprise amino acid variation including phenylalanine Phe) at position 139, alanine (Ala) at position 182, serine (Ser) at position 187, and glutamine (Gln) at position 299, and carry at least one additional mutated amino acid at position 87, position 217, position 260 or position 276, and possess a higher catalytic activity than that of the wild-type when using D-glucose as substrate. These recombinant glucose isomerases can be used for direct production of high fructose corn syrup containing 55.% [wt] or higher concentration of fructose.