Abstract: The present disclosure provides a method for preparing a nicotinamide mononucleotide cocrystal, and aims to solve the technical problems of larger content/weight difference and inconsistent quality of nicotinamide mononucleotide (NMN) medicines or health care products due to poor fluidity of existing nicotinamide mononucleotide crystals. The method includes the steps of mixing nicotinamide mononucleotide as an active pharmaceutical ingredient with isonicotine as a cocrystal former by adopting solution synthesis and then performing crystal precipitation. The method has the advantages of simple operation and wide application range.

Abstract: The present invention provides a method for preparation of an enzyme-modified stevia sugar. The method includes the steps of adding a ?-fructosidase to a solution in which a stevia sugar raw material and sucrose are dissolved to obtain a reaction solution, adjusting the pH of the reaction solution to be 5.0-8.0, maintaining a reaction temperature at 20-45° C., and after a reaction with stirring, collecting the enzyme-modified stevia sugar. The stevia sugar raw material includes one or more of stevioside and rebaudioside A, and the ?-fructosidase is derived from Microbacterium saccharophilum or Aspergillus japonicus. The preparation method takes a short time, is efficient and convenient to operate, low in cost, high in conversion rate, green and environmentally friendly, and can be widely applied to industrial scale production. The present invention further provides an enzyme for preparation of the enzyme-modified stevia sugar and application thereof.

Abstract: An acid phosphatase mutant, and method for preparing nicotinamide riboside by same. The mutant is a protein of the following (a), (b) or (c): (a) a protein, having an amino acid sequence shown in SEQ ID NO: 3; (b) a protein, derived from (a), having catalytic activity higher than an acid phosphatase parent having an amino acid sequence shown in SEQ ID NO: 2, obtained by substituting, deleting or adding several amino acids in the amino acid sequence shown in SEQ ID NO: 3, using nicotinamide mononucleotide as a substrate; (c) a protein, having catalytic activity higher than the acid phosphatase shown in SEQ ID NO: 2, having 90% or more homology with the amino acid sequence of the protein defined by (a) or (b), and using nicotinamide mononucleotide as a substrate. It is used to prepare nicotinamide riboside and the conversion rate can be 99%.

Abstract: A nicotinamide riboside composition and preparation method thereof, the icotinamide riboside composition comprises nicotinamide riboside and/or a salt thereof and konjac glucomannan or rebaudioside A. The nicotinamide riboside composition provided by the present invention, used to increase the concentration of NAD in cells, thereby preventing and improving various unhealthy conditions caused by NAD deficiency. is stable in property and easy to store and transport.

Abstract: The present invention provides a method for preparing nicotinamide mononucleotide (NMN) by bioanalysis. The method includes a step of catalytically reacting a plurality of raw materials including nicotinamide, ATP, and ribose in the presence of nicotinamide phosphoribosyltransferase (Nampt), ribose phosphate pyrophosphokinase, and ribokinase, to prepare the NMN.

Abstract: An NADH compound, and a formulation and use thereof, relating to the technical field of biomedicine and health care products. The NADH compound includes NADH or its physiologically acceptable salt and L-carnitine or its physiologically acceptable salt, and can be used as a weight loss product. The NADH compound has an increased effect in weight loss, and may achieve long-term drug administration of the product.

Abstract: The present invention relates to a process for purifying crude NADPH product prepared by biocatalysis. The objective of the present invention is to solve the technical problems of low yield and low purity of the purified product in the existing ion exchange resin method. The present invention comprises sequentially the following steps: pretreatment, loading onto an ion column, elution of cations, pre-elution of impurities etc. The yield of the purification process disclosed in the present invention can be up to 85% or higher and the purified NADPH has a purity of up to 98% or higher.

Abstract: The present invention discloses a Nicotinamide phosphoribosyltransferase (nampt) mutant and use thereof. The present invention relates to a nicotinamide phosphoribosyltransferase (Nampt) mutant artificially obtained through genic site-directed mutation. An object of the present invention is to provide a Nampt mutant having a catalytic activity higher than that of a conventional wild type parent, wherein the enzymatic activity of the Nampt mutant provided in the present invention is 1.2-6.9 times of the enzymatic activity of the parent.

Abstract: The present invention relates to a process for purifying crude NADPH product prepared by biocatalysis. The objective of the present invention is to solve the technical problems of low yield and low purity of the purified product in the existing ion exchange resin method. The present invention comprises sequentially the following steps: pretreatment, loading onto an ion column, elution of cations, pre-elution of impurities etc. The yield of the purification process disclosed in the present invention can be up to 85% or higher and the purified NADPH has a purity of up to 98% or higher.

Abstract: The present invention discloses a Nicotinamide phosphoribosyltransferase (nampt) mutant and use thereof. The present invention relates to a nicotinamide phosphoribosyltransferase (Nampt) mutant artificially obtained through genic site-directed mutation. An object of the present invention is to provide a Nampt mutant having a catalytic activity higher than that of a conventional wild type parent, wherein the enzymatic activity of the Nampt mutant provided in the present invention is 1.2-6.9 times of the enzymatic activity of the parent.

Abstract: A method for purifying a salt of reduced form of ?-nicotinamide adenine dinucleotide (NADH) includes: sequentially microfiltrating and nanofiltrating a reaction solution obtained after an enzymatic reaction, collecting a concentrate for use; adding an ion pair reagent to the concentrate, and purifying by gradient elution to obtain a purified filtrate 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 to obtain a filtrate by using a cation exchange resin; and nanofiltrating the filtrate, and freeze drying in a vacuum freeze drier. The method results in an excellent purity and yield of a salt of NADH that meets requirements in industry.

Abstract: A method for purifying ?-nicotinamide mononucleotide (NMN) includes: sequentially microfiltrating and nanofiltrating a crude product solution containing NMN using membrane concentration devices to obtain a concentrated crude product solution; adjusting the concentrated crude product solution to pH 3-7 to obtain a loading solution, loading the loading solution 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 100% ethanol as a mobile phase B, to obtain a purified sample solution; concentrating the purified sample solution by nanofiltration and freeze drying in a vacuum freeze drier to obtain a purified NMN.

Abstract: The present invention discloses a Nicotinamide phosphoribosyltransferase (nampt) mutant and use thereof. The present invention relates to a nicotinamide phosphoribosyltransferase (Nampt) mutant artificially obtained through genic site-directed mutation. An object of the present invention is to provide a Nampt mutant having a catalytic activity higher than that of a conventional wild type parent, wherein the enzymatic activity of the Nampt mutant provided in the present invention is 1.2-6.9 times of the enzymatic activity of the parent.

Abstract: The present invention discloses a Nicotinamide phosphoribosyltransferase (nampt) mutant and use thereof. The present invention relates to a nicotinamide phosphoribosyltransferase (Nampt) mutant artificially obtained through genic site-directed mutation. An object of the present invention is to provide a Nampt mutant having a catalytic activity higher than that of a conventional wild type parent, wherein the enzymatic activity of the Nampt mutant provided in the present invention is 1.2-6.9 times of the enzymatic activity of the parent.

Abstract: The present invention provides a method for preparing nicotinamide mononucleotide (NMN) by biocatalysis. The method includes a step of catalytically reacting a plurality of raw materials including nicotinamide, ATP, and ribose in the presence of nicotinamide phosphoribosyltransferase (Nampt), ribose phosphate pyrophosphokinase, and ribokinase, to prepare the NMN.

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: 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.