62 results about "D-tagatose" patented technology

There is disclosed a method for disrupting biofilm and for inhibiting biofilm formation in an aqueous environment that comprises contacting said environment with an effective amount of D-tagatose.

A reduced calorie frozen beverage comprising: (a) at least one non-nutritive sweetener, (b) erythritol, (c) D-tagatose, (d) maltodextrin, and (e) a nutritive sweetener.

A combination of a sugar alcohol and D-tagatose is used to produce naturally sweetened, diet beverages or food products. The sugar alcohol and D-tagatose can also be used in combination with one or more nutritive sweeteners to lower the calories of a full-calorie beverage or food product while preserving the taste.

Recombinant microorganisms are useful for producing xylitol by fermentation of arabinose. The recombinant microorganisms are produced by transformation of host microorganisms with heterologous polynucleotide sequences coding for each of L-xylulose reductase, D-tagatose 3-epimerase, and L-arabinose isomerase, which transformants express the heterologous polynucleotides at a sufficient functional level to be effective to produce xylitol from arabinose. Production of xylitol is effected by contacting these recombinant microorganisms with a substrate comprising arabinose under conditions effective to produce xylitol from arabinose.

Oral intake of D-tagatose in a prebiotic food induces production of butyrate and stimulates the growth of beneficial bacteria in the human colon. Therefore it is believed to be useful in food or the like as preventive drug against colon cancer.

The invention discloses a recombinant L-arabinose isomerase (L-AI) as well as a gene and preparation method thereof and a method for preparing D-tagatose by utilizing the L-AI. Especially bacillus subtilis is used for expressing L-arabinose isomerase, the recombinant L-arabinose isomerase with biological activity is obtained, and the L-AI is more beneficial to industrial production of D-tagatose. The preparation method disclosed by the invention has the characteristic of simplicity, high efficiency and short cycle.

The invention provides an incretin-associated medicine capable of restraining secretion of GIP completely and promoting secretion of GLP-1 and highly safe. The medicine capable of promoting the secretion of GLP-1 (glucagon-like peptide-1) and restraining the secretion of the GIP (glucose-dependent insulinotropic peptide) comprises non-antagonistic inhibitor of clastic enzyme of cane sugar, such as L-gum sugar, D-wood sugar and D-tagatose, as an active ingredient.

The invention relates to a method for preparing D-tagatose and L-tagatose from dulcitol in the technical field of biology, which comprises the following steps: preparing a culture medium; inoculating acid-producing bacteria into the culture medium to prepare primary seed liquid and secondary seed liquid; culturing the second seed liquid to obtain a water solution containing the D-tagatose and the L-tagatose. The invention also relates to a preparation method adopting resting cell technology, which comprises the following steps: inoculating the acid-producing bacteria into the culture medium to be cultured; centrifugating the cultured bacteria after finishing the to form somatic cells, suspending the somatic cells by using the water solution containing the D-tagatose, and culturing the water solution to obtain the water solution containing the D-tagatose and the L-tagatose. The invention also relates to a preparation method adopting immobilized cell technology, which comprises the following steps: inoculating the acid-producing bacteria into the culture medium to be cultured; centrifugating the cultured bacteria after finishing the culture to obtain somatic cells; obtaining the water solution containing the D-tagatose and the L-tagatose by adopting the immobilized cell technology. The methods of the invention are green and safe, have high conversion efficiency, and can prepare the D-tagatose and the L-tagatose of pharmaceutical grade.

The invention discloses L-AI (L-arabinose isomerase). The L-AI is prepared through the step as follows: 279th phenylalanine of L-AI of Bacillus coagulans NL01 is mutated into isoleucine, and the L-AI is obtained, wherein the GenBank registration number of a nucleotide sequence of an L-AI gene araA is KX356659. The invention further discloses escherichia coli containing the L-AI as well as a construction method and an application of the escherichia coli. According to the constructed recombinant escherichia coli, F279I expressed by the escherichia coli has high catalytic efficiency on D-galactose. The optimal reaction temperature of a whole-cell catalysis reaction system is mild, a browning reaction can be avoided, and the L-AI better facilitates industrial production of D-tagatose when compared with wild type L-AI and other common L-AI from thermophilic bacteria and thermoacidophiles. Meanwhile, the whole-cell catalysis reaction system adopts simple components and has greater industrial production and application potential and economic value.

The invention discloses a method for preparing D-tagatose by an enzyme process. The method comprises the following steps: 1) separately establishing engineering bacteria containing galactitol dehydrogenase gene and engineering bacteria containing NADH oxidase gene or establishing coexpression engineering bacteria containing galactitol dehydrogenase gene and NADH oxidase gene; 2) fermenting the established engineering bacteria to obtain a whole cell containing galactitol dehydrogenase and NADH oxidase; and 3) with the whole cell containing galactitol dehydrogenase and NADH oxidase or the free enzyme of galactitol dehydrogenase and NADH oxidase as a catalyst, catalyzing the galactitol by taking NAD+ as a hydrogen acceptor in a weakly alkaline condition to obtain D-tagatose. Compared with traditional production method depending on L-arabinose isomerase, in the invention, the substrate conversion rate is high (>99.0%) and the product is easy to separate; and moreover, the co-product of a coenzyme circulation system adopted in the method is water which does not influence the separation and purification of the principal product.

The current disclosure provides a process for enzymatically converting a saccharide into tagatose. The invention also relates to a process for preparing tagatose where the process involves converting fructose 6-phosphate (F6P) to tagatose 6-phosphate (T6P), catalyzed by an epimerase, and converting the T6P to tagatose, catalyzed by a phosphatase.

The present invention relates to a low calorie coffee mix composition with a natural sweet taste prepared by using D-tagatose instead of sugar for a diet or a low calorie coffee mix.

The present invention is directed towards genetic modification of native gene encoding for D-tagatose 3-epimerase and rhamnose isomerase to substantially increase the expression level of these enzymes and use of said enzymes in a process to produce rare monosaccharides such as psicose and allose. Also disclosed in the present invention is expression constructs comprising the modified genes and a host cells to express the same.

Pharmaceutical compositions including D-tagatose along with a stilbene or stilbenoid component, or a salt or derivative thereof. Methods of prophylaxis and therapy by administering to a mammal a pharmaceutically effective amount of D-tagatose, optionally in combination with a stilbene or stilbenoid component, or a salt or derivative thereof to prevent or treat atherosclerosis, the metabolic syndrome, obesity, or diabetes.

The invention belongs to the technical field of bioengineering and specifically relates to a method for biosynthesis of D-tagatose by an immobilized enzyme catalyst. The method for biosynthesis of theD-tagatose by the immobilized enzyme catalyst is as follows: first, recombinant Bacillus subtilis is prepared, and an L-arabinose isomerase immobilized enzyme catalyst is constructed; and recombinantBacillus subtilis spores are added to a D-galactose reaction solution for transformation by oscillation under certain conditions to obtain the D-tagatose. The novel food-safe immobilized enzyme catalyst is constructed, the biotransformation process for biosynthesis of the D-tagatose by the immobilized enzyme catalyst is optimized, the transformation rate is improved, the specific activity of theimmobilized enzyme catalyst is as high as 2.10* 10<-9> U/spore, and the transformation rate of the D-tagatose reaches 95%. A new green, safe, high-efficiency and economical D-tagatose synthesis technology and method are developed, the high-efficiency production of the food-grade D-tagatose is realized, and the method has broad industrial application prospects.

The invention belongs to the field of biology and chemical industry, and particularly discloses a method for continuously producing D-tagatose by adopting D-galactose as a raw material on the basis of enzymatic isomerization reaction and a continuous chromatographic separation in-situ coupling technology. The method comprises the following steps of preparing a buffering solution; adequately dissolving the thermophilic L-arabinose isomerase in the water to obtain an enzyme solution; adequately dissolving D-galactose in the water to obtain a raw material solution; mixing and preheating the raw material solution, the buffering solution and the enzyme solution to obtain a feeding solution of a simulated moving bed reactor (SMBR); and placing the feeding solution into the SMBR to obtain a D-tagatose product solution through the in-situ reaction and separation. By determining the appropriate operating condition of the SMBR, the conversion rate of the D-galactose reaches more than 80 percent, the purity of the D-tagatose reaches more than 95 percent, and the yield is more than 80 percent. The method is low in cost, less in pollution and high in conversion rate; moreover, continuity in production can be realized, the consistency of the product quality can be guaranteed, and the commercialized application prospect is good.