57 results about "Tagatose" patented technology

The invention discloses L-arabinose isomerase, engineering bacteria and application, the amino acid sequence of the L-arabinose isomerase is shown as SEQ ID NO: 3, and the gene sequence for coding the L-arabinose isomerase is shown as SEQ ID NO: 2. On the basis of a genome of a Peribacillussp.S4 strain, a gene for coding the L-arabinose isomerase is excavated, and a stable prokaryotic expression system is constructed by performing codon optimization on the gene, so that the large-scale controllable production of the L-arabinose isomerase is realized, the yield of the enzyme is remarkably increased, the production cost of the enzyme is reduced, and the method is suitable for industrial production. A stable and economical enzyme source is provided for the production of D-tagatose; the L-arabinose isomerase expressed by the constructed engineering bacteria can significantly improve the yield of D-tagatose, and industrialization of D-tagatose is facilitated.

Disclosed herein are formulations (including sweet proteins and rare sugars) for improving the sweetness of low glycemic index rare sugars without altering the texture and flavor of the rare sugars and methods for improving the sweetness of rare sugars. More specifically, the present invention discloses methods for improving the sweetness of rare sugars without altering the sweetness profile, texture and flavor of the primary sugars. The invention also discloses the addition of Brazitame protein with liquid rare sugars at different temperatures during the synthesis of the rare sugars, before crystallization or before or after caramelization of the rare sugars, to increase sweetness. The Brazilian sweet protein increases the sweetness of rare sugars, but is not limited to D-psicose, D-tagatose, D-allose, isomaltulose, trehalose, sorbose, pinose, leucobiose and the like. The invention also provides for the evaluation of non-nutritional sweeteners (such as aspartame, acesulfame, sodium cyclamate, neotame, saccharin, sucralose, stevioside, etc.), as each has a limitation of taste quality if used with rare sugars. However, the use of Brazilian sweet protein does not alter the flavor and texture of rare sugars, and the taste profile matches sucrose.

The present invention relates to a use of an enzyme belonging to the aldolase group and comprising a polypeptide having at least 30% identity with an amino acid sequence selected from SEQ ID NO: 1 to SEQ ID NO: 4, for stereoselectively preparing D-tagatose-1,6-bisphosphate (TBP) or D-tagatose-1-phosphate. The present invention also relates to a method for preparing D-tagatose-1,6-bisphosphate (TBP) or D-tagatose-1-phosphate, comprising a step of reacting, in a suitable reaction medium, dihydroxyacetone phosphate (DHAP) or at least an isomer thereof or analog thereof, and optionally D-glyceraldehyde, with an enzyme belonging to the aldolase group, said enzyme comprising a polypeptide having at least 30% identity with an amino acid sequence selected from SEQ ID NO: 1 to SEQ ID NO: 4. Finally, the present invention relates to a process for preparing D-tagatose.

The invention belongs to the technical field of food coloring, and particularly relates to a compound sweetening agent capable of coloring at low temperature for food as well as a preparation method and application of the compound sweetening agent. The D-psicose and tagatose chewable tablets are prepared from the following raw materials in parts by mass: 15 to 20 parts of D-psicose, 1 to 5 parts of tagatose, 2 to 8 parts of D-xylose, 20 to 25 parts of xylitol, 30 to 35 parts of solid maltitol, 30 to 35 parts of liquid maltitol, 10 to 14 parts of polydextrose and 0.5 to 1.5 parts of stevioside. The sweetening agent with a coloring function is perfectly combined with other sugar-free sweetening agents, so that function synergy is realized, food can quickly generate good color and luster in a low-temperature state, and the nutrition of the food is prevented from being lost.

The present application relates to a fructose-4-epimerase variant exhibiting tagatose conversion activity and a method for preparing tagatose using the same.

To provide an immobilized enzyme composition for hexose production or an improved process for hexose production. [Solution] The present invention relates to an immobilized enzyme composition for the preparation of hexoses. Examples of hexoses include tagatose, psicose, fructose, allose, mannose, galactose, altrose, talose, sorbose, gross, idose, and inositol. The present invention also relates to an enzymatic process for preparing hexoses from sugars by contacting starch derivatives with the immobilized enzyme composition of the present invention.

The utility model discloses an ion exchange device for tagatose production, which relates to the technical field of ion exchange and comprises a base, a fixing support is fixedly connected to the upper end of the base, and four fixing rods are fixedly connected to the side wall of the fixing support. The end, away from the fixing support, of the fixing rod is fixedly connected with a first exchange assembly, a second exchange assembly, a third exchange assembly and a fourth exchange assembly respectively, and the first exchange assembly, the second exchange assembly, the third exchange assembly and the fourth exchange assembly each comprise an installation cylinder. The position of the inner cylinder in the mounting cylinder can be conveniently adjusted, so that the height of the whole ion exchange assembly can be flexibly adjusted, the device can meet the mounting requirements of equipment with different heights, the applicability and the flexibility of the device are greatly enhanced, and in the mounting or dismounting process, only the limiting cylinder needs to be simply rotated, and the mounting and dismounting are convenient. Therefore, the pipeline can be quickly spliced with or detached from the liquid outlet at the lower end of the mounting cylinder and the liquid inlet at the upper end of the inner cylinder.

The present application relates to the technical field of biotechnology, and particularly relates to a tagatose-6-phosphate phosphatase mutant and a method for synthesizing tagatose from scratch. The method provided by the present application is a one-pot method for biosynthesizing D-tagatose by using starch or dextrin as a substrate, adopting a multi-enzyme cascade reaction system composed of a tagatose-6-phosphate phosphatase mutant, a glycogen-debranching enzyme, an alpha-glucan phosphorylase, a phosphoglucomutase, a glucose-6-phosphate isomerase, a D-tagatose-6-phosphate-3-epimerase and a 4-alpha-glucan transferase. The method can prepare tagatose from ordinary and inexpensive starting materials (starch or dextrin) at a high yield, improves the overall conversion rate of the system and the final yield of tagatose, provides a new technical approach for realizing low-cost and green production of tagatose, and has the advantages of high yield, low cost and being more suitable for industrial production.

The application belongs to the technical field of biology and specifically relates to a method for synthesizing D-tagatose through multi-enzyme cascade catalysis, which uses lactose as a substrate and utilizes beta-galactoside enzyme, L-arabinose isomerase, glucose isomerase, fructokinase, tagatose-1,6-diphosphate aldolase, polyphosphate kinase and phosphatase for synchronous cascade catalysis to synthesize D-tagatose. The method improves the conversion rate of D-tagatose by continuously converting the intermediate product D-glucose into D-tagatose, provides a new method for synthesizing D-tagatose from lactose, and provides certain theoretical basis and technical support for realizing the industrialized production of high-value-added D-tagatose.

The invention relates to the technical field of food, and provides a rare sugar composition and a preparation method thereof, and the rare sugar composition comprises tagatose and psicose in a mass ratio of (40-98): (2-10). The preparation method comprises the following steps: by taking lactose hydrolysate as a raw material, adding calcium hydroxide into the lactose hydrolysate for reaction, wherein the reaction product comprises the rare sugar composition. According to the rare sugar composition, the rare sugar is high in purity and clean and pure in flavor, the sweetness and taste of the rare sugar are close to those of cane sugar, the rare sugar composition can serve as a substitute of cane sugar, according to the preparation method of the rare sugar composition, lactose serves as a raw material and is isomerized into tagatose and psicose, the conversion rates of the tagatose and the psicose can reach 40% and 4% respectively, reaction conditions are mild, the preparation process is simple and controllable, and the preparation cost is low. And the production process has flexibility, rare sugar mixtures with different components and different specifications can be obtained by combining separation and purification process adjustment, different production processes can be selected according to actual requirements of products, and the method has a good industrial application prospect.

This invention belongs to the field of biosynthesis technology and relates to a method for producing D-tagatose under nickel-free conditions and its application. The method includes: mixing tagatose 4-epimerase with a substrate solution, reacting the mixture, and collecting the supernatant by centrifugation to obtain the product. The substrate solution is prepared from D-fructose, glycine, sodium hydroxide, and water. This invention uses tagatose 4-epimerase to catalyze the production of D-tagatose, and the reaction system does not contain nickel ions or other heavy metal ions, thus avoiding the safety hazards caused by nickel residues. This method has a wider range of applications and higher safety.

The invention discloses a method for producing D-tagatose with high efficiency and low cost. According to the invention, a double-enzyme cascade engineering strain B.subtilis WB800N-pHT01-araA-lacZ, which can be used for simultaneously expressing a beta-galactosidase gene lacZ and an L-arabinose isomerase gene araA, is constructed, and the double-enzyme cascade engineering strain B.subtilis WB800N-pHT01-araA-lacZ is constructed; culturing the engineering strain, centrifugally collecting thalli, resuspending the collected thalli by using a substrate solution containing whey powder (lactose), and reacting at constant temperature; and finally, centrifuging the reaction liquid after the reaction is finished, taking supernate, filtering the supernate through a 0.22 m water system small filter, and determining the D-tagatose in the supernate by high performance liquid chromatography, the yield of the D-tagatose being up to 77.5 g / L. The method provided by the invention can realize efficient reutilization of the milk product byproduct whey powder, and has the advantages of simple operation method, mild reaction conditions, high efficiency, low cost and the like.

The present invention relates to a process for preparing tagatose from a biomass or any carbohydrate source derived sugar. The present invention includes methods for producing tagatose using a range of enzymes to convert biomass, such as, but not limited to, starch, maltose, maltodextrin, cellulose, sucrose from juice, and monosaccharides, such as, but not limited to, glucose and / or fructose, etc. The invention also focuses on the use of enzymes alone and / or fused with enzymes involved in successive steps for the economical, efficient conversion of biomass sugars into tagatose.

The invention discloses recombinant escherichia coli for producing D-tagatose by using redox enzyme driven by cofactor regeneration as well as a construction method and application of the recombinant escherichia coli, and belongs to the technical field of biological engineering. The method comprises the following steps: introducing xylose reductase xyrB, glucose dehydrogenase Gox2015, galactitol dehydrogenase RlGDH mutant T193G / G98C and water-producing NADH oxidase SpNox into escherichia coli, so as to construct recombinant escherichia coli; according to the method disclosed by the invention, a way for synthesizing the D-tagatose by regenerating and driving oxidoreductase through cofactors is designed and constructed, and lactose in whey can be completely converted into the D-tagatose and sodium gluconate by combining the way with beta-galactosidase, so that high-valued utilization of a dairy product processing by-product whey is realized.

The invention discloses a D-tagatose-3-epimerase mutant and application thereof, the D-tagatose-3-epimerase mutant has a single-point mutation or a multi-point mutation in the 45th mutation, the 48th mutation, the 50th mutation, the 80th mutation, the 93th mutation, the 98th mutation and the 144th mutation relative to an amino acid sequence SEQ ID NO.1 of a wild type D-tagatose-3-epimerase, and the D-tagatose-3-epimerase mutant has a single-point mutation or a multi-point mutation in the 45th mutation, the 48th mutation, the 50th mutation, the 80th mutation, the 93th mutation, the 98th mutation and the 144th mutation. The invention also provides a corresponding coding gene, a recombinant vector, a genetically engineered bacterium, a biocatalyst and application in preparation of rare sugars. The invention develops the D-tagatose-3-epimerase mutant which has stronger adaptability with glucose isomerase and is more stable in a cascade reaction, is beneficial to improving the efficiency of reaction for preparing rare sugar by using xylose, can simultaneously consider higher substrate concentration and D-xylose conversion rate, and reduces the production cost of the product.

The invention discloses tagatose-containing flavor biscuits with a low glycemic index. The tagatose-containing flavor biscuits are mainly prepared from the following components in parts by weight: 55-70 parts of whole wheat flour, 7-15 parts of wheat bran, 15-30 parts of nutritional sweet substances, 30-50 parts of grease, 5-15 parts of bean flour, 3-7 parts of tartary buckwheat flour, 1-4 parts of resistant dextrin, 0.5-3 parts of milk powder, 0.2-2 parts of natural plant extracts and 0.5-2 parts of additives. Meanwhile, the invention provides a corresponding preparation method. According to the tagatose-containing flavored biscuit with the low glycemic index, sugar alcohol is replaced with tagatose, on one hand, the glycemic index is reduced, on the other hand, the color and flavor of the biscuit are improved, in combination with an enzyme inhibition mechanism of the mulberry leaf extract or the white kidney bean extract, the starch hydrolysis rate can be reduced, and the content of dietary fibers in the biscuit is high; the perfect unification of the function and the taste of the biscuit product is realized.

The invention discloses bread capable of regulating and controlling protein accumulation behaviors through tagatose coupled vital gluten and biologically modified dietary fibers to achieve low GI and a preparation method of the bread, and relates to the technical field of baking. Kneading dough; making dough; performing fermentation; performing baking; the raw materials of the compound functional sugar substitute bread not containing the butter are evenly mixed, water is added, the mixture is kneaded into dough, the dough is whipped, the whipping is divided into high-speed whipping and low-speed whipping, and the tagatose is coupled with the vital gluten and the biologically modified dietary fibers to regulate and control the protein accumulation behavior, so that the low-GI bread is achieved. By replacing 60% or more of cane sugar with tagatose, replacing 15% or more of high-gluten flour with biologically modified dietary fiber and replacing 7% or more of high-gluten flour with vital gluten for bread making, the bread made by the method has high specific volume and good flavor, the use amount of cane sugar in bread making is greatly reduced, and the bread is more suitable for bread making. And the use amount of the high-gluten wheat flour is reduced to a certain extent.

The application discloses a method for producing D-tagatose by a three-enzyme cascade method, and belongs to the field of biotechnology. In the method, fructose is used as a substrate, a reaction system containing metal ions and ATP is used, fructose kinase FRK derived from Clostridium acetobutylicm, D-tagatose 6-phosphate 4-epimerase GatZ derived from Caldilinea aerophila DSM 14535 and D-tagatose-6-phosphate phosphatase MmPase derived from Methanothermobacter marburgensis are used to produce D-tagatose. The yield of D-tagatose is 2.7-9 times of the original yield by optimizing the temperature, the type and the concentration of the metal ions.

The invention discloses a tagatose-4-epimerase and an application of the tagatose-4-epimerase in preparation of D-tagatose. The amino acid sequence of the tagatose-4-epimerase comprises a sequence as shown in SEQ ID NO. 1 to SEQ ID NO. 9. The invention also discloses a preparation method of the tagatose-4-epimerase. The tagatose-4-epimerase disclosed by the invention is used as a catalyst to catalyze D-fructose, and the yield of D-tagatose can reach more than 30%.

The application belongs to the technical field of biotechnology, and particularly relates to a recombinant Escherichia coli and application of the recombinant Escherichia coli in simultaneous production of D-mannose, D-psicose and D-tagatose. Specifically, the application provides a recombinant Escherichia coli, the strain of which simultaneously expresses five key enzymes, can use cheap glucose as a substrate, and can simultaneously synthesize D-mannose, D-psicose and D-tagatose in a single reaction system through a multistage enzyme cascade reaction, so that a one-pot three-sugar production mode is realized. In the technical scheme, PPGK can use polyphosphate to replace ATP to provide a phosphate group, so that the addition of an expensive auxiliary factor is avoided, and the production cost is significantly reduced. Meanwhile, the three products are simultaneously generated in a single system, so that subsequent separation and purification steps are simplified, and the application has a good industrial application prospect.

Disclosed are components and methods for preparing tagatose from galactose via isomerization reactions using engineered components. The engineered components include microbial cells and methods for preparing microbial cells that have been engineered to catalyze isomerization of galactose to tagatose, in which the microbial cells express cytoplasmically an exogenous L-arabinose isomerase enzyme. The disclosed microbial cells may further be modified for use in methods for preparing tagatose from galactose via isomerization reactions where the microbial cells are treated with reagents that permeabilize the cells. The disclosed methods enable isomerization reactions of galactose to tagatose at relatively high rates, high conversions, and elevated temperatures.

This invention discloses a strain for the efficient synthesis of D-tagatose, its preparation method, and its applications. Through strategies such as the discovery of novel galactitol dehydrogenase and promoter engineering, this invention initially increased tagatose yield by 28.48%. Simultaneously, a highly efficient and sensitive tagatose biosensor was developed, which was used as a screening tool for xylose reductase. Ss XR molecularly modified the strain to obtain the F128M-Q219K double mutant, which achieved a tagatose yield of 5.39 g / L in the producing strain. Based on this, amino acid complementation optimization was performed on the high-yielding strain, and the final engineered strain achieved a tagatose yield of 44.61 g / L in a 5 L bioreactor. This study provides a new strategy and core technology support for the efficient biosynthesis of tagatose.

An L-rhamnose isomerase which can be obtained from a microorganism belonging to the genus Erwinia, has a subunit of a molecular mass of about 48 kDa as determined by SDS-PAGE, and has the substrate specificity of (A) and (B) described below. (A) has an isomerase activity which recognizes and reacts with CHO group at C1 and OH group at C2 of an aldose, converts CHO group at C1 into OH group, and converts OH group at C2 into CO group, or recognizes and reacts with OH group at C1 and CO group at C2 of a ketose, converts OH group at C1 into CHO group, and converts CO group at C2 into OH group. (B) has an activity of catalyzing isomerization between L-rhamnose and L-rhamnulose, between L-lyxose and L-xylulose, between L-mannose and L-fructose, between D-ribose and D-ribulose, between L-talose and L-tagatose, and between D-allose and D-psicose.

This application discloses a mouthwash and its preparation method, belonging to the field of mouthwash. The mouthwash includes a composition comprising a main filler and an active substance; the main filler includes tagatose; by mass parts, the main filler is 40-90 parts and the active substance is 0.1-10 parts. In this application, by setting the main filler to 40-90 parts, and by including tagatose, the mouthwash contains a relatively high amount of tagatose, ensuring that the mouthwash is less susceptible to moisture absorption during storage, thereby improving the mouthwash's taste.

The application belongs to the field of biopharmacy and bioconversion, and particularly relates to a tagatose-4-epimerase mutant and application thereof in preparation of D-tagatose. The tagatose-4-epimerase mutant is obtained by single mutation or combined mutation of amino acid residues at specific positions of the amino acid sequence shown in SEQ ID NO. 1. Compared with wild-type tagatose-4-epimerase, the mutant has improved catalytic activity in the reaction of preparing D-tagatose. The tagatose-4-epimerase mutant has the advantages of mild reaction condition, green environmental protection, single product, simple separation and purification, and greatly reduced production cost.

The application discloses a recombinant domain fusion enzyme and application thereof in preparation of D-allulose, wherein the recombinant domain fusion enzyme is formed by splicing and recombining a 5' domain and a partial 3' domain of D-tagatose 3-epimerase and an active center domain of xylose isomerase. The application uses the domain fusion enzyme of the 5' domain and the partial 3' domain of D-tagatose 3-epimerase and the active center domain of xylose isomerase as a biological catalyst, and the yield of D-allulose generated by catalyzing isomerization of 260 g / L glucose is 35.9%. The method disclosed by the application is rapid and efficient, reaction conditions are simple, substrate conversion rate is high, and byproducts are few, so that the pressure of separation and purification is reduced, and the method is suitable for large-scale industrial production.

The application discloses an engineered bacillus subtilis strain for producing tagatose, a construction method and application thereof, and belongs to the technical field of bioengineering. The engineered strain takes bacillus subtilis as a host, co-expresses L-arabinose isomerase from Erysipelothrix larvae and beta-galactosidase from escherichia coli, and constructs the bacillus subtilis for co-expressing double enzymes through ribosome binding sites or promoters in series. The double-enzyme bacillus subtilis whole cell catalyzes lactose to produce D-tagatose, and the yield and conversion efficiency of D-tagatose are significantly improved after optimization of the enzymatic reaction. The application adopts single-strain double-enzyme co-expression and one-step whole-cell catalysis, uses low-cost lactose as a substrate, and has the advantages of mild reaction, less by-product, simplified process, no endotoxin safety hazard, and the like. The application solves the problems of low conversion rate, high substrate cost and complicated strain compounding in the prior art, and is suitable for industrialized production of food-grade D-tagatose.

The application discloses a tagatose 4-epimerase mutant with improved catalytic efficiency and application thereof. Thermoproteales archaeon The tagatose 4-epimerase mutant is obtained by replacing the serine at the 46th position with alanine in the amino acid sequence of tagatose 4-epimerase from The tagatose 4-epimerase mutant has significantly improved catalytic activity compared with the wild type, and the catalytic efficiency and yield of the mutant in a whole cell system are improved, which indicates that the recombinant mutant bacteria have good industrial application potential.

The invention discloses preparation and application of a phosphoric-acid-dependence-free tagatose-diphosphate aldolase mutant, and belongs to the field of gene engineering and enzyme engineering. The tagatose-diphosphate aldolase KoT4E gene derived from Ko is expressed in E. coli BL21 (DE3), the tagatose-diphosphate aldolase is applied to a reaction system with d-fructose as a substrate, enzyme reaction is carried out under the conditions that the pH value is 8.5 and the temperature is 70 DEG C, and the yield of the d-fructose after reaction is carried out for 12 hours reaches 140.5 g / L. The recombinant strain is subjected to high-density fermentation, a crude enzyme liquid obtained after cell wall breaking of thallus cells is added into a 1.5 L large reaction system, the yield of d-tagatose can reach 126.75 g / L after the reaction is conducted for 12 h, and industrial production of d-tagatose can be achieved.

This invention provides a compound composition for regulating glucose and lipid metabolism in diabetes and its application, belonging to the fields of medicine, food, and health products. The composition comprises an enzymatically hydrolyzed extract of Polygonatum sibiricum, a compound extract of traditional Chinese medicine including Astragalus membranaceus, ginseng, mulberry leaf, cinnamon, white kidney bean, and bitter melon, probiotics including Lactobacillus rhamnosus and Bifidobacterium bifidum B11, hydrolyzed collagen peptides, and tagatose, scientifically formulated according to the principles of traditional Chinese medicine. This composition can comprehensively regulate the multidimensional pathological characteristics of diabetes, such as glucose and lipid metabolism disorders, chronic inflammation, and weight loss, exerting a synergistic effect. Its hypoglycemic, lipid-regulating, anti-inflammatory, and weight-recovery-promoting effects are significantly better than the sum of the individual effects of each component. It can also significantly improve serum free fatty acid, fasting insulin, and inflammatory factor levels, providing a new approach for developing safe and effective adjunctive treatment products for diabetes.