The disclosure discloses a method for producing maltodextrin with a single polymerization degree by multienzyme coupling, and belongs to the technical field of biology. The disclosure provides a method for producing non-reducing maltodextrin with a uniform and low polymerization degree. After a reaction is preformed for 2-6 hours by using the method of the disclosure, the content of 4-O-α-maltohexaosyl α-D-glucoside in a reaction solution can be as high as 57.2% to 77.3%, accounting for 50% to 90% of the total amount of maltodextrin in the reaction solution. In maltodextrin prepared by using the method of the disclosure, non-reducing maltodextrin with low polymerization degree only includes 4-O-α-maltohexaosyl α-D-glucoside, and the content of non-reducing maltodextrin with low polymerization degree can be 50% to 90% of the total amount of maltodextrin. Therefore, only filtration is needed in preparation of non-reducing maltodextrin with low polymerization degree by using the method of the disclosure; additional separation and purification steps are not needed; high-purity non-reducing maltodextrin with low polymerization degree can be obtained; and the production cost is low.

The present invention relates to high intensity sweetener glycosides which have been modified using a glycosyltransferase so as to reduce off-flavours. The invention also relates to uses of the modified high intensity sweetener glycosides and methods of production thereof.

Lipase enzymes and methods of using the lipases in a baking for improving the volume, stability, tolerance of a baked product and/or reducing and reducing or eliminating the use of DATEM.

The disclosure discloses a method for producing long-chain glycosylated genistein and belongs to the technical fields of enzyme engineering and fermentation engineering. The disclosure provides a method for producing long-chain glycosylated genistein. By using this method to produce long-chain glycosylated genistein, the content of long-chain glycosylated genistein in a reaction solution and the ratio of the content of long-chain glycosylated genistein in the reaction solution to the content of total glycosylated genistein in the reaction solution can be increased. The content of long-chain glycosylated genistein in the reaction solution can be increased to 10.3 g/L, and the ratio of the content of long-chain glycosylated genistein in the reaction solution to the content of total glycosylated genistein in the reaction solution can be increased to 70%.

The invention provides cyclodextrin inclusion complex delivery vehicles, in which the cyclodextrin inclusion complex is provided together with enzyme having a cyclodextrin-degrading activity capable of digesting the cyclodextrin, so that upon delivery of the vehicle to a target the enzyme is activated and releases the guest molecule from the cyclodextrin cavity. In alternative aspects, these cyclodextrin inclusion complex delivery vehicles are for example provided in the form of medicaments, food ingredients, medical food ingredients, nutritional supplement ingredients, dietary supplement ingredients, herbicides, insecticides, fungicides, animal repellents, pheromones, plant growth regulators, fragrances, fabrics or packaging materials.

The present invention relates to preparation and application of a cyclodextrin glucosyltransferase mutant, belonging to the fields of gene engineering and enzyme engineering. By mutating amino acids of cyclodextrin glucosyltransferase, the enzyme activity of the obtained mutant can reach 2.5 times that of wild enzyme. In addition, the cyclodextrin glucosyltransferase mutant obtained in the present invention is simple in purification and suitable for industrial production.

The present invention provides enzymes that have been optimized by implementation of Protein Repair One Stop Shop (PROSS), an algorithm that generates protein design(s) for enhanced stability without changing either enzymatic properties or enzyme active site conformation of the respective enzyme. The protein design(s) generated by PROSS introduce mutations to the amino acid sequence of a wild-type protein, resulting in a mutated amino acid sequence that encodes a variant of the wild-type enzyme, i.e., an enzyme variant, which has an enhanced stability, core packing, surface polarity and backbone rigidity, a higher functional expression, and/or a combination thereof, compared to the stability core packing, surface polarity and backbone rigidity, functional expression and/or a combination thereof, of the wild-type enzyme.

A method for producing an inositol derivative includes a step of reacting inositol and dextrin in the presence of cyclodextrin glucanotransferase to generate an inositol derivative in which a sugar is bonded to the inositol, and to obtain a solution containing the inositol derivative and the cyclodextrin glucanotransferase; and a step of removing the cyclodextrin glucanotransferase in the solution using an ultrafiltration membrane, in which a deactivation treatment of the cyclodextrin glucanotransferase in the solution is not performed.

A method of preparing a glucosylated steviol glycoside composition involving by treating stevia materials with cyclodextrin glycosyltransferase.

An isolated and/or purified -glucanotransferase from Exiguobacterium acetylicum, recombinantly engineered variants thereof, active fragments thereof, synthetic nucleic acids encoding the -glucanotransferase and variants thereof, host cells comprising the synthetic nucleic acids, and compositions comprising the -glucanotransferase are provided. Methods of using the compositions include the manufacture of oligosaccharides.