9 results about "Allose" patented technology

The invention discloses a synthesis method of helicid, and relates to the technical field of compound synthesis, glucose is taken as an initial raw material, allose is obtained through a series of reactions, pentaacetyl allose is prepared from allose through acetylation reaction, tetraacetyl alloside is prepared through selective deacetylation reaction, substitution reaction and nucleophilic substitution reaction, and the helicid is synthesized through a one-step method. And finally, carrying out a deacetylation reaction on the tetraacetyl alloside to prepare helicid. Helicid has the effects of calming, sleeping, easing pain and resisting inflammation, and can be applied to preparation of medicaments with corresponding effects. The preparation method of the helicid provided by the invention is simple to operate, can be used for large-scale industrial production, and overcomes the defect of insufficient yield of naturally extracted helicid.

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 invention discloses a preparation method of an L-rhamnose isomerase mutant and a preparation method of D-allose, and belongs to the technical field of genetic engineering. The amino acid sequence of the L-rhamnose isomerase mutant is as shown in SEQ ID NO. 3. According to the L-rhamnose isomerase mutant disclosed by the invention, the 268th amino acid of the amino acid sequence of the wild type L-rhamnose isomerase is mutated from S to T, and the enzyme activity of the obtained L-rhamnose isomerase mutant is remarkably improved, so that the catalytic efficiency is improved when the D-allose is prepared by catalyzing the reaction of D-psicose, and the yield of the D-allose is further improved.

Treatment with epimerase in vitro forms D-psicose from D-fructose dissolved in aqueous solution, and then D-psicose is converted into the oxidized cofactor NAD(P). + A method for preparing an aqueous solution containing allose by reducing allitol to allitol in vitro with NAD(P)H-dependent oxidoreductase, which is accompanied by the formation of a compound, and then enzymatically oxidizing allitol to allose. (Figure 1)

The invention relates to the technical field of biology, in particular to a preparation and purification process of a DPEase mutant. According to the present invention, I46E / K86I / K86V / H102P / Y111A / N176P / C213N / M249P / Y285E modification is performed on the D-psicose 3-epimerase DPEase derived from Rumiclostridium cellulolyticum, such that the expression quantity and the enzyme activity of the enzyme in Escherichia coli are improved, and the industrial fermentation process and the industrial protein purification process of the enzyme are optimized, such that the D-psicose 3-epimerase prepared by using the process can be easily produced under the conditions of short time and lowest cost so as to significantly improve the yield and the yield of the enzyme; the conversion rate is the same as or even higher than that in the prior art, and the systematic optimization strategy enables the production efficiency to be higher and is more suitable for large-scale industrial production.

This disclosure relates to microorganisms that can be used for the biosynthesis of D-allose. Methods for producing the disclosed microorganisms and for producing D-allose are also provided.

This invention discloses an L-rhamnose isomerase mutant and a method for preparing D-allose, belonging to the field of genetic engineering technology. The amino acid sequence of the L-rhamnose isomerase mutant is shown in SEQ ID NO.3. This invention significantly increases the enzyme activity of the L-rhamnose isomerase mutant by mutating amino acid position 268 of the wild-type L-rhamnose isomerase sequence from S to T, thereby improving the catalytic efficiency in the preparation of D-allose from D-allulose and ultimately increasing the yield of D-allose.

A process for producing an aqueous solution containing allose by forming D-psicose in vitro from D-fructose, which is dissolved in an aqueous solution, by treating the dissolved D-fructose with an epimerase, whereupon the D-psicose is reduced in vitro to allitol by treating the D-psicose with an NAD(P)H-dependent oxidoreductase, resulting in the formation of oxidized cofactor NAD(P)+, and then the allitol is enzymatically oxidized to obtain allose.

The invention discloses L-rhamnose isomerase with a long half-life period and application of the L-rhamnose isomerase in preparation of D-allose, and belongs to the technical field of gene engineering. The amino acid sequence of the L-rhamnose isomerase is as shown in any one of the following: (1) an amino acid sequence as shown in SEQ ID NO.4; (2) an amino acid sequence as shown in SEQ ID NO.6; and (3) an amino acid sequence as shown in SEQ ID NO.8. According to the L-rhamnose isomerase mutant, the wild L-rhamnose isomerase is mutated, and the obtained three L-rhamnose isomerase mutants are higher in enzyme activity and longer in half-life period, so that when the L-rhamnose isomerase mutants are applied to catalyzing D-psicose reaction to prepare D-allose, the yield of the D-allose is effectively increased.