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2-O-(α-D-Galactopyranosyl)-D-glucopyranose, also known as lactose, is a disaccharide sugar composed of two monosaccharide units: D-glucose and D-galactose. In 2-O-(a-D-Galactopyranosyl)-D-glucopyranose, the galactose unit is linked to the second carbon of the glucose unit through an α-1,2 glycosidic bond. Lactose is commonly found in milk and dairy products, and it is a significant source of energy for infants. It is also used in the food industry as a sweetener and as a component in various products such as baked goods, confectionery, and ice cream. Lactose is not easily digestible for some individuals, particularly those with lactose intolerance, due to the absence of the enzyme lactase, which is required to break down the glycosidic bond and release the individual monosaccharides.

7286-57-9

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7286-57-9 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 7286-57-9 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 7,2,8 and 6 respectively; the second part has 2 digits, 5 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 7286-57:
(6*7)+(5*2)+(4*8)+(3*6)+(2*5)+(1*7)=119
119 % 10 = 9
So 7286-57-9 is a valid CAS Registry Number.

7286-57-9Relevant academic research and scientific papers

A SUCROSE PHOSPHORYLASE FOR THE PRODUCTION OF KOJIBIOSE

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Page/Page column 11, (2016/06/13)

The present invention relates to the production of the disaccharide kojibiose which is known to be a powerful prebiotic. The invention indeed discloses the generation of genetically modified sucrose phosphorylases which convert -via a transglycosylation reaction- sucrose into kojibiose in a very efficient manner. Hence, the present invention relates to a cost-effective production method of kojibiose which is useful within industry.

Redesign of the Active Site of Sucrose Phosphorylase through a Clash-Induced Cascade of Loop Shifts

Kraus, Michael,Grimm, Clemens,Seibel, Jürgen

, p. 33 - 36 (2016/01/15)

Sucrose phosphorylases have been applied in the enzymatic production of glycosylated compounds for decades. However, several desirable acceptors, such as flavonoids or stilbenoids, that exhibit diverse antimicrobial, anticarcinogenic or antioxidant properties, remain poor substrates. The Q345F exchange in sucrose phosphorylase from Bifidobacterium adolescentis allows efficient glucosylation of resveratrol, (+)-catechin and (-)-epicatechin in yields of up to 97 % whereas the wild-type enzyme favours sucrose hydrolysis. Three previously undescribed products are made available. The crystal structure of the variant reveals a widened access channel with a hydrophobic aromatic surface that is likely to contribute to the improved activity towards aromatic acceptors. The generation of this channel can be explained in terms of a cascade of structural changes arising from the Q345F exchange. The observed mechanisms are likely to be relevant for the design of other tailor-made enzymes.

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