497-84-7

Basic information

• Product Name: Isomaltulose
• CAS NO: 497-84-7
• Molecular Weight: 342.3
• Mol File: 497-84-7.mol
• Article Data: 6

Chemical Properties

• CAS DataBase Reference: Isomaltulose(CAS DataBase Reference)
• NIST Chemistry Reference: Isomaltulose(497-84-7)
• EPA Substance Registry System: Isomaltulose(497-84-7)

Safety Data

• Hazardous Substances Data: 497-84-7(Hazardous Substances Data)

Upstream product

• 57-50-1 Sucrose 
• 59-92-7 levodopa 
• 24822-33-1 D-isomaltose 

Downstream Products

• 57-48-7 D-Fructose 
• 24822-33-1 D-isomaltose 
• 3458-28-4 D-Mannose 
• 50-99-7 D-glucose 
• 1462942-81-9 4-[(1'R,2'S,3'R)-4′-(α-D-glucopyranosyloxy)-1',2',3'-trihydroxybutyl]-2-phenylimidazole 
• 55-21-0 benzamide 
• 209977-51-5 N-acetyl-6-O-(α-D-glucopyranosyl)-D-glucosamine 
• 67-47-0 5-hydroxymethyl-2-furfuraldehyde 
• 4746-18-3 isomaltulose phenylosazone 
• 20942-96-5 α-D-glucopyranosyl-(1->6)-D-gulitol 
• 20942-99-8 1-O-α-D-glucopyranosyl-D-mannitol 

Relevant articles and documents

Hydrolysis of low-molecular-weight oligosaccharides and oligosaccharide alditols by pig intestinal sucrase/isomaltase and glucosidase/maltase

The ability of purified pig intestinal sucrase/isomaltase (SI; EC 3.2.1.10/48) and glucosidase/maltase (GM; EC 3.2.1.20) to hydrolyze di- and oligosaccharides consisting of D-glucose and D-fructose residues and the corresponding alditols was studied. The products, after incubation, reflect different binding patterns at both catalytic sites of SI. The active site of the sucrase subunit cleaves α,β-(1→2) glycosidic bonds, and only two monomer units of the substrates bind with favorable affinity. Oligosaccharides and reduced oligosaccharides containing α-(1→6) and α-(1→1) glycosidic bonds are hydrolyzed by isomaltase, and for the active site of this subunit more than two subsites were postulated. Moreover, different binding sites for various aglycons seem to exist for isomaltase. Oligosaccharide alcohols are cleaved at lower rates if the reduced sugar residue occupies the aglycon binding site. GM also hydrolyzes α-(1→1) linkages, but at a lower rate. The enzyme has the ability to bind compounds containing residues other than D-glucose. There are indications for similarities between GM and the isomaltase subunit of SI in the binding mode of oligosaccharides. Copyright (C) 2000 Elsevier Science Ltd.

Mechanism-Oriented Redesign of an Isomaltulose Synthase to an Isomelezitose Synthase by Site-Directed Mutagenesis

An isomelezitose synthase was redesigned out of the sucrose isomerase from Protaminobacter rubrum for the synthesis of isomelezitose (6-OF-glucosylsucrose), a potential nutraceutical. The variants F297A, F297P, R333K, F321A-F319A and E428D catalyze the formation of isomelezitose in up to 70% yield.

Method for preparing crystalline isomaltulose and hydrogenated isomaltulose

Provided is a method for manufacturing crystalline isomaltulose from sucrose, comprising the steps of: 1) contacting an α-glucosyltransferase enzyme to aqueous sucrose solution or slurry under the condition wherein the α-glucosyltransferase enzyme is active; in which said condition is maintained after the concentration of isomaltulose in the reaction mixture reaches the point at which crystals are formed, and 2) separating the reaction mixture into crystalline isomaltulose and remaining syrup. According to the present invention, enzymatic conversion of sucrose and crystallization of isomaltulose are carried out simultaneously in a same reaction vessel. In addition, the enzyme can be used repeatedly.