1980-14-9

Basic information

• Product Name: maltoheptaose
• CAS NO: 1980-14-9
• Molecular Formula: C₄₂H₇₂O₃₆
• Molecular Weight: 1152.99948
• Mol File: 1980-14-9.mol
• Article Data: 4

Chemical Properties

• Appearance: /
• CAS DataBase Reference: maltoheptaose(CAS DataBase Reference)
• NIST Chemistry Reference: maltoheptaose(1980-14-9)
• EPA Substance Registry System: maltoheptaose(1980-14-9)

Safety Data

• Hazardous Substances Data: 1980-14-9(Hazardous Substances Data)

Upstream product

• 59-56-3 α-D-glucopyranosyl-1-phosphate 
• 528-50-7 cellobiose 
• 2106-10-7 1-deoxy-1-fluoro-α-D-glucose 
• 1263-76-9 Maltotetraose 

Downstream Products

• 345319-76-8 5-O-α-D-glucopyranosyl-(+)-catechin 
• 345319-75-7 (+)-catechin 7-α-O-glucoside 
• 67-47-0 5-hydroxymethyl-2-furfuraldehyde 
• 50-99-7 D-glucose 
• 99-20-7 TREHALOSE 
• 1668-09-3 maltopentaose 
• 172957-44-7 maltopentaosyltrehalose 
• 71314-43-7 2,3,4,6-tetra-O-acetyl-α-D-glucopyranosyl-[(1→4)-2,3,6-tri-O-acetyl-α-D-glucopyranosyl]₅-(1→4)-1,2,3,6-tetra-O-acetyl-α,β-D-glucopyranose 
• 1263-76-9 maltotetraose 
• 5090-06-2 malto-nonaose 
• 1668-09-3 maltopentaose 

Relevant articles and documents

Characterization and mechanism of action of Microbacterium imperiale glucan 1,4-α-maltotriohydrolase

In this study, glucan 1,4-α-maltotriohydrolase (AMTS) from Microbacterium imperiale was purified and characterized. Hydrolysis by AMTS was affected by starch structure (e.g., amylose versus amylopectin) and hydrolysis time. During the initial phase of hydrolysis of maltooligosaccharides (G4-G7), AMTS displayed a unique transfer specificity to the transfer of maltotriosyl units. After extensive hydrolysis, maltotriose became the major end product, followed by glucose and maltose. Maltotetraose (G4) was the smallest donor in transglycosylation reactions by AMTS. This is the first study that reports transglycosylation activity of AMTS on maltooligosaccharides. The results of this study suggest that high purity maltotriose can be produced by the hydrolytic action of AMTS on starch.

Subsite Structure of Chalara paradoxa Glucoamylase and Interaction of the Glucoamylase with Cyclodextrins

The action of Chalara paradoxa glucoamylase (raw-starch-digesting enzyme) was studied with linear and cyclic maltodextrins.Subsite affinities (Ai) of the amylase were evaluated by the subsite theory.The active site was considered to be made up of seven subsites: A1 = 0.05 kcal/mol, A2 = 4.99 kcal/mol, A3 = 1.30 kcal/mol, A4 = 0.77 kcal/mol, A5 = 0.33 kcal/mol, A6 = 0.21 kcal/mol and A7 = 0.21 kcal/mol.Inhibitions by alpha-, beta-, and gamma-cyclodextrins were competitive for starch digestion by C. paradoxa glucoamylase.The inhibitor constants (Ki) of α-, β-, and γ-cyclodextrin for the amylase were 8.9, 1.4, and 3.9 mM, respectively.The Michaelis constant (Km) of 6-O-α-maltosyl-α-cyclodextrin digestion was 0.79 mM for the amylase.