66451-58-9

Basic information

• Product Name: 4-nitrophenyl α-maltotrioside
• Synonyms: 4-nitrophenyl α-maltotrioside
• CAS NO: 66451-58-9
• Molecular Weight: 625.538
• Mol File: 66451-58-9.mol

Chemical Properties

• CAS DataBase Reference: 4-nitrophenyl α-maltotrioside(CAS DataBase Reference)
• NIST Chemistry Reference: 4-nitrophenyl α-maltotrioside(66451-58-9)
• EPA Substance Registry System: 4-nitrophenyl α-maltotrioside(66451-58-9)

Safety Data

• Hazardous Substances Data: 66451-58-9(Hazardous Substances Data)

Upstream product

• 7585-39-9 β‐cyclodextrin 
• 3767-28-0 4-nitrophenyl-α-D-glucopyranoside 
• 118291-90-0 2-chloro-4-nitrophenol-α-D-maltotrioside 
• 66068-38-0 p‐nitrophenyl‐α‐D-maltopentoglycoside 
• 133978-86-6 C₆₀H₉₂N₄O₄₀S 
• 66068-37-9 4-nitrophenyl α-maltotetraoside 
• 74173-30-1 C₄₂H₆₅NO₃₃ 

Downstream Products

• 100-02-7 4-nitro-phenol 
• 6401-81-6 maltotriose 

Relevant articles and documents

Acceptor-induced modification of regioselectivity in CGTase-catalyzed glycosylations of p-nitrophenyl-glucopyranosides

Cyclodextrin glycosyltransferases (CGTase) are reported to selectively catalyze α(1→4)-glycosyl transfer reactions besides showing low hydrolytic activity. Here, the effect of the anomeric configuration of the glycosyl acceptor on the regioselectivity of

Study of the action of human salivary alpha-amylase on 2-chloro-4-nitrophenyl α-maltotrioside in the presence of potassium thiocyanate

The degradation mechanism of a synthetic substrate, 2-chloro-4-nitrophenyl α-maltotrioside (CNP-G3), by human salivary alpha-amylase (HSA) was investigated by kinetic and product analyses. It was observed that the enzyme attacked the various CNP-maltooligosaccharides (CNP-G3, to CNP-G6) releasing free CNP. Addition of 500 mM potassium thiocyanate (KSCN) was also found to greatly increase the rates of CNP-release. It was the fastest with CNP-G3, and, in the presence of KSCN, was almost comparable to that of degradation of maltopentaose (G5). On the other hand, addition of KSCN decreased the rate of cleavage between glucan-glucan bonds in maltopentaose. Product analysis showed that KSCN addition altered the cleavage distribution which occurred 100% at the bond between CNP and G3, and that product distribution of free CNP was largely dependent on substrate concentration. Formation of CNP-G6, a larger product than the original substrate CNP-G3, was found to be present in the digest at high concentrations of substrate and in the presence of KSCN. Based on these results, a degradation pathway for CNP-G3 involving transglycosylation besides direct hydrolysis is proposed. The increase of the CNP-release by the addition of KSCN would result from a corresponding increase in the interaction between the CNP moiety and the corresponding subsite near the catalytic site, as well as the enhancement of the catalytic efficiency.

The action of germinated barley alpha-amylases on linear maltodextrins

The actions of barley alpha-amylase isozymes 1 and 2 (EC 3.2.1.1) on malto-oligosaccharides and their p-nitrophenyl glycosides were similar, but not identical.For each isozyme, transglycosylation occurred with small substrates that were hydrolysed with difficulty, whereas the rates of hydrolysis increased with increase in the size of the substrate for both the malto-oligosaccharides and the p-nitrophenyl glycosides.A p-nitrophenyl group was found to mimic a glucose residue to a large extent.The differences in action of the isozymes are believed to be caused by differences at more than one subsite of the active site.Alysine-arginine substitution is postulated to account for some of the observed variations.

A Novel Approach to the Determination of Trace α-Amylase by Photographic Assay. The Synthesis and Enzymatic Characterization of an Oligosaccharide Derivative as a Substrate for α-Amylase from Porcine Pancreas

In line with a new concept for the photographic assay on the basis of chemical amplification by the catalytic Ag* nuclei, an α-amylase substrate containing a new sensitive labeling component and a bioaffinity group was designed and synthesized.The analysis of enzymatic degradation proved that the substrate can release efficiently the labeling component without loss of photographic activity.

Synthesis of p-nitrophenyl 6(5)-O-benzyl-alpha-maltopentaoside, a substrate for alpha amylases.

p-Nitrophenyl alpha-maltopentaoside, having a benzyl group on O-6 of the terminal (nonreducing) D-glucosyl group was prepared by use of a reductive ring-opening reaction. Highly regioselective reduction of p-nitrophenyl O-(2,3-di-O-benzoyl-4,6-O-benzylidene-alpha-D-glucopyranosyl)-(1----4)- tris[O-(2,3,6-tri-O-benzoyl-alpha-D-glucopyranosyl)-(1----4)]-2,3,6-tri- O- benzoyl-alpha-D-glucopyranoside by dimethylamine-borane and p-toluenesulfonic acid, followed by debenzoylation, gave p-nitrophenyl O-(6-O-benzyl-alpha-D-glucopyranosyl)-(1----4)-tris[O-alpha-D-glucopyran osyl- (1----4)]-alpha-D-glucopyranoside. An experiment was done on the mode of action of human pancreatic and salivary alpha amylases on this derivative. The compound is suitable as a substrate for the assay of alpha amylase when used with glucoamylase and alpha-D-glucosidase as coupling enzymes.