cas 66068-37-9, 4-Nitrophenyla-D-maltotetraoside

Articles about 66068-37-9Total 4 be found

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
Strompen, Simon,Miranda-Molina, Alfonso,López-Munguía, Agustín,Castillo, Edmundo,Saab-Rincón, Gloria
p. 46 - 54
(2015/03/05)

Transglycosylation reaction of maltotriose-forming amylase from Streptomyces griseus
A maltotriose-forming amylase from Streptomyces griseus produced predominantly p-nitrophenyl α-maltotetraoside through a transglycosylation reaction from maltotetraose as a donor and p-nitrophenyl α-D-glucopyranoside as an acceptor in an organic co-solven
Usui, Taichi,Murata, Takeomi,Yabuuchi, Yoshihiko,Ogawa, Koichi
p. 57 - 66
(2007/10/02)

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.
MacGregor, Alex. W.,Morgan, Joan E.,MacGregor, E. Ann
p. 301 - 314
(2007/10/02)

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.
Ono, Mitsunori,Suzuki, Nobuo,Hirano, Shigeo,Itoh, Isamu,Masuta, Nobuhito
p. 395 - 398
(2007/10/02)