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56808-39-0

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56808-39-0 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 56808-39-0 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 5,6,8,0 and 8 respectively; the second part has 2 digits, 3 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 56808-39:
(7*5)+(6*6)+(5*8)+(4*0)+(3*8)+(2*3)+(1*9)=150
150 % 10 = 0
So 56808-39-0 is a valid CAS Registry Number.

56808-39-0Downstream Products

56808-39-0Relevant articles and documents

SYNTHETIC CATALYSTS FOR CARBOHYDRATE PROCESSING

-

, (2022/01/24)

The disclosure relates to molecularly-imprinted cross-linked micelles that can selectively hydrolyze carbohydrates.

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

Strompen, Simon,Miranda-Molina, Alfonso,López-Munguía, Agustín,Castillo, Edmundo,Saab-Rincón, Gloria

, p. 46 - 54 (2015/03/05)

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

Synthesis of chromogenic substrates of α-amylases on a cyclodextrin basis

Farkas, Erzsebet,Janossy, Lorant,Harangi, Janos,Kandra, Lili,Liptak, Andras

, p. 407 - 415 (2007/10/03)

One-pot acetylation and subsequent partial acetolysis of α-, β-and γ- cyclodextrins resulted in crystalline peracetylated malto-hexaose, -heptaose, and -octaose, respectively. Prolonged acetolysis of β-cyclodextrin gave a mixture of acetylated maltooligosaccharides, from which peracetylated malto- triose, -tetraose, and -pentaose were isolated. The acetylated oligosaccharides were converted into α-acetobromo derivatives, and then transformed into 4-nitrophenyl and 2-chloro-4-nitrophenyl β-glycosides. From the 4-nitrophenyl glycosides 4,6-O-benzylidene derivatives were prepared, which were used together with the free glycosides as substrates of porcine pancreatic α-amylase.

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