4419-94-7

Usage

Uses

Used in Biochemical Research:
P-NITROPHENYL BETA-D-LACTOPYRANOSIDE is used as a substrate for determining β-lactosidase activity. P-NITROPHENYL BETA-D-LACTOPYRANOSIDE serves as an indicator of enzymatic activity, as the release of the 4-nitrophenyl group upon cleavage results in a color change that can be measured spectrophotometrically. This property makes it a valuable tool for studying enzyme kinetics, inhibitor screening, and enzyme characterization.
Used in Enzyme Assays:
P-NITROPHENYL BETA-D-LACTOPYRANOSIDE is used as a substrate for cellobiohydrolase, an enzyme involved in the breakdown of cellulose. The color change upon enzymatic cleavage allows researchers to monitor the progress of the enzymatic reaction and assess the efficiency of the enzyme in breaking down cellulose.
Used in Determining Substrate Specificity:
P-NITROPHENYL BETA-D-LACTOPYRANOSIDE is used to determine the substrate specificity for β-glucosidase from the yeast Debaryomyces hansenii. By using P-NITROPHENYL BETA-D-LACTOPYRANOSIDE as a substrate, researchers can gain insights into the enzyme's preferences for specific substrates and its potential applications in various industrial processes, such as biofuel production or the synthesis of specific glycosides.

InChI:InChI=1/C18H25NO13/c20-5-9-11(22)12(23)14(25)18(30-9)32-16-10(6-21)31-17(15(26)13(16)24)29-8-3-1-7(2-4-8)19(27)28/h1-4,9-18,20-26H,5-6H2/t9?,10?,11-,12-,13+,14-,15-,16+,17+,18-/m0/s1

Upstream product

• 84034-75-3 4-nitrophenyl-2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl-(1→4)-2,3,6-tetra-O-acetyl-β-D-glucopyranoside 
• 2492-87-7 4-nitrophenyl-β-D-glucoside 
• 2021-84-3 α-galactosyl fluoride 
• 133-89-1 uridine-5'-diphosphogalactose 
• 439-03-2 2,3,4,6-tetra-O-acetyl-α-D-galactopyranosyl fluoride 
• 25878-60-8 D-galactose pentaacetate 
• 5987-78-0 p-nitrophenyl 2,3,4,6-tetra-O-acetyl-β-D-glucopyranosyde 
• 100-02-7 4-nitro-phenol 
• 604-69-3 β-D-glucose pentaacetate 
• 198561-70-5 C₃₇H₄₉NO₂₃ 
• 69-79-4 D-maltose 
• 3616-19-1 1,2,3,6,2',3',4',6'-octa-O-acetylmaltose 
• 133978-86-6 C₆₀H₉₂N₄O₄₀S 
• 109055-07-4 blocked p-nitrophenyl maltoheptaoside 

Downstream Products

• 148705-00-4 p-nitrophenyl 3',4'-O-isopropylidene-β-lactoside 
• 17691-02-0 p-Aminophenyl 4-O-(β-D-galactopyranosyl)-β-D-glucopyranoside 
• 2149582-14-7 α-D-Neu5Ac-(2->3)-β-D-Gal-(1->4)-β-D-Glc-OC6H4NO2-p 
• 2149582-14-7 4-nitrophenyl O-(5-acetamido-3,5-dideoxy-D-glycero-α-D-galacto-2-nonulopyranosylonicacid)-(2→3)-O-β-D-galactopyranosyl-(1→4)-β-D-glucopyranoside 
• 100-02-7 4-nitro-phenol 
• 3767-28-0 4-nitrophenyl-α-D-glucopyranoside 
• 492-62-6 alpha-D-glucopyranose 
• 1402245-83-3 C₂₄H₃₅NO₁₈ 
• 1402245-94-6 C₄₄H₅₅NO₂₈ 
• 42935-29-5 (4-amino-phenyl)-(O⁴-α-D-glucopyranosyl-β-D-glucopyranoside) 
• 135253-89-3 N-{4-[(2S,3R,4R,5S,6R)-3,4-Dihydroxy-6-hydroxymethyl-5-((2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yloxy)-tetrahydro-pyran-2-yloxy]-phenyl}-acrylamide 
• 94367-66-5 p-succinylamidophenyl β-lactoside 

Relevant academic research and scientific papers

SYNTHETIC CATALYSTS FOR CARBOHYDRATE PROCESSING

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

PHENOL GLYCOSIDES AND THEIR USE IN THE TREATMENT OF UROLITHIASIS

The present invention relates to novel derivatives of polyphenol glycoside or polyalcohols of formula (1), wherein R1, R2, R3 is selected from the group consisting of H, OH, C(O)R4, C(0) OR4, 0 (Gly H3)n, wherein n = 0 1, 2, 3, and R4 is selected from the group consisting of H, alkyl, and Gly is a mono- or disaccharide residue. The present invention also relates to novel derivatives of glycoside polyphenols or polyalcohols, as pharmaceutical composition comprising a novel polyphenol glycoside or polyalcohols and the use of novel polyphenol glycoside or polyalcohols for the treatment of urolithiasis.

BEVERAGE DISPENSING EQUIPMENT

Apparatus and methods for reducing biofouling in drink such as beer dispensing equipment are described.

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

Environmentally benign glycosylation of aryl pyranosides and aryl/alkyl furanosides demonstrating the versatility of thermostable CGTase from Thermoanaerobacterium sp.

An extensive study on the specificity of transglycosylation and disproportionation of Thermoanaerobacterium sp. cyclodextrin glucosyltransferases against aryl glucopyranosides or furanosides is reported. While a mixture of maltoside and isomaltoside was obtained respectively using p-nitrophenyl glucopyranoside as an acceptor, only one regioisomer, namely p-nitrophenyl α-d-Glcp-(1,3)-α-l-Araf, was isolated using p-nitrophenyl arabinofuranoside as an acceptor. Interestingly, similar outcomes were found when using p-nitrophenyl galactofuranoside. Furthermore, activation by microwave irradiation resulted in faster reaction times and higher yields and led to glucosidic oligosaccharides with up to 70% conversion. The influence of the anomeric and C-4 configurations of the glycosidic acceptors on the transglycosylation, previously stated for the CGTase family, was not observed and unconventional substrate specificity towards alkyl furanosides was highlighted. This journal is the Partner Organisations 2014.

Glycosynthase with broad substrate specificity-an efficient biocatalyst for the construction of oligosaccharide library

A versatile glycosynthase (TnG-E338A) with strikingly broad substrate scope has been developed from Thermus nonproteolyticus β-glycosidase (TnG) by using site-directed mutagenesis. The practical utility of this biocatalyst has been demonstrated by the facile generation of a small library containing various oligosaccharides and a steroidal glycoside (total 25 compounds) in up to 100 % isolated yield. Moreover, an array of eight gluco-oligosaccharides has been readily synthesized by the enzyme in a one-pot, parallel reaction, which highlights its potential in the combinatorial construction of a carbohydrate library that will assist glycomic and glycotherapeutic research. Significantly, the enzyme provides a means by which glycosynthase technology may be extended to combinatorial chemistry.

Creation of an α-mannosynthase from a broad glycosidase scaffold

α-Mannosides made easy: Mutation of a family-GH31 α-glucosidase that displays plasticity to alterations at the 2-OH position of donor substrates created an efficient α-mannoside-synthesizing biocatalyst. A simple fluoride donor reagent was used for the synthesis of a range of mono-α-mannosylated conjugates using the α-mannosynthase displaying low (unwanted) oligomerization activity. Copyright

Isolation and characterization of a novel α-glucosidase with transglycosylation activity from Arthrobacter sp. DL001

A strain of Arthrobacter sp. DL001 with high transglycosylation activity was successfully isolated from the Yellow Sea of China. To purify the extracellular enzyme responsible for transglycosylation, a four-step protocol was adopted and the enzyme with electrophoretical purity was obtained. The purified enzyme has a molecular mass of 210 kDa and displays a narrow hydrolysis specificity towards α-1,4-glucosidic bond. Its hydrolytic activity was identified as decreasing in the order of maltotriose > panose > maltose. Only 3.61% maltose activity occurs when p-nitrophenyl α-d-glycopyranoside serves as a substrate, suggesting that this enzyme belongs to the type II α-glucosidase. In addition, the enzyme was able to transfer glucosyl groups from the donors containing α-1,4-glucosidic bond specific to glucosides, xylosides and alkyl alcohols in α-1,4- or α-1,6-manners. A decreased order of activity was observed when maltose, maltotriose, panose, β-cyclodextrin and soluble starch served as glycosyl donors, respectively. When maltose was utilized as a donor and a series of p-nitrophenyl-glycosides as acceptors, the glucosidase was capable of transferring glucosyl groups to p-nitrophenyl-glucosides and p-nitrophenyl-xylosides in α-1,4- or α-1,6-manners. The yields of p-nitrophenyl-oligosaccharides could reach 42-60% in 2 h. When a series of alkyl alcohols were utilized as acceptors, the enzyme exhibited its transglycosylation activities not only to the primary alcohols but also to the secondary alcohols with carbon chain length 1-4. Therefore, all the results indicated that the purified α-glucosidase present a useful tool for the biosynthesis of oligosaccharides and alkyl glucosides.

Aryl O- and S-galactosides and lactosides as specific inhibitors of human galectins-1 and -3: Role of electrostatic potential at O-3

Phase transfer catalyzed reaction was used for the high yielding synthesis of aryl 1-thio-β-d-galacto- and lacto-pyranosides carrying a panel of substituents on the phenyl groups. Best galectin-1 inhibitors were simple p-nitrophenyl thiogalactoside 5a for

α-Glucosidase mutant catalyzes "α-glycosynthase"-type reaction

Replacement of the catalytic nucleophile Asp481 by glycine in Schizosaccharomyces pombe α-glucosidase eliminated the hydrolytic activity. The mutant enzyme (D481G) was found to catalyze the formation of an α-glucosidic linkage from β-glucosyl fluoride and