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[ CAS No. 2001-96-9 ] {[proInfo.proName]}

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Cat. No.: {[proInfo.prAm]}
Chemical Structure| 2001-96-9
Chemical Structure| 2001-96-9
Structure of 2001-96-9 * Storage: {[proInfo.prStorage]}
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Product Details of [ 2001-96-9 ]

CAS No. :2001-96-9 MDL No. :MFCD00047519
Formula : C11H13NO7 Boiling Point : -
Linear Structure Formula :- InChI Key :MLJYKRYCCUGBBV-YTWAJWBKSA-N
M.W : 271.22 Pubchem ID :91509
Synonyms :

Calculated chemistry of [ 2001-96-9 ]

Physicochemical Properties

Num. heavy atoms : 19
Num. arom. heavy atoms : 6
Fraction Csp3 : 0.45
Num. rotatable bonds : 3
Num. H-bond acceptors : 7.0
Num. H-bond donors : 3.0
Molar Refractivity : 63.44
TPSA : 124.97 Ų

Pharmacokinetics

GI absorption : High
BBB permeant : No
P-gp substrate : No
CYP1A2 inhibitor : No
CYP2C19 inhibitor : No
CYP2C9 inhibitor : No
CYP2D6 inhibitor : No
CYP3A4 inhibitor : No
Log Kp (skin permeation) : -8.2 cm/s

Lipophilicity

Log Po/w (iLOGP) : 1.1
Log Po/w (XLOGP3) : -0.34
Log Po/w (WLOGP) : -0.59
Log Po/w (MLOGP) : -1.36
Log Po/w (SILICOS-IT) : -2.35
Consensus Log Po/w : -0.71

Druglikeness

Lipinski : 0.0
Ghose : None
Veber : 0.0
Egan : 0.0
Muegge : 0.0
Bioavailability Score : 0.55

Water Solubility

Log S (ESOL) : -1.34
Solubility : 12.3 mg/ml ; 0.0454 mol/l
Class : Very soluble
Log S (Ali) : -1.82
Solubility : 4.08 mg/ml ; 0.015 mol/l
Class : Very soluble
Log S (SILICOS-IT) : 0.0
Solubility : 271.0 mg/ml ; 1.0 mol/l
Class : Soluble

Medicinal Chemistry

PAINS : 0.0 alert
Brenk : 2.0 alert
Leadlikeness : 0.0
Synthetic accessibility : 3.84

Safety of [ 2001-96-9 ]

Signal Word:Warning Class:N/A
Precautionary Statements:P261-P305+P351+P338 UN#:N/A
Hazard Statements:H302-H315-H319-H335 Packing Group:N/A
GHS Pictogram:

Application In Synthesis of [ 2001-96-9 ]

* All experimental methods are cited from the reference, please refer to the original source for details. We do not guarantee the accuracy of the content in the reference.

  • Downstream synthetic route of [ 2001-96-9 ]

[ 2001-96-9 ] Synthesis Path-Downstream   1~85

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  • [ 2816-24-2 ]
  • [ 144683-70-5 ]
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  • [ 87-72-9 ]
  • [ 100-02-7 ]
YieldReaction ConditionsOperation in experiment
With water; In aq. buffer; at 45℃; for 0.166667h;pH 7.5;Kinetics; The standard activity assay used pNP beta-D-Xylp as substrate. Release of p-nitrophenol (pNP) was measured by continuous monitoring at 401 nm. Reactions were performed in 50 mM Tris-HCl, pH 7.5 and the substrate concentration was 5 mM. Assays were performed at 45 C for 10 min. Activity was determined by using a standard calibration curve for pNP (epsilon = 12514M-1cm-1). One unit of beta-xylosidase activity was defined as the amount of enzyme releasing 1 mumol of pNP per minute. Kinetic parameters Km and kcat were determined using variable substrate concentrations (1-75 mM) in the standard assay. Data were calculated from triplicate assays. Kinetic parameters were derived from Michaelis-Menten representations using the SigmaPlot 2000 software (version 6.1 with Enzyme Kinetics module 1.0; SPSS Science, Paris, France).
  • 9
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  • [ 6763-34-4 ]
  • [ 100-02-7 ]
  • 10
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  • [ 100-02-7 ]
YieldReaction ConditionsOperation in experiment
With dalcochinase F1H96 mutant; sodium acetate; at 30℃;pH 5;Enzymatic reaction;Kinetics; General procedure: The catalytic efficiencies (kcat/Km) of the wild-type and mutant forms of dalcochinase for hydrolysis of various pNP-glycoside substrates were determined from progress curves at low substrate concentrations (less than 1/5 Km of wild-type dalcochinase toward the same substrate) in 0.1 M sodium acetate, pH 5.0 at 30 C. The pnitrophenol released was monitored by following the absorbance at 360 nm until substrate depletion was observed. When the substrate concentration is low, the rate of reaction (v) is related to the substrate concentration by the equation:35nu=kcat/Km[E]0[S]. The change in absorbance with respect to time was fitted to first-order rate equation using the program GraFit 5.0 (ErithacusSoftware Limited, Horley, UK) to yield pseudo-first-order rate constant that corresponds to (kcat/Km) [E]0. Since [E]0, which was the concentration of enzyme used in the reaction, was known, the value of kcat/Km could be easily obtained.
With Os4BGlu13; In aq. acetate buffer; at 30℃; for 0.25h;pH 5;Enzymatic reaction; The activities of protein fractions to hydrolyze pNPGlc weretested in a manner similar to previously published methods[27e30]. Aliquots of enzyme solutions were incubated with 4 mMpNPGlc in 50 mM sodium acetate (NaOAc) buffer, pH 5.0, (totalreaction volume 50 ml) at 30 C for 20 min. The reactions werestopped by adding 150 ml of 2 M sodium carbonate (Na2CO3). Thereleased p-nitrophenol (pNP) was quantified by measuring theabsorbance at 405 nm (A405) with a microplate reader (ThermoLabsystems, Helsinki, Finland), and comparing it to that of a pNPstandard curve. The hydrolysis of GA4-GE was determined by asimilar reaction in 50 mM NaOAc, followed with a peroxidase/glucose oxidase-based glucose assay (PGO assay, SigmaeAldrich),as previously described [24]. In all cases, control reactions incubated without b-glucosidase enzyme served as blanks. Proteinconcentrations were determined with a Bio-Rad Bradford assaywith bovine serum albumin (BSA) as a standard.
With recombinant beta-xylosidase Dt-xyl3 from Dictyoglomus turgidum; In aq. buffer; at 75℃; for 0.166667h;pH 5;Enzymatic reaction;Kinetics; General procedure: pNP method. The reaction mixture contained the following: 10 muL of20mM substrate pNPX dissolved in sodium phosphate buffer (50 mM,pH 6.0), 180 muL of sodium phosphate buffer (50 mM, pH 6.0) and 10 muLof purified enzyme. The reaction was carried out at 75 C for 10 min,and the reaction was quenched by adding 600 muL of Na2CO3 (1 M) [6].The enzymatic activity was immediately measured by detecting theliberated pNP at 405 nm. For every sample, the activity was measuredthree separate times. One unit of beta-xylosidase activity (1 U) was definedas the amount of enzyme required to liberate 1 mumol of pNP per minuteunder the above assay conditions, which is consistent with the literaturereference [17].
  • 11
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  • (2S,3R,4R,5R)-2-(4-Nitro-phenoxy)-5-triethylsilanyloxy-tetrahydro-pyran-3,4-diol [ No CAS ]
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  • [ 79-04-9 ]
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  • [ 173468-09-2 ]
  • 14
  • [ 2106-10-7 ]
  • [ 2001-96-9 ]
  • p-nitrophenyl (β-D-glucopyranosyl)-(1->3)-(β-D-glucopyranosyl)-(1->3)-β-D-xylopyranoside [ No CAS ]
  • C29H43NO22 [ No CAS ]
  • 4-nitrophenyl β-D-glucopyranosyl-(1->3)-β-D-xylopyranoside [ No CAS ]
  • 15
  • [ 2021-84-3 ]
  • [ 2001-96-9 ]
  • [ 144683-69-2 ]
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  • [ 7512-17-6 ]
  • [ 2001-96-9 ]
  • N-[(3R,4R,5S,6R)-2,4,5-Trihydroxy-6-((2S,3R,4S,5R)-3,4,5-trihydroxy-tetrahydro-pyran-2-yloxymethyl)-tetrahydro-pyran-3-yl]-acetamide [ No CAS ]
  • 17
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  • [ 144683-70-5 ]
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  • [ 249928-93-6 ]
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  • [ 144683-70-5 ]
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  • [ 2021-62-7 ]
  • [ 2001-96-9 ]
  • [ 144683-70-5 ]
  • [ 144683-69-2 ]
  • 22
  • ginsenoside Re [ No CAS ]
  • [ 2001-96-9 ]
  • 20(S)-protopanaxatriol 6-O-α-L-rhamnopyranosyl-(1->2)-[β-D-xylopyranosyl-1(->4)]-β-D-glucopyranosyl-20-O-β-D-glucopyranoside [ No CAS ]
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  • [ 173468-35-4 ]
  • p-nitrophenyl β-D-xylopyranosyl-(1->4)-tris [(1->4)-β-D-(1->4)-xylopyranosyl]-β-D-xylopyranoside [ No CAS ]
  • p-nitrophenyl β-D-xylopyranosyl-(1->4)-tetrakis [(1-> 4)-β-D-(1->4)-xylopyranosyl]-β-D-xylopyranoside [ No CAS ]
  • p-nitrophenyl β-D-xylopyranosyl-(1-> 4)-pentakis-[(1-> 4)-β-D-(1-> 4)-xylopyranosyl]-β-D-xylopyranoside [ No CAS ]
  • 24
  • [ 2001-96-9 ]
  • [ 220069-61-4 ]
  • p-nitrophenyl (β-D-glucopyranosyl)-(1->3)-(β-D-glucopyranosyl)-(1->3)-β-D-xylopyranoside [ No CAS ]
  • 26
  • [ 108-05-4 ]
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  • [ 709663-88-7 ]
  • 4-nitrophenyl 2-O-acetyl-β-D-xylopyranoside [ No CAS ]
  • 4-nitrophenyl 3-O-acetyl-β-D-xylopyranoside [ No CAS ]
  • [ 709663-85-4 ]
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  • [ 108-05-4 ]
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  • 4-nitrophenyl 2,4-di-O-acetyl-β-D-xylopyranoside [ No CAS ]
  • [ 709663-85-4 ]
  • 28
  • [ 2001-96-9 ]
  • [ 59997-96-5 ]
  • p-nitrophenyl β-D-xylopyranosyl-(1->2)-β-D-xylopyranoside [ No CAS ]
  • p-nitrophenyl β-D-xylopyranosyl-(1->3)-β-D-xylopyranoside [ No CAS ]
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  • [ 2816-24-2 ]
  • [ 144683-70-5 ]
  • [ 144683-69-2 ]
  • (2S,3R,4S,5R,6R)-2-[(2S,3R,4S,5R)-4,5-Dihydroxy-2-(4-nitro-phenoxy)-tetrahydro-pyran-3-yloxy]-6-hydroxymethyl-tetrahydro-pyran-3,4,5-triol [ No CAS ]
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  • [ 2001-96-9 ]
  • (4R,5R,6S)-4,5-Dihydroxy-6-(4-nitro-phenoxy)-dihydro-pyran-3-one [ No CAS ]
  • [ 808770-13-0 ]
  • [ 808770-18-5 ]
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  • [ 3945-26-4 ]
  • [ 108-24-7 ]
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  • 4-nitrophenyl (2,3,4-tri-O-acetyl-β-D-xylopyranosyl)-(1->3)-O-2,4-di-O-acetyl-β-D-xylopyranoside [ No CAS ]
  • 4-nitrophenyl [(2,3,4-tri-O-acetyl-β-D-xylopyranosyl)-(1->4)-O-2,3-di-O-acetyl-β-D-xylopyranosyl]-(1->3)-O-2,4-di-O-acetyl-β-D-xylopyranoside [ No CAS ]
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  • (2S,3R,4S,5R)-2-{(3R,4R,5R,6S)-6-[(2S,3R,4S,5R)-3,5-Dihydroxy-2-(4-nitro-phenoxy)-tetrahydro-pyran-4-yloxy]-4,5-dihydroxy-tetrahydro-pyran-3-yloxy}-tetrahydro-pyran-3,4,5-triol [ No CAS ]
  • [ 6819-07-4 ]
  • [ 173468-29-6 ]
  • p-nitrophenyl β-D-xylopyranosyl-(1->3)-β-D-xylopyranoside [ No CAS ]
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  • [ 2106-10-7 ]
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  • 4-nitrophenyl β-D-glucopyranosyl-(1->4)-β-D-xylopyranoside [ No CAS ]
  • 4-nitrophenyl β-D-glucopyranosyl-(1->3)-β-D-xylopyranoside [ No CAS ]
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  • [ 2021-84-3 ]
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  • [ 144683-70-5 ]
  • [ 144683-69-2 ]
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  • [ 100-02-7 ]
  • MOC-L-Phe-albumin [ No CAS ]
  • [ 2001-96-9 ]
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  • [ 2001-96-9 ]
  • 4-nitrophenyl 2,3-di-O-acetyl-4-O-chloroacetyl-β-D-xylopyranoside [ No CAS ]
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  • [ 173468-12-7 ]
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  • [ 162088-89-3 ]
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  • p-nitrophenyl 2,4-di-O-sulfo-β-D-xylopyranoside disodium salt [ No CAS ]
  • p-nitrophenyl 2,3,4-tri-O-sulfo-β-D-xylopyranoside trisodium salt [ No CAS ]
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  • p-nitrophenyl 2,3-di-O-sulfo-β-D-xylopyranoside disodium salt [ No CAS ]
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  • p-nitrophenyl 2-O-sulfo-β-D-xylopyranoside sodium salt [ No CAS ]
  • p-nitrophenyl 2,3-di-O-sulfo-β-D-xylopyranoside disodium salt [ No CAS ]
  • 54
  • [ 2001-96-9 ]
  • p-nitrophenyl 3-O-sulfo-β-D-xylopyranoside sodium salt [ No CAS ]
  • p-nitrophenyl 4-O-sulfo-β-D-xylopyranoside sodium salt [ No CAS ]
  • p-nitrophenyl 3,4-di-O-sulfo-β-D-xylopyranoside disodium salt [ No CAS ]
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  • [ 1235988-94-9 ]
  • [ 637761-31-0 ]
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  • [ 1033330-68-5 ]
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  • [ 1258524-24-1 ]
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  • [ 552-71-6 ]
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  • [ 2280-44-6 ]
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  • [ 498-05-5 ]
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  • [ 10257-28-0 ]
  • [ 2001-96-9 ]
  • β-D-xylopyranosyl-(1->6)-D-galactopyranoside [ No CAS ]
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  • [ 530-26-7 ]
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  • [ 20880-58-4 ]
  • 66
  • [ 87-72-9 ]
  • [ 2001-96-9 ]
  • β-D-xylopyranosyl-(1->4)-D-lyxopyranoside [ No CAS ]
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  • [ 28697-53-2 ]
  • [ 2001-96-9 ]
  • C10H18O9 [ No CAS ]
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  • [ 2001-96-9 ]
  • [ 57-50-1 ]
  • [ 1281872-79-4 ]
  • [ 177092-90-9 ]
  • 69
  • [ 2001-96-9 ]
  • [ 58166-22-6 ]
  • β-D-xylopyranosyl-(1->4)-α-D-glucopyranosyl-(1->3)-β-D-fructofuranoside [ No CAS ]
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  • [ 35899-89-9 ]
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  • [ 1357933-61-9 ]
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  • [ 2956-16-3 ]
  • [ 2001-96-9 ]
  • [ 144683-70-5 ]
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  • [ 3945-26-4 ]
  • [ 108-24-7 ]
  • [ 2001-96-9 ]
  • 4-nitrophenyl (2,3,4-tri-O-acetyl-β-D-xylopyranosyl)-(1->3)-O-2,4-di-O-acetyl-β-D-xylopyranoside [ No CAS ]
  • [ 162088-89-3 ]
  • 4-nitrophenyl O-(2,3,4-tri-O-acetyl-β-D-xylopyranosyl)-(1<*>4)-O-(2,3-di-O-acetyl-β-D-xylopyranosyl)-(1<*>4)-2,3-di-O-acetyl-β-D-xylopyranoside [ No CAS ]
  • [ 24624-78-0 ]
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  • [ 3945-26-4 ]
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  • [ 173468-29-6 ]
  • 74
  • [ 1226-39-7 ]
  • [ 35599-02-1 ]
  • [ 2106-10-7 ]
  • [ 2001-96-9 ]
  • [ 2492-87-7 ]
  • [ 3150-24-1 ]
  • 4-nitrophenyl β-D-glucopyranosyl-(1->3)-β-D-fucopyranoside [ No CAS ]
  • 4-nitrophenyl β-D-glucopyranosyl-(1->3)-β-D-galactopyranoside [ No CAS ]
  • C23H33NO17 [ No CAS ]
  • 4-nitrophenyl β-D-glucopyranosyl-(1->4)-β-D-xylopyranoside [ No CAS ]
  • [ 26255-70-9 ]
  • 4-nitrophenyl β-D-glucopyranosyl-(1->3)-β-D-xylopyranoside [ No CAS ]
  • 4-nitrophenyl β-D-glucopyranosyl-(1→4)-β-D-mannopyranoside [ No CAS ]
  • [ 2713-54-4 ]
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  • [ 4049-33-6 ]
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  • [ 2001-96-9 ]
  • [ 100-02-7 ]
  • [ 58-86-6 ]
YieldReaction ConditionsOperation in experiment
With Aspergillus niger GS1 beta-xylosidase; In aq. acetate buffer; at 60℃;pH 5;Enzymatic reaction;Kinetics; Concentrations of p-nitrophenyl-beta-d-xylopyranoside were varied from 0.3 to 10mM. Substrate dilutions were contacted with 0.2mug beta-xylosidase in sodium acetate buffer pH 5.0, at 60C, in a total volume of 300muL. Kinetic parameters were estimated by fitting initial velocities (Vo) versus substrate concentrations to the Michaelis-Menten equation using a non-linear correlation curve-fitting software (Graph-Pad Prism 5.00; San Diego, CA, USA).
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  • [ 111-87-5 ]
  • [ 2001-96-9 ]
  • [ 6743-68-6 ]
YieldReaction ConditionsOperation in experiment
With GH39 xylosidase from Bacillus halodurans, F116A mutant; In water; at 45℃; for 1h; General procedure: The synthesis of pentyl and octyl xyloside by the wild-type enzyme and the mutant enzymes were carried out in water. The reaction medium was composed by the donor, pNP beta-D-Xylp (5 mM), the acceptor, pentan-1-ol or octan-1-ol (5 and 10%, v/v, respectively), the enzyme (0.1 IU/mL) and an internal standard for HPLC analysis, hexyl glucoside (3 mM). The reactions (1-1.5 mL) were carried out in closed glass vessels with a magnetic stirring and were incubated in a thermostated oil bath for 1 h at 45 C under vigorous agitation (1000 r.p.m.). The reactions were stopped by incubating the reaction mixtures during 10 min at 100 C, then were evaporated using a speed vac concentrator and resuspended in DMSO (90 muL), centrifuged (10 min, 2000 × g) in order to pellet the residues and filtered on 0.2 mum (PTFE membrane). The quantification of alkyl xylosides was performed by HPLC using a RP-C18 column (Nucleodur 100-5 C18 ec, 250mm × 4mm, Macherey Nagel). Standard alkyl xylosides were purified as previously described [8]. Products were eluted at 0.6 mL/min with a mobile phase composed of an acetonitrile:water mixture (20:80 for pentyl xylosides and 40:60 for octyl xylosides). The detection of eluates was performed with a dynamic light scattering detector (PL-ELS 1000; Polymer Laboratories). The amounts of xylosides produced were corrected by using the internal standard concentration detected. Results are expressed as mean values obtained from triplicate reactions which allow calculating standard errors.
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  • [ 71-41-0 ]
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  • [ 6743-66-4 ]
YieldReaction ConditionsOperation in experiment
With GH39 xylosidase from Bacillus halodurans; In water; at 45℃; for 1h; General procedure: The synthesis of pentyl and octyl xyloside by the wild-type enzyme and the mutant enzymes were carried out in water. The reaction medium was composed by the donor, pNP beta-D-Xylp (5 mM), the acceptor, pentan-1-ol or octan-1-ol (5 and 10%, v/v, respectively), the enzyme (0.1 IU/mL) and an internal standard for HPLC analysis, hexyl glucoside (3 mM). The reactions (1-1.5 mL) were carried out in closed glass vessels with a magnetic stirring and were incubated in a thermostated oil bath for 1 h at 45 C under vigorous agitation (1000 r.p.m.). The reactions were stopped by incubating the reaction mixtures during 10 min at 100 C, then were evaporated using a speed vac concentrator and resuspended in DMSO (90 muL), centrifuged (10 min, 2000 × g) in order to pellet the residues and filtered on 0.2 mum (PTFE membrane). The quantification of alkyl xylosides was performed by HPLC using a RP-C18 column (Nucleodur 100-5 C18 ec, 250mm × 4mm, Macherey Nagel). Standard alkyl xylosides were purified as previously described [8]. Products were eluted at 0.6 mL/min with a mobile phase composed of an acetonitrile:water mixture (20:80 for pentyl xylosides and 40:60 for octyl xylosides). The detection of eluates was performed with a dynamic light scattering detector (PL-ELS 1000; Polymer Laboratories). The amounts of xylosides produced were corrected by using the internal standard concentration detected. Results are expressed as mean values obtained from triplicate reactions which allow calculating standard errors.
  • 80
  • [ 2001-96-9 ]
  • [ 2460-44-8 ]
YieldReaction ConditionsOperation in experiment
With CAZyme xylosidase 1 from Lucigen; sodium succinate; at 25℃;pH 6;Enzymatic reaction;Kinetics; Catalytic behavior; Initial-rates for determination of kinetic parameters acting on4NPX and 4NPA reactions were conducted by adding enzyme toreactions containing substrate equilibrated at 25 C and continuouslymonitoring the 400 nm absorbance change over time(380 nm for pH 3.5). pH 4 and 4.5 reactions were run using a discontinuousmethod; adding aliquots of 4NPX reaction mixturesto 100 mM sodium hydroxide and aliquots of 4NPA reaction mixturesto 100 mM sodium carbonate pH 11 at various time pointsand reading the absorbance at 400 nm.
  • 81
  • [ 2106-10-7 ]
  • [ 2001-96-9 ]
  • p-nitrophenyl 6-O-(β-D-glucopyranosyl)-4-O-(β-D-glucopyranosyl)-β-D-xylopyranoside [ No CAS ]
  • 4-nitrophenyl β-D-glucopyranosyl-(1->4)-β-D-xylopyranoside [ No CAS ]
  • 4-nitrophenyl β-D-glucopyranosyl-(1->3)-β-D-xylopyranoside [ No CAS ]
  • 82
  • 4-nitrophenyl 2-O-acetyl-β-D-xylopyranoside [ No CAS ]
  • [ 2001-96-9 ]
  • 83
  • 4-nitrophenyl 3-O-acetyl-β-D-xylopyranoside [ No CAS ]
  • [ 2001-96-9 ]
  • 85
  • [ 2001-96-9 ]
  • [ 100-02-7 ]
  • [ 2460-44-8 ]
YieldReaction ConditionsOperation in experiment
With beta-D-xylosidase from Aspergillus awamori X-100; water; In aq. acetate buffer; at 37℃;pH 4.5;Enzymatic reaction;Kinetics; beta-Xylosidase activity towards p-nitrophenyl beta-D-xylopyranoside (pNPXyl) was determined at 37 C in 50 mM sodium acetate buffer,pH 4.5. One unit of the b-D-xylosidase activity was defined as anamount of the enzyme releasing 1 mM of p-nitrophenol from pNPXyl per min.
With beta-xylosidase B from Bifidobacterium adolescentis ATCC15703; bovine serum albumin; In aq. buffer; at 30℃;pH 5;Enzymatic reaction;Kinetics; General procedure: All kinetic studies were carried out by discontinuous assays in glass tubes at 30 C as follows. Different substrate concentrations were solubilised in 450 muL of 100 mM sodium citrate buffer, pH 5.0, supplemented with 0.1% BSA (w/v). Initial hydrolysis rates were determined by adding 50 muL of properly diluted enzyme to the reaction mix. Enzyme concentrations used for kinetic measurements are mentioned in Table 1. At time intervals, 50 muL of samples were taken and the reaction stopped by the addition of 250 muL of 1M Na2CO3. The released chromogenic groups were determined in micro-plates by reading 200 muL of the stopped reaction mix using a Sunrise spectrophotometer (Tecan). The extinction coefficient used and wavelength monitored for each of the substrate used were: 3,4-dinitrophenol (3,4-dNP), Deltaepsilon=1.30 mM-1cm-1, lambda= 405 nm; 4-nitrophenol (4-NP), Deltaepsilon= 1.60 mM-1cm-1, lambda= 405 nm; 2-nitrophenol (2-NP), Deltaepsilon=0.31 mM-1cm-1, lambda= 405 nm; 4-methylumbelliferone (4-MU), Deltaepsilon=1.68 mM-1cm-1, lambda=360 nm. The quantity of released leaving group (LG) was calculated using appropriate standard curves and negative controls containing all of the reactants except the enzyme, in order to remove background noise issued from spontaneous hydrolysis of the substrates. The values of kcat and Km were determined by non-linear regression analysis using the program SigmaPlot 11.0. In cases where the Km values were too high to be estimated, kcat/Km values were calculated from the reaction rates at low substrate concentration. Indeed, when [S]?Km the reaction rates are given by the equation v=kcat[E]0[S]/Km and thus kcat/Km can be calculated by dividing the slope of the plot of v=f([S]) by the enzyme concentration.
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