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Documentos Principais

T7407

Sigma-Aldrich

Trigalacturonic acid

≥90% (HPLC)

Sinônimo(s):

α-D-GalA-(1→4)-α-D-GalA-(1→4)-α-D-GalA, α-D-GalA-(1→4)-α-D-GalA-(1→4)-D-GalA

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About This Item

Fórmula empírica (Notação de Hill):
C18H26O19
Número CAS:
Peso molecular:
546.39
Número MDL:
Código UNSPSC:
12352201
ID de substância PubChem:
NACRES:
NA.25

Nível de qualidade

Ensaio

≥90% (HPLC)

forma

powder

cor

white

solubilidade

water: 50 mg/mL, clear, colorless

temperatura de armazenamento

−20°C

cadeia de caracteres SMILES

OC(C=O)C(O)C(OC1OC(C(OC2OC(C(O)C(O)C2O)C(O)=O)C(O)C1O)C(O)=O)C(O)C(O)=O

InChI

1S/C18H26O19/c19-1-2(20)3(21)10(9(27)14(28)29)34-18-8(26)6(24)11(13(37-18)16(32)33)35-17-7(25)4(22)5(23)12(36-17)15(30)31/h1-13,17-18,20-27H,(H,28,29)(H,30,31)(H,32,33)

chave InChI

FMNDXLWVYMQMHF-UHFFFAOYSA-N

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Outras notas

To gain a comprehensive understanding of our extensive range of Oligosaccharides for your research, we encourage you to visit our Carbohydrates Category page.

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, type N95 (US)


Certificados de análise (COA)

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Polygalacturonases are enzymes involved in the degradation of pectic substances, being extensively used in food industries, textile processing, degumming of plant rough fibres, and treatment of pectic wastewaters. Polygalacturonase (PG) production by thermophilic fungus Thermoascus aurantiacus on solid-state fermentation was
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The family 2 pectate lyase from Yersinia enterocolitica (YePL2A), solved to 1.5A, reveals it to be the first prokaryotic protein reported to display the rare (alpha/alpha)(7) barrel fold. In addition to its apo form, we have also determined the structure
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The aim of this study was to develop an Escherichia coli-based metabolic selection system for the uncovering of new oligogalacturonate-active enzymes. Based on the expression of the specific permease TogMNAB, this system enabled the entry of oligogalacturonates into the cytoplasm
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A new exopolygalacturonate lyase (Pel) gene of the hyperthermophilic bacterium Thermotoga maritima was cloned and overexpressed in Escherichia coli cells. A 42 kDa monomeric Pel was shown to undergo N-terminal processing by cleavage at a putative site between alanine and

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