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X3876

Xylanase from Trichoderma viride

greener alternative

lyophilized powder, ≥100 units/mg protein

Sinónimos:

1,4-β-D-Xylanxylanohydrolase, endo-1,4-β-Xylanase

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Número CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-800-2
MDL number:
Número CE:
Specific activity:
≥100 units/mg protein
Biological source:
fungus (Trichoderma viride)
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biological source

fungus (Trichoderma viride)

Quality Level

form

lyophilized powder

specific activity

≥100 units/mg protein

mol wt

22 kDa

greener alternative product characteristics

Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.

sustainability

Greener Alternative Product

foreign activity

β-glucosidase and β-xylosidase ≤0.1%, cellulase <0.2%

greener alternative category

storage temp.

2-8°C

General description

We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for energy efficiency and waste prevention when used in cellulosic ethanol research. For more information see the article in biofiles and Enzymes for Alternative Energy Research
Xylanase is a hemicellulolytic enzyme. It is synthesized by microorganisms like bacteria, yeast and fungi.[1]
Xylanase from Trichoderma viride was shown to have molecular weight of 22 kDa with a Pi of 9.3.

Application

Xylanase from Trichoderma viride has been used as a component of an enzyme mixture for the hydrolysis of hemicellulose-rich solution (autohydrolysate).[2] It has also been used as a cell-wall degrading enzyme to determine the efficiency of p-coumaryl esterase to release p-coumaroyl and feruloyl group.[3]

Biochem/physiol Actions

Xylanase (endo-1,4-β-Xylanase) is involved in the hydrolysis of xylan.[4] It has a wide range of applications in industrial processes such as, bioleeching of craft pulp in paper industry and production of hydrolysates from agro-industrial wastes. Xylanase is also used in nutritional enhancement of lignocellulosic feed and in clarification of juice and wines.[1]

Physical form

Contains sorbitol and sodium acetate buffer salts

Other Notes

One unit will liberate 1 μmole of 4-nitrophenol from 4-nitrophenol-xylan per min at pH 4.5 at 30 °C.

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Este artículo
C8546A7420H2125
specific activity

≥100 units/mg protein

specific activity

≥1 unit/mg solid

specific activity

30-60 units/mg protein (biuret)

specific activity

0.3-3.0 unit/mg solid (using a β-galactose dehydrogenase system and locust bean gum as substrate)

biological source

fungus (Trichoderma viride)

biological source

-

biological source

-

biological source

-

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

powder

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

mol wt

22 kDa

mol wt

-

mol wt

-

mol wt

-

foreign activity

β-glucosidase and β-xylosidase ≤0.1%, cellulase <0.2%

foreign activity

-

foreign activity

-

foreign activity

-


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pictograms

Health hazard

signalword

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hcodes

Hazard Classifications

Resp. Sens. 1

Clase de almacenamiento

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)



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Contenido relacionado

Instructions


Saleh Sabiha-Hanim et al.
Bioresource technology, 102(2), 1234-1239 (2010-08-28)
Oil palm (Elaeis guineensis Jacq.) is one of the most important commercial crops for the production of palm oil, which generates 10.88 tons of oil palm fronds per hectare of plantation as a by-product. In this study, oil palm frond
M L T M Polizeli et al.
Applied microbiology and biotechnology, 67(5), 577-591 (2005-06-10)
Xylan is the principal type of hemicellulose. It is a linear polymer of beta-D-xylopyranosyl units linked by (1-4) glycosidic bonds. In nature, the polysaccharide backbone may be added to 4-O-methyl-alpha-D-glucuronopyranosyl units, acetyl groups, alpha-L-arabinofuranosyl, etc., in variable proportions. An enzymatic
Agnieszka Wikiera et al.
Molecules (Basel, Switzerland), 26(5) (2021-04-04)
The biological activity of apple pectin extracted conventionally or enzymatically using endo-xylanase and endo-cellulase, was tested in vitro. The analyses were performerd in tetraplicates and the statistical significance of the differences were assessed using ANOVA, Tukey post hoc and LSD



Número de artículo de comercio global

SKUGTIN
X3876-250UN04061837546310
X3876-1KU04061832851877

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