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X3876 Sigma-Aldrich

Xylanase from Trichoderma viride

Green Alternative

lyophilized powder, 100-300 units/mg protein

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

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Description

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 from Trichoderma viride was shown to have molecular weight of 22 kDa with a Pi of 9.3.

Xylanase is a hemicellulolytic enzyme. It is synthesized by microorganisms like bacteria, yeast and fungi.

Application

Xylanase from Trichoderma viride has been used as a component of an enzyme mixture for the hydrolysis of hemicellulose-rich solution (autohydrolysate). 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.

Packaging

1000 units in glass bottle

250 units in poly bottle

Biochem/physiol Actions

Xylanase (endo-1,4-β-Xylanase) is involved in the hydrolysis of xylan. 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.

Unit Definition

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

Physical form

Contains sorbitol and sodium acetate buffer salts

Other Notes

View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer

Safety & Documentation

Safety Information

Personal Protective Equipment 
RIDADR 
NONH for all modes of transport
WGK Germany 
WGK 3
Flash Point(F) 
Not applicable
Flash Point(C) 
Not applicable
Protocols & Articles

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References

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