X3876
Xylanase from Trichoderma viride
lyophilized powder, 100-300 units/mg protein
Synonym(s):
1,4-β-D-Xylanxylanohydrolase, endo-1,4-β-Xylanase
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About This Item
Recommended Products
biological source
fungus (Trichoderma viride)
Quality Level
form
lyophilized powder
specific activity
100-300 units/mg protein
mol wt
22 kDa
composition
Protein, ~50% biuret
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
, Enabling
storage temp.
2-8°C
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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.
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
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Meenakshi Goyal et al.
Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology], 39(3), 535-541 (2008-07-01)
In the present study, cultural and nutritional conditions for enhanced production of xylanase by a local soil isolate of Trichoderma viride, using various lignocellulosic substrates in submerged culture fermentation have been optimized. Of the lignocellulosics used, maize straw was the
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
Low-molecular-weight xylanase from Trichoderma viride
Ujiie, M.
Applied and Environmental Microbiology, 57, 1860-1862 (1994)
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
W S Borneman et al.
Applied and environmental microbiology, 57(8), 2337-2344 (1991-08-01)
An extracellular p-coumaroyl esterase produced by the anaerobic fungus Neocallimastix strain MC-2 released p-coumaroyl groups from 0-[5-0-((E)-p-coumaroyl)-alpha-L-arabinofuranosyl]-(1----3)-0-beta -D-xylopyranosyl-(1----4)-D-xylopyranose (PAXX). The esterase was purified 121-fold from culture medium in successive steps involving ultrafiltration column chromatography on S-sepharose and hydroxylapatite, isoelectric focusing
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