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Bacillus subtilis Xylanase Enzyme (Food Grade)

 Product Information

Cat #
MBS-0976
CAS No.
9025-57-4
Enzyme Commission Number
EC 3.2.1.8
Product Overview
High-quality enzyme products. Well-defined strains can be also provided for our clients to manufacture fermented products in a cost-effective way.
Features
Ready-to-use product, accelerating research progress, enhancing application performance.
Method
Technology
Synonyms
endo-(1→4)-β-xylan 4-xylanohydrolase; endo-1,4-xylanase; xylanase; β-1,4-xylanase; endo-1,4-xylanase; endo-β-1,4-xylanase; endo-1,4-β-D-xylanase; 1,4-β-xylan xylanohydrolase; β-xylanase; β-1,4-xylan xylanohydrolase; endo-1,4-β-xylanase; β-D-xylanase
Type
Function
Applications
Research Use
Storage
Should be stored in a dry and cool place, avoiding high temperature.
Storage Buffer
Shelf Life
Strains
Bacillus subtilis
Source
Bacillus subtilis
Appearance
Molecular Weight
Color / Form
Instruction
Enzyme Class
Hydrolases
Production Methods
Fermentation
Activity
> 200,000u/g
Specific Enzyme Activity
Purity
Unit Definition
One unit of Xylanase equals to the amount of enzyme, which hydrolyzes xylan to get 1 μg Of reducing sugar (in xylose) in 1 min. at 50°C and pH5.0.
Amino Acids Sequence
WARNINGS
Shipping
Formula
Reaction
Endohydrolysis of (1→4)-β-D-xylosidic linkages in xylans
Recommendation
Species Reactivity
Contents
Compatibility
Melting Point
Final Titre
Fermentation Time
Recovery Yield
Starting Material
Specification
On customer requests
Substrates
Concentration
Usage And Dosage

 Description

Xylanase is the name given to a class of enzymes which degrade the linear polysaccharide beta-1,4-xylan into xylose, thus breaking down hemicellulose, one of the major components of plant cell walls. As such, it plays a major role in micro-organisms thriving on plant sources for the degradation of plant matter into usable nutrients. Xylanases are produced by fungi, bacteria, yeast, marine algae, protozoans, snails, crustaceans, insect, seeds, etc., (mammals do not produce xylanases).

For Research Use Only.
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