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  4. Recombinant Pectate Lyase from Aspergillus sp.
Biologics

Recombinant Pectate Lyase from Aspergillus sp.

 Product Information

Cat #
MBS-1132
CAS No.
9015-75-2
Enzyme Commission Number
EC 4.2.2.2
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
polygalacturonic transeliminase; pectic acid transeliminase; polygalacturonate lyase; endopectin methyltranseliminase; pectate transeliminase; endogalacturonate transeliminase; pectic acid lyase; pectic lyase; α-1,4-D-endopolygalacturonic acid lyase; PGA lyase; PPase-N; endo-α-1,4-polygalacturonic acid lyase; polygalacturonic acid lyase; pectin trans-eliminase; Polygalacturonic acid trans-eliminase
Type
Function
Favours pectate, the anion, over pectin, the methyl ester (which is the preferred substrate of EC 4.2.2.10, pectin lyase).
Applications
Research and Development
Storage
Store at 4°C (or at -20°C long term).
Storage Buffer
Shelf Life
Strains
Aspergillus spp.
Source
Aspergillus sp.
Appearance
Molecular Weight
~ 45 kDa
Color / Form
Instruction
Enzyme Class
Lyases
Production Methods
Fermentation
Activity
180 U/mg protein on polygalacturonic acid (pH 8, 40°C).
Specific Enzyme Activity
Purity
Unit Definition
Amino Acids Sequence
WARNINGS
Shipping
Formula
Reaction
Eliminative cleavage of (1→4)-α-D-galacturonan to give oligosaccharides with 4-deoxy-α-D-galact-4-enuronosyl groups at their non-reducing ends
Recommendation
Species Reactivity
Contents
Compatibility
Melting Point
Final Titre
Fermentation Time
Recovery Yield
Starting Material
Specification
On customer requests
Substrates
Concentration
Usage And Dosage
Product Type
Enzymes

 Description

Pectate lyase (EC 4.2.2.2) is an enzyme involved in the maceration and soft rotting of plant tissue. Pectate lyase is responsible for the eliminative cleavage of pectate, yielding oligosaccharides with 4-deoxy-α-D-mann-4-enuronosyl groups at their non-reducing ends. The protein is maximally expressed late in pollen development. It has been suggested that the pollen expression of pectate lyase genes might relate to a requirement for pectin degradation during pollen tube growth. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides.

For Research Use Only.
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