P2736
Pectinase from Aspergillus niger
aqueous solution
Synonym(s):
Pectinex 3XL®, Pectinex® 3X L
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About This Item
CAS Number:
UNSPSC Code:
12352204
EC Number:
232-885-6
MDL number:
Product Name
Pectinase from Aspergillus niger, aqueous solution
form
aqueous solution
concentration
≥3000 units/mL
storage temp.
2-8°C
Application
Petctinase is an enzyme from Aspergillus niger that is used in plant protoplast preparation to digest cell wall prior to organelle isolation. It has been used to conduct partial saccharification of sugars. Pectinases are used to study their role in the invasion of plant tissues by phytopathogens, the spoilage of produce and various food processing and plant biotechnology applications.
Biochem/physiol Actions
Pectolytic enzyme preparation produced from a selected strain of Aspergillus niger: contains mainly pectintranseliminase, polygalacturonase, and pectinesterase and small amounts of hemicellulases and cellulases. Pectinases hydrolyses pectin, which is a component of the cell wall. They may attack methyl-esterified pectin or de-esterified pectin. It is a source of pectinase activity, also containing cellulase and hemicellulase activities.
Legal Information
A product of Novozyme Corp.
Pectinex is a registered trademark of Novozymes Corp.
Other Notes
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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Meredith C Edwards et al.
Applied and environmental microbiology, 77(15), 5184-5191 (2011-06-15)
Ethanologenic Escherichia coli strain KO11 was sequentially engineered to contain the Klebsiella oxytoca cellobiose phosphotransferase genes (casAB) as well as a pectate lyase (pelE) from Erwinia chrysanthemi, yielding strains LY40A (casAB) and JP07 (casAB pelE), respectively. To obtain an effective
Ding-Tao Wu et al.
Carbohydrate polymers, 97(2), 398-405 (2013-08-06)
Polysaccharides from Ganoderma spp. and their adulterants were firstly investigated and compared using saccharide mapping, enzymatic (endo-1,3-β-D-glucanase and pectinase) digestion followed by polysaccharide analysis using carbohydrate gel electrophoresis analysis. The results showed that both 1,3-β-D-glucosidic and 1,4-α-D-galactosiduronic linkages were existed
Junjiao Zhang et al.
Bioresource technology, 146, 543-548 (2013-08-27)
The present work aims to construct a robust recombinant Bacillus subtilis to achieve secretory production of alkaline polygalacturonate lyase (PGL). First, 6 signal peptides (amyX, bpr, vpr, yvgO, wapA and nprE) were screened with a semi-rational approach and comparatively investigated
Mahejibin Khan et al.
Annual review of food science and technology, 4, 21-34 (2012-11-30)
The understanding that enzymatic degradation of fruit pectin can clarify juices and improve juice yields resulted in the search for microbial pectinases and application in vegetable- and fruit-processing industries. Identified enzymes were classified on the basis of their catalytic activity
Roselei Claudete Fontana et al.
Bioresource technology, 123, 157-163 (2012-09-04)
The production of endo- and exo-polygalacturonase (PG) by Aspergillus oryzae was assessed in stirred tank reactors (STRs), internal-loop airlift reactors (ILARs) and external-loop airlift reactors (ELARs). For STR production, we compared culture media formulated with either pectin (WBE) or partially
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