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Sigma-Aldrich

Pectinase from Aspergillus niger

aqueous solution

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Synonym(s):
Pectinex 3XL®, Pectinex® 3X L
CAS Number:
9032-75-1
Enzyme Commission number:
3.2.1.15 (BRENDA, IUBMB)
EC Number:
232-885-6
MDL number:
MFCD00131809

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.

Other Notes

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

Legal Information

A product of Novozyme Corp.
Pectinex is a registered trademark of Novozymes Corp.

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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
Tao Tu et al.
Food chemistry, 141(3), 2974-2981 (2013-07-23)
A novel endo-polygalacturonase (endo-PG I) from Achaetomium sp. Xz8 was identified, overexpressed in Pichia pastoris, and characterized in this report. Recombinant endo-PG I is distinguished from other enzyme counterparts by its high activity towards polygalacturonic acid (49,934 U/ml) and high
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
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
Sara Posé et al.
Journal of experimental botany, 64(12), 3803-3815 (2013-07-23)
Antisense-mediated down-regulation of the fruit-specific polygalacturonase (PG) gene FaPG1 in strawberries (Fragaria×ananassa Duch.) has been previously demonstrated to reduce fruit softening and to extend post-harvest shelf life, despite the low PG activity detected in this fruit. The improved fruit traits
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