P0690
Pectinase from Aspergillus niger
BioReagent, suitable for plant cell culture, aqueous glycerol solution, ≥5 units/mg protein (Lowry)
Synonym(s):
Poly-(1,4-α-D-galacturonide) glycanohydrolase, Polygalacturonase solution from Aspergillus niger
product line
BioReagent
form
aqueous glycerol solution
specific activity
≥5 units/mg protein (Lowry)
technique(s)
cell culture | plant: suitable
application(s)
agriculture
storage temp.
2-8°C
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Application
Pectinase P0690 is a natural pectinase (polygalacturonase) produced by Aspergillus niger. This enzyme breaks down pectin found in the middle lamella of plant cell walls. Pectinase helps facilitate the maceration of plant materials and extraction processes including organelle preparation.
Used in plant protoplast preparation to digest cell wall prior to organelle isolation.
Physical form
Solution in 40% glycerol
Other Notes
One unit will liberate 1.0 μmole of galacturonic acid from polygalacturonic acid per min at pH 4.0 at 25 °C.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Vincenzo Lionetti et al.
Proceedings of the National Academy of Sciences of the United States of America, 107(2), 616-621 (2010-01-19)
Plant cell walls represent an abundant, renewable source of biofuel and other useful products. The major bottleneck for the industrial scale-up of their conversion to simple sugars (saccharification), to be subsequently converted by microorganisms into ethanol or other products, is
Sina Pricelius et al.
Journal of agricultural and food chemistry, 57(3), 1006-1012 (2009-02-05)
Attractive color is one of the most important sensory characteristics of fruit and berry products, and elderberry juice is widely used as natural colorant. When pectinase preparations were used in the production of elderberry juice for clarification, a concomitant decrease
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
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
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