P5431
Pectolyase from Aspergillus japonicus
aseptically filled, lyophilized powder, ≥2 units/mg solid
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About This Item
sterility
aseptically filled
form
lyophilized powder
specific activity
≥2 units/mg solid
storage temp.
2-8°C
Application
Used in plant protoplast preparation to digest cell wall prior to organelle isolation.
Physical form
Lyophilized powder containing lactose
Preparation Note
Prepared from P 3026
Other Notes
One unit will liberate 1.0 μmole of galacturonic acid from polygalacturonic acid per min at pH 5.5 at 25 °C.
Reported to contain two types of pectinase, endopolygalacturonase (EC3.2.1.15), endopectin lyase (EC4.2.2.10) and a maceration stimulating factor.
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Storage Class
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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Paulo Roberto Adalberto et al.
The Analyst, 137(20), 4855-4859 (2012-09-05)
Polygalacturonases (EC 3.2.1.15) hydrolyze the α-1,4-glycosidic linkages in polygalacturonic acid chains. The interest on specific inhibitors of pectinase and the versatility of magnetic support for enzyme immobilization endorsed the preparation of an immobilized enzyme reactor (IMER). This work presents the
Shashi Kant et al.
Protein expression and purification, 87(1), 11-16 (2012-10-17)
Polygalacturonases are the pectinolytic enzymes that catalyze the hydrolytic cleavage of the polygalacturonic acid chain. In the present study, polygalacturonase from Aspergillus niger (MTCC 3323) was purified. The enzyme precipitated with 60% ethanol resulted in 1.68-fold purification. The enzyme was
Claudia Schinke et al.
International microbiology : the official journal of the Spanish Society for Microbiology, 15(1), 1-7 (2012-07-28)
Macrophomina phaseolina, phylum Ascomycota, is a phytopathogenic fungus distributed worldwide in hot dry areas. There are few studies on its secreted lipases and none on its colony radial growth rate, an indicator of fungal ability to use nutrients for growth