P5431
Pectolyase from Aspergillus japonicus
aseptically filled, lyophilized powder, ≥2 units/mg solid
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
sterility
aseptically filled
form
lyophilized powder
specific activity
≥2 units/mg solid
storage temp.
2-8°C
Looking for similar products? Visit Product Comparison Guide
Application
Used in plant protoplast preparation to digest cell wall prior to organelle isolation.
Other Notes
Reported to contain two types of pectinase, endopolygalacturonase (EC3.2.1.15), endopectin lyase (EC4.2.2.10) and a maceration stimulating factor.
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
Unit Definition
One unit will liberate 1.0 μmole of galacturonic acid from polygalacturonic acid per min at pH 5.5 at 25 °C.
Physical form
Lyophilized powder containing lactose
Preparation Note
Prepared from P 3026
comparable product
Product No.
Description
Pricing
Storage Class
13 - Non Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
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
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
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
S S Ahmed et al.
Genetics and molecular research : GMR, 11(3), 3091-3104 (2012-09-26)
Molecular chaperones of plasmid pBI121 carrying CaMV35S promoter and a nucleotide sequence of plasmid pBI221 were inserted into plasmid pCAMBIA2300 to construct an intermediate vector: pVBG2307. This novel vector pVBG2307 contains a greatly expanded multiple cloning site with an adjacent
Peerapat Roongsattham et al.
BMC plant biology, 12, 150-150 (2012-08-28)
Cell separation that occurs during fleshy fruit abscission and dry fruit dehiscence facilitates seed dispersal, the final stage of plant reproductive development. While our understanding of the evolutionary context of cell separation is limited mainly to the eudicot model systems
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service