P3026
Pectolyase from Aspergillus japonicus
lyophilized powder, ≥0.3 units/mg solid
Synonyma:
Pectolytic enzyme
Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen
About This Item
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Doporučené produkty
biological source
Aspergillus sp. (A. japonicus)
form
lyophilized powder
specific activity
≥0.3 units/mg solid
mol wt
50 kDa
greener alternative product characteristics
Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.
sustainability
Greener Alternative Product
greener alternative category
, Enabling
storage temp.
2-8°C
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General description
We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for energy efficiency and waste prevention when used in cellulosic ethanol research. For more information see the article in biofiles and Enzymes for Alternative Energy Research.
Pectolyase or pectin lyase is stable in the temperature range of 40-50°C and is a 50 kDa enzyme with an isoelectric pH of 3.8.
Pectolyase or pectin lyase is stable in the temperature range of 40-50°C and is a 50 kDa enzyme with an isoelectric pH of 3.8.
Application
Pectolyase from Aspergillus japonicus has been used:
- in the lysis of chlorella cells for protoplast generation
- as component of enzyme digestion buffer for Arabidopsis meiotic chromosome isolation
- to induce reorganization of Arabidopsis root cap cell architecture
Used in plant protoplast preparation to digest cell wall prior to organelle isolation. It is used in complex carbohydrate analysis. Product P3026 is provided in a lyophilized powder containing lactose. Product P3026 has been used to digest Crassula root tips prior to meiotic analysis.
Used in plant protoplast preparation to digest cell wall prior to organelle isolation.
Biochem/physiol Actions
Pectolyase catalyzes the eliminative cleavage of a-(1- 4)-Dgalacturonan methyl ester to give oligosaccharides with 4-deoxy-6-O-methyl-a-D-galact-4-enuronosyl groups at their non-reducing ends. It contain two types of pectinase, endopolygalacturonase, endo-pectin lyase and a maceration stimulating factora.
Pectolyase is used for protoplast isolation from plant cells. It also mediates ethylene hormone synthesis.
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.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Osvědčení o analýze (COA)
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Zákazníci si také prohlíželi
Susann Hesse et al.
Frontiers in plant science, 10, 773-773 (2019-07-10)
During prophase I a meiosis-specific proteinaceous tripartite structure, the synaptonemal complex (SC), forms a scaffold to connect homologous chromosomes along their lengths. This process, called synapsis, is required in most organisms to promote recombination between homologs facilitating genetic variability and
P J De Lange et al.
Annals of botany, 101(6), 881-899 (2007-12-07)
Crassula hunua and C. ruamahanga have been taxonomically controversial. Here their distinctiveness is assessed so that their taxonomic and conservation status can be clarified. Populations of these two species were analysed using morphological, chromosomal and DNA sequence data. It proved
Identification of sporopollenin as the outer layer of cell wall in microalga Chlorella protothecoides
He X, et al.
Frontiers in Microbiology, 7, 1047-1047 (2016)
Pectic enzymes in pectolyase: separation, characterization, and induction of ethylene in fruits
Baldwin EA and Pressey R
Plant Physiology, 90(1), 191-196 (1989)
Isolation and properties of pectinases from the fungus Aspergillus japonicus
Semenova MV, et al.
Biochemistry (Moscow), 68(5), 559-569 (2003)
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