P3026
Pectolyase from Aspergillus japonicus
lyophilized powder, ≥0.3 units/mg solid
Synonyme(s) :
Pectolytic enzyme
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About This Item
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54
Produits recommandés
Source biologique
Aspergillus sp. (A. japonicus)
Forme
lyophilized powder
Activité spécifique
≥0.3 units/mg solid
Poids mol.
50 kDa
Caractéristiques du produit alternatif plus écologique
Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.
sustainability
Greener Alternative Product
Autre catégorie plus écologique
, Enabling
Température de stockage
2-8°C
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Description générale
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.
Actions biochimiques/physiologiques
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.
Autres remarques
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
Définition de l'unité
One unit will liberate 1.0 μmole of galacturonic acid from polygalacturonic acid per min at pH 5.5 at 25 °C.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
Certificats d'analyse (COA)
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Les clients ont également consulté
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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