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L3295

Sigma-Aldrich

Phospholipase A1 from Aspergillus oryzae

Synonyme(s) :

Lecitase Ultra, PLA1

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About This Item

Numéro de classification (Commission des enzymes):
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Produit recombinant

expressed in Aspergillus oryzae

Niveau de qualité

Forme

liquid

Activité spécifique

≥10 KLU/g

Température de stockage

2-8°C

Description générale

Phospholipase A1 (PLA1) catalyzes the hydrolysis of acyl group from position 1 of lecithin to yield lysolecithin. It is expressed in a wide range of organisms such as rat platelets, bovine brain and testis, hornet venom, bonito muscle and fungi. Gene coding for PLA1 consists of four exons and three short introns spanning 1,056bp of genomic DNA. Mature protein contains 269 aminoacids and two possible N-glycosylation sites (Asn27 and Asn55).

Application

Phospholipase A1 from Aspergillus oryzae has been used:
  • in the preparation of sn-1 and sn-2 C18:1- lysophosphatidylcholine (LPC) regioisomer standards
  • as a catalyst for the synthesis 6-O-glucosyl-poly(3-hydroxyalkanoates) in a micro-aqueous system
  • to catalyze the synthesis of methyl butanoate and methyl benzoate flavor esters in continuous flow microreactor
  • to hydrolyze 17:0 phosphocholine (PC)

Remarque sur l'analyse

minimum activity 10 KLU/G liquid

Informations légales

Lecitase is a trademark of Novozymes Corp.

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

Thermomyces lanuginosus lipase-catalyzed synthesis of natural flavor esters in a continuous flow microreactor
Gumel AM and Annuar MSM
3 Biotech, 6(1), 24-24 (2016)
Naoaki Arima et al.
Journal of lipid research, 53(3), 513-521 (2011-12-17)
Members of the pancreatic lipase family exhibit both lipase activity toward triacylglycerol and/or phospholipase A(1) (PLA(1)) activity toward certain phospholipids. Some members of the pancreatic lipase family exhibit lysophospholipase activity in addition to their lipase and PLA(1) activities. Two such
Yukichi Fujikawa et al.
Lipids, 47(3), 303-312 (2011-11-30)
A cDNA encoding protein with homology to plant secretory phospholipase A₂ (sPLA₂), denoted as Nt1 PLA₂, was isolated from tobacco (Nicotiana tabacum). The cDNA encodes a mature protein of 118 amino acid residues with a putative signal peptide of 29
Nicole A Housley et al.
Journal of bacteriology, 193(18), 4634-4642 (2011-07-19)
Here we have characterized the Rickettsia prowazekii RP534 protein, a homologue of the Pseudomonas aeruginosa ExoU phospholipase A (PLA) secreted cytotoxin. Our studies showed that purified recombinant RP534 PLA possessed the predicted PLA(2) and lyso-PLA(2) activities based on what has
Alyssa L Bolen et al.
Journal of lipid research, 52(5), 958-970 (2011-03-12)
Platelet activation initiates an upsurge in polyunsaturated (18:2 and 20:4) lysophosphatidic acid (LPA) production. The biochemical pathway(s) responsible for LPA production during blood clotting are not yet fully understood. Here we describe the purification of a phospholipase A(1) (PLA(1)) from

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