L3295
Phospholipase A1 from Aspergillus oryzae
Synonym(s):
Lecitase™ Ultra, PLA1
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About This Item
Specific activity:
≥10 KLU/g
Recombinant:
expressed in Aspergillus oryzae
recombinant
expressed in Aspergillus oryzae
form
liquid
specific activity
≥10 KLU/g
storage temp.
2-8°C
Quality Level
Analysis Note
minimum activity 10 KLU/G liquid
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)
General description
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).
Legal Information
Lecitase is a trademark of Novozymes Corp.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
常规特殊物品
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S G Monic et al.
Scientific reports, 12(1), 4766-4766 (2022-03-21)
Phospholipases are esterases involved in lipid catabolism. In pathogenic micro-organisms (bacteria, fungi, parasites) they often play a critical role in virulence and pathogenicity. A few phospholipases (PL) have been characterised so far at the gene and protein level in unicellular
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
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)
Jonah E Zarrow et al.
Journal of lipid research, 63(1), 100156-100156 (2021-11-30)
N-acyl-phosphatidylethanolamine (NAPE)-hydrolyzing phospholipase D (NAPE-PLD) is a zinc metallohydrolase enzyme that converts NAPEs to bioactive N-acyl-ethanolamides. Altered NAPE-PLD activity may contribute to pathogenesis of obesity, diabetes, atherosclerosis, and neurological diseases. Selective measurement of NAPE-PLD activity is challenging, however, because of
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
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