L3295
Phospholipase A1 from Aspergillus oryzae
Sinónimos:
Lecitase™ Ultra, PLA1
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About This Item
Productos recomendados
recombinant
expressed in Aspergillus oryzae
form
liquid
specific activity
≥10 KLU/g
storage temp.
2-8°C
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).
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)
Analysis Note
minimum activity 10 KLU/G liquid
Legal Information
Lecitase is a trademark of Novozymes Corp.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
10 - Combustible liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificados de análisis (COA)
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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
Structure and function of phosphatidylserine-specific phospholipase A1
Biochimica et Biophysica Acta, 1582(1-3), 26-32 (2002)
Molecular cloning and expression of the gene encoding a phospholipase A1 from Aspergillus oryzae
Bioscience, Biotechnology, and Biochemistry, 63(5), 820-826 (1999)
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