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L3295

Sigma-Aldrich

Phospholipase A1 from Aspergillus oryzae

Synonym(s):

Lecitase Ultra, PLA1

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About This Item

Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in Aspergillus oryzae

Quality Level

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.

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
Specific enrichment of 2-arachidonoyl-lysophosphatidylcholine in carotid atheroma plaque from type 2 diabetic patients
Menegaut L, et al.
Atherosclerosis, 251(1), 339-347 (2016)
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
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)
Patrick J Fleming et al.
Biochimica et biophysica acta, 1818(2), 126-134 (2011-08-06)
Understanding the forces that stabilize membrane proteins in their native states is one of the contemporary challenges of biophysics. To date, estimates of side chain partitioning free energies from water to the lipid environment show disparate values between experimental and

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