L3295
Phospholipase A1 from Aspergillus oryzae
Synonym(s):
Lecitase™ Ultra, PLA1
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L3295-50ML
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recombinant
expressed in Aspergillus oryzae
Quality Level
form
liquid
specific activity
≥10 KLU/g
storage temp.
2-8°C
1 of 4
This Item | L0777 | P6534 | P8913 |
|---|---|---|---|
| specific activity ≥10 KLU/g | specific activity ≥100,000 U/g | specific activity ≥600 units/mg protein | specific activity ≥20 units/mg protein |
| form liquid | form solution | form ammonium sulfate suspension | form lyophilized powder |
| recombinant expressed in Aspergillus oryzae | recombinant - | recombinant - | recombinant - |
| storage temp. 2-8°C | storage temp. 2-8°C | storage temp. 2-8°C | storage temp. −20°C |
| Quality Level 200 | Quality Level 200 | Quality Level 200 | Quality Level 200 |
General description
Phospholipase A1 (PLA1) catalyzes the hydrolysis of acyl group from position 1 of lecithin to yield lysolecithin.[1] It is expressed in a wide range of organisms such as rat platelets, bovine brain and testis, hornet venom, bonito muscle and fungi.[2] 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).[1]
Application
Phospholipase A1 from Aspergillus oryzae has been used:
- in the preparation of sn-1 and sn-2 C18:1- lysophosphatidylcholine (LPC) regioisomer standards[3]
- as a catalyst for the synthesis 6-O-glucosyl-poly(3-hydroxyalkanoates) in a micro-aqueous system[4]
- to catalyze the synthesis of methyl butanoate and methyl benzoate flavor esters in continuous flow microreactor[5]
- to hydrolyze 17:0 phosphocholine (PC)[6]
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
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C Preston Moon et al.
Proceedings of the National Academy of Sciences of the United States of America, 108(25), 10174-10177 (2011-05-25)
The transfer free energies of the twenty natural amino acid side chains from water to phospholipid bilayers make a major contribution to the assembly and function of membrane proteins. Measurements of those transfer free energies will facilitate the identification of
Structure and function of phosphatidylserine-specific phospholipase A1
Aoki J, et al.
Biochimica et Biophysica Acta, 1582(1-3), 26-32 (2002)
Enzymatic synthesis of 6-O-glucosyl-poly (3-hydroxyalkanoate) in organic solvents and their binary mixture
Gumel AM, et al.
International Journal of Biological Macromolecules (2013)
Yuh-Ren Chen et al.
Archives of microbiology, 193(6), 419-428 (2011-03-10)
The lysis protein of the colicinogenic operon is essential for colicin release and its main function is to activate the outer membrane phospholipase A (OMPLA) for the traverse of colicin across the cell envelope. However, little is known about the
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)
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