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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

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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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
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
Molecular cloning and expression of the gene encoding a phospholipase A1 from Aspergillus oryzae
Watanabe I, et al.
Bioscience, Biotechnology, and Biochemistry, 63(5), 820-826 (1999)

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