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Merck

L3295

Sigma-Aldrich

Phospholipase A1 from Aspergillus oryzae

Sinónimos:

Lecitase Ultra, PLA1

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About This Item

Comisión internacional de enzimas:
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

signalword

Danger

hcodes

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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Structure and function of phosphatidylserine-specific phospholipase A1
Aoki J, et al.
Biochimica et Biophysica Acta, 1582(1-3), 26-32 (2002)
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
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
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)
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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