L3295
Phospholipase A1 from Aspergillus oryzae
Synonym(s):
Lecitase™ Ultra, PLA1
recombinant
expressed in Aspergillus oryzae
form
liquid
specific activity
≥10 KLU/g
storage temp.
2-8°C
Quality Level
Analysis Note
minimum activity 10 KLU/G liquid
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)
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).
Legal Information
Lecitase is a trademark of Novozymes Corp.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
常规特殊物品
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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)
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
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)
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