Liu_2016_Enzyme.Microb.Technol_82_82

Reference

Title : Lipase-catalyzed synthesis of palmitanilide: Kinetic model and antimicrobial activity study - Liu_2016_Enzyme.Microb.Technol_82_82
Author(s) : Liu KM , Liu KJ
Ref : Enzyme Microb Technol , 82 :82 , 2016
Abstract :

Enzymatic syntheses of fatty acid anilides are important owing to their wide range of industrial applications in detergents, shampoo, cosmetics, and surfactant formulations. The amidation reaction of Mucor miehei lipase Lipozyme IM20 was investigated for direct amidation of triacylglycerol in organic solvents. The process parameters (reaction temperature, substrate molar ratio, enzyme amount) were optimized to achieve the highest yield of anilide. The maximum yield of palmitanilide (88.9%) was achieved after 24 h of reaction at 40 degreesC at an enzyme concentration of 1.4% (70 mg). Kinetics of lipase-catalyzed amidation of aniline with tripalmitin has been investigated. The reaction rate could be described in terms of the Michaelis-Menten equation with a Ping-Pong Bi-Bi mechanism and competitive inhibition by both the substrates. The kinetic constants were estimated by using non-linear regression method using enzyme kinetic modules. The enzyme operational stability study showed that Lipozyme IM20 retained 38.1% of the initial activity for the synthesis of palmitanilide (even after repeated use for 48 h). Palmitanilide, a fatty acid amide, exhibited potent antimicrobial activity toward Bacillus cereus.

PubMedSearch : Liu_2016_Enzyme.Microb.Technol_82_82
PubMedID: 26672452
Gene_locus related to this paper: rhimi-lipas

Related information

Substrate Tripalmitin
Gene_locus rhimi-lipas

Citations formats

Liu KM, Liu KJ (2016)
Lipase-catalyzed synthesis of palmitanilide: Kinetic model and antimicrobial activity study
Enzyme Microb Technol 82 :82

Liu KM, Liu KJ (2016)
Enzyme Microb Technol 82 :82