Catalytic behavior of Pseudomonas cepacia lipase in w/o microemulsions

 
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1995 (EN)
Catalytic behavior of Pseudomonas cepacia lipase in w/o microemulsions (EN)

Dimitriadis, LE (EN)
Stamatis, H (EN)
Kolisis, FN (EN)
Xenakis, LA (EN)

N/A (EN)

The activity of purified Pseudomonas cepacia lipase has been investigated in esterification reactions of various aliphatic alcohols with natural fatty acids. The reactions were carried out in microemulsions formed in isooctane by bis-(2-ethylhexyl)sulfosuccinate sodium salt (AOT). Kinetic studies showed that the reaction follows a ping-pong bi-bi mechanism with inhibition by both substrates. The apparent kinetic parameters of the reaction were found to be K(m octanol) = 310 mM, K(m lauric acid) = 78 mM, and V(max) = 250 μmol min-1 mg-1. The same system was used for the synthesis of mono- and diglycerides from glycerol and lauric acid, which was successful at very low(o) values. The catalytic behavior of P. cepacia lipase was also studied in esterification reactions performed in a nonionic microemulsion system formulated by tetraethyleneglycoldodecylether (C12E4). The optimum activity was found at about w(o) = 8. The apparent values of V(max app) and K(m app) for octanol were calculated and found to be 100 μmol min-1 mg-1 and 76 mM, respectively.The activity of purified Pseudomonas cepacia lipase has been investigated in esterification reactions of various aliphatic alcohols with natural fatty acids. The reactions were carried out in microemulsions formed in isooctane by bis-(2-ethylhexyl)sulfosuccinate sodium salt (AOT). Kinetic studies showed that the reaction follows a pingpong bi-bi mechanism with inhibition by both substrates. The apparent kinetic parameters of the reaction were found to be Km octanol = 310 mM, Km lauric acid = 78 mM, and Vmax = 250 μmol min-1 mg-1. The same system was used for the synthesis of mono- and diglycerides from glycerol and lauric acid, which was successful at very low wo values. The catalytic behavior of P. cepacia lipase was also studied in esterification reactions performed in a nonionic microemulsion system formulated by tetraethyleneglycoldodecylether (C12E4). The optimum activity was found at about wo = 8. The apparent values of Vmax app and Km app for octanol were calculated and found to be 100 μmol min-1 mg-1 and 76 mM, respectively. (EN)

journalArticle

Glycerides (EN)
pseudomonas (EN)
triacylglycerol (EN)
Esters (EN)
Lipase (EN)
Isooctane (EN)
Pseudomonas (EN)
Alcohols (EN)
Surface active agents (EN)
Aliphatic alcohols (EN)
Micelles (EN)
Burkholderia cepacia (EN)
Reaction kinetics (EN)
emulsion (EN)
Bacteria (EN)
Catalysis (EN)
Microemulsions (EN)
Bis-(2-ethylhexyl)sulfosuccinate sodium salt (EN)
Reverse micelles (EN)
surfactant (EN)
Enzymes (EN)
triacylglycerol lipase (EN)
Ping pong bi-bi mechanisms (EN)
Surfactants (EN)
Fatty acids (EN)
Esterification (EN)
article (EN)
enzyme kinetics (EN)
Synthesis (chemical) (EN)
Hydrolysis (EN)
esterification (EN)
nonhuman (EN)
Kinetics (EN)

Εθνικό Μετσόβιο Πολυτεχνείο (EL)
National Technical University of Athens (EN)

Biotechnology and Bioengineering (EN)

1995


John Wiley & Sons Inc, New York, NY, United States (EN)



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