Catalytic behavior of Pseudomonas cepacia lipase in w/o microemulsions

Stamatis, H; Xenakis, LA; Dimitriadis, LE; Kolisis, FN

dc.contributor.author	Stamatis, H	en
dc.contributor.author	Xenakis, LA	en
dc.contributor.author	Dimitriadis, LE	en
dc.contributor.author	Kolisis, FN	en
dc.date.accessioned	2014-03-01T01:10:52Z
dc.date.available	2014-03-01T01:10:52Z
dc.date.issued	1995	en
dc.identifier.issn	0006-3592	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/11467
dc.subject	Esterification	en
dc.subject	Glycerides	en
dc.subject	Kinetics	en
dc.subject	Lipase	en
dc.subject	Reverse micelles	en
dc.subject	Surfactants	en
dc.subject.classification	Biotechnology & Applied Microbiology	en
dc.subject.other	Alcohols	en
dc.subject.other	Bacteria	en
dc.subject.other	Catalysis	en
dc.subject.other	Esterification	en
dc.subject.other	Esters	en
dc.subject.other	Fatty acids	en
dc.subject.other	Hydrolysis	en
dc.subject.other	Micelles	en
dc.subject.other	Microemulsions	en
dc.subject.other	Reaction kinetics	en
dc.subject.other	Surface active agents	en
dc.subject.other	Synthesis (chemical)	en
dc.subject.other	Aliphatic alcohols	en
dc.subject.other	Bis-(2-ethylhexyl)sulfosuccinate sodium salt	en
dc.subject.other	Isooctane	en
dc.subject.other	Ping pong bi-bi mechanisms	en
dc.subject.other	Reverse micelles	en
dc.subject.other	Enzymes	en
dc.subject.other	surfactant	en
dc.subject.other	triacylglycerol	en
dc.subject.other	triacylglycerol lipase	en
dc.subject.other	article	en
dc.subject.other	emulsion	en
dc.subject.other	enzyme kinetics	en
dc.subject.other	esterification	en
dc.subject.other	nonhuman	en
dc.subject.other	pseudomonas	en
dc.subject.other	Burkholderia cepacia	en
dc.subject.other	Pseudomonas	en
dc.title	Catalytic behavior of Pseudomonas cepacia lipase in w/o microemulsions	en
heal.type	journalArticle	en
heal.identifier.primary	10.1002/bit.260450106	en
heal.identifier.secondary	http://dx.doi.org/10.1002/bit.260450106	en
heal.language	English	en
heal.publicationDate	1995	en
heal.abstract	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
heal.publisher	John Wiley & Sons Inc, New York, NY, United States	en
heal.journalName	Biotechnology and Bioengineering	en
dc.identifier.doi	10.1002/bit.260450106	en
dc.identifier.isi	ISI:A1995QF88700005	en
dc.identifier.volume	45	en
dc.identifier.issue	1	en
dc.identifier.spage	33	en
dc.identifier.epage	41	en