How large are the active sites of the lipases from Candida rugosa and from Pseudomonas cepacia ?

Exl, Christina; Hönig, Helmut; Renner, G.; Rogi-Kohlenprath, Renate; Seebauer, Veronika; Seufer-Wasserthal, Peter

doi:10.1016/0957-4166(92)80014-n

Cited by 19 publications

(3 citation statements)

References 28 publications

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“…1 Pseudomonas cepacia (previously classified as P. fluorescens) lipase (PCL) is one of the most frequently used enzymes for enantioselective resolutions to create chiral alcohols. 2, 3 For secondary alcohols, the enzyme, together with a few other lipases, has been predicted to react with the enantiomer shown in Fig. 1 faster than the other enantiomer from an empirical rule based on the sizes of substituents at the carbon stereocentre.…”

Section: Introductionmentioning

confidence: 99%

Studies on hydrolysis of chiral, achiral and racemic alcohol esters with Pseudomonas cepacia lipase: mechanism of stereospecificity of the enzyme

Nishizawa¹,

Ohgami²,

Matsuo³

et al. 1997

J. Chem. Soc., Perkin Trans. 2

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Section: Introductionmentioning

confidence: 99%

Studies on hydrolysis of chiral, achiral and racemic alcohol esters with Pseudomonas cepacia lipase: mechanism of stereospecificity of the enzyme

Nishizawa¹,

Ohgami²,

Matsuo³

et al. 1997

J. Chem. Soc., Perkin Trans. 2

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“…Small fatty acids are not as good substrates as longer ones. Lipase from P. cepacia was shown to catalyze fatty acids with a length of at least 9.2 Å and a width of at most 3.6 Å . In 5-DSA, the presence of the doxyl ring, with dimensions of about 8 Å, at the fifth carbon atom of the fatty acid chain drastically modifies the width of the fatty acid moiety hindering the access of the active site.…”

Section: Resultsmentioning

confidence: 99%

Interfacial Properties of Lecithin Microemulsions in the Presence of Lipase. A Membrane Spin-Probe Study

1999

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The interfacial properties of lecithin layers in isooctane and in water-in-oil microemulsions were studied by electron paramagnetic resonance spectroscopy. The mobility of the spin probes 5- and 12-doxyl stearic acid (12-DSA) were monitored in both binary and tertiary lecithin systems. In the binary systems the two probes showed important differences caused by the relative positioning of the nitroxide group within the hydrophobic chains of lecithin. The concentration of lecithin also affected the mobility of the probe. In the lecithin microemulsions the presence of water and alcohol restored the probe mobility to some extent. Depending on the water content, the curvature of the lecithin layer was modified in a “hedgehog” way, i.e., when the size of the reverse micelles increased, the spacing among the hydrophobic lecithin tails decreased. The effect of the nature and concentration of the alcohol on the structure of the lecithin interface was also examined. The observed differences were mainly caused by the different partitioning of the alcohols among the various microdomains of the microemulsions. When an enzyme such as lipase was solubilized in the water core of the lecithin reverse micelles, the mobility of the 12-DSA was modified as a function of time. This was caused by the catalytic esterification of the fatty acid probe with propanol, a reaction that could be followed directly by monitoring the electron paramagnetic resonance spectra.

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“…Αυτή η υπόθεση ενισχύεται και από τη σύγκριση των διαστάσεων που έχουν αναφερθεί για το εύρος της υδρόφοβης θήκης του καταλυτικού κέντρου της λιπάσης και των διαστάσεων του πενταμελούς παραμαγνητικού δακτυλίου. Για την λιπάση από P.cepacia οι Exl και συνεργάτες (Exl et al 1992) (Fersht, 1985).…”

Section: επίδραση της παρουσίας ενζύμων στα μικρογαλακτώματαunclassified

Δομικες Μελετες Μικρογαλακτωματων Παρουσια Ενεργων Μακρομοριων.

Αβραμιώτης¹

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Γ. Στάικο. Επίκουρο Καθηγητή και Κ. Τσιγγάνο, Καθηγητή, κατά τη σημερινή συνεδρίαση για την κρίση της διδακτορικής διατριβής του κ. Σπύρου Αβραμιώτη με θέμα: Δομικές μελέτες μικρογαλακτωμάτων παρουσία ενεργών μακρομορίων. Ψήφισε &.&Ρ.φ.** , ..'Ζ.^.$. ότι το περιεχόμενο της διατριβής είναι πρωτότυπο και αποτελεί ουσιαστική συμβολή στην επιστήμη και την βαθμολόγησε με το βαθμό Ä/^/.^.^e.

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How large are the active sites of the lipases from Candida rugosa and from Pseudomonas cepacia ?

Cited by 19 publications

References 28 publications

Studies on hydrolysis of chiral, achiral and racemic alcohol esters with Pseudomonas cepacia lipase: mechanism of stereospecificity of the enzyme

Studies on hydrolysis of chiral, achiral and racemic alcohol esters with Pseudomonas cepacia lipase: mechanism of stereospecificity of the enzyme

Interfacial Properties of Lecithin Microemulsions in the Presence of Lipase. A Membrane Spin-Probe Study

Δομικες Μελετες Μικρογαλακτωματων Παρουσια Ενεργων Μακρομοριων.

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