Pseudomonas fluorescens lipase in asymmetric synthesis

Xie, Zhuo-Feng

doi:10.1016/s0957-4166(00)80450-4

Cited by 179 publications

(11 citation statements)

References 35 publications

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“…Increasing the steric bulk in the 3-position led to dramatic enhancement of the configurational stability; for the tert-butyl derivative 426c, a complete chirality transfer occurred 307 . Some epimerization took place with the 3-cyclohexylalkynyl carbamate 307 .…”

Section: Synthetic Applications Of Lithiated N-boc-allylaminesmentioning

confidence: 99%

Asymmetric Deprotonation with Alkyllithium–(−)‐Sparteine

Hoppe

Christoph

2009

Patai's Chemistry of Functional Groups

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Introduction Non‐Mesomerically Stabilized Organolithium Compounds (−)‐Sparteine‐Induced Lithiation with Formation of Benzyl‐Type Organolithiums Allyllithium–(−)‐Sparteine Complexes Lithium–(−)‐Sparteine Complexes of 2‐Alkynyl Carbamates Axial–Chiral and Planar–Chiral Lithium–(−)‐Sparteine Complexes Enantioselective Addition of Achiral Carbanionic Compounds in the Presence of (−)‐Sparteine

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Section: Synthetic Applications Of Lithiated N-boc-allylaminesmentioning

confidence: 99%

Asymmetric Deprotonation with Alkyllithium–(−)‐Sparteine

Hoppe

Christoph

2009

Patai's Chemistry of Functional Groups

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“…In this new study, the effect of the immobilization conditions on the final properties of the lipase from Pseudomonas fluorescens (PFL) has been studied. PFL is a lipase presenting a large lid and it is very used in literature (Xie, 1991;Gilbert, 1993;Rosenau and Jaeger, 2000;Rios et al, 2018;Sánchez et al, 2018) and has been used as model in different studies, like the lipase-lipase interactions that promote the formation of lipase-lipase aggregates involving two open lipase structures (Fernández-Lorente et al, 2003;Palomo et al, 2004Palomo et al, , 2005. The comparison of the effect of the immobilization conditions on the features of the biocatalyst when using highly loaded and a lowly loaded biocatalysts is presented.…”

Section: Introductionmentioning

confidence: 99%

Effects of Enzyme Loading and Immobilization Conditions on the Catalytic Features of Lipase From Pseudomonas fluorescens Immobilized on Octyl-Agarose Beads

Arana-Peña

Rios

Carballares

et al. 2020

Front. Bioeng. Biotechnol.

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The lipase from Pseudomonas fluorescens (PFL) has been immobilized on octyl-agarose beads under 16 different conditions (varying pH, ionic strength, buffer, adding some additives) at two different loadings, 1 and 60 mg of enzyme/g of support with the objective of check if this can alter the biocatalyst features. The activity of the biocatalysts versus p-nitrophenyl butyrate and triacetin and their thermal stability were studied. The different immobilization conditions produced biocatalysts with very different features. Considering the extreme cases, using 1 mg/g preparations, PFL stability changed more than fourfolds, while their activities versus pNPB or triacetin varied a 50-60%. Curiously, PFL specific activity versus triacetin was higher using highly enzyme loaded biocatalysts than using lowly loaded biocatalysts (even by a twofold factor). Moreover, stability of the highly loaded preparations was higher than that of the lowly loaded preparations, in many instances even when using 5 • C higher temperatures (e.g., immobilized in the presence of calcium, the highly loaded biocatalysts maintained after 24 h at 75 • c a 85% of the initial activity, while the lowly loaded preparation maintained only 27% at 70 • C). Using the highly loaded preparations, activity of the different biocatalysts versus pNPB varied almost 1.7-folds and versus triacetin 1.9-folds. In this instance, the changes in stability caused by the immobilization conditions were much more significant, some preparations were almost fully inactivated under conditions where the most stable one maintained more than 80% of the initial activity. Results suggested that immobilization conditions greatly affected the properties of the immobilized PFL, partially by individual molecule different conformation (observed using lowly loaded preparations) but much more relevantly using highly loaded preparations, very likely by altering some enzymeenzyme intermolecular interactions. There is not an optimal biocatalyst considering all parameters. That way, preparation of biocatalysts using this support may be a powerful tool to tune enzyme features, if carefully controlled.

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“…Some lipases are also stable in non-aqueous organic solvents and catalyze the esterification and transesterification reactions. [1][2][3][4][5] The specific catalysis of the lipases enables production of useful polyesters by various polymerization modes. 6 Lactones, such as β-butyrolactone, ε-caprolactone and so on, can be the substrates of the lipase-catalyzed ringopening polymerization, 7,8 while hydroxy fatty acids can be used as the substrates of another reation type lipase-catalyzed polycondensation.…”

Section: Introductionmentioning

confidence: 99%

Enzymatic formation of 13,26-Dihexyl-1,14-dioxacyclohexacosane-2,15-dione via Oligomerization of 12-Hydroxystearic acid

2009

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The enzymatic polymerization of 12-hydroxystearic acid (12-HSA) was carried out with Lipase CA ® in benzene to produce poly(12-hydroxystearate) (PHS) with a low molecular weight. When this polymerization was continued for a long reaction time, the PHS once formed was depolymerized into a cyclic diester, 13,16-dihexyl-1,14-dioxacyclohexacosane-2,15-dione (12-HSAD). Similar polymerization and depolymerization were observed when 12-hydroxyoleic acid (12-HOA) was treated with Lipase CA ® , whereas only polymerization occurred when 12-hydroxydodecanoic acid (12-HDA) was treated in a similar manner. The preferential formation of cyclic diesters for 12-HSA was attributed to the structural requirements due to the bulky n-hexyl side groups stemming from the ring systems.

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Pseudomonas fluorescens lipase in asymmetric synthesis

Cited by 179 publications

References 35 publications

Asymmetric Deprotonation with Alkyllithium–(−)‐Sparteine

Asymmetric Deprotonation with Alkyllithium–(−)‐Sparteine

Effects of Enzyme Loading and Immobilization Conditions on the Catalytic Features of Lipase From Pseudomonas fluorescens Immobilized on Octyl-Agarose Beads

Enzymatic formation of 13,26-Dihexyl-1,14-dioxacyclohexacosane-2,15-dione via Oligomerization of 12-Hydroxystearic acid

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