<i>Burkholderia cepacia</i> lipase: A versatile catalyst in synthesis reactions

Sánchez, Daniel Alberto; Tonetto, Gabriela Marta; Ferreira, Marı́a Luján

doi:10.1002/bit.26458

Cited by 98 publications

(69 citation statements)

References 197 publications

(224 reference statements)

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“…As a result, lipases have application in the food, detergents, cosmetics, textile, pharmaceutical, and biofuels industries . Among available lipases, Burkholderia cepacia lipase (BCL), also known as Pseudomonas cepacia lipase, displays relevant biocatalytic properties, such as high substrate specificity and selectivity, high thermal stability, and high tolerance to nonaqueous solvents . Therefore, BCL is commonly applied in organic media, particularly when hydrophobic compounds are part of the reaction media .…”

Section: Introductionmentioning

confidence: 99%

“…14 Among available lipases, Burkholderia cepacia lipase (BCL), also known as Pseudomonas cepacia lipase, displays relevant biocatalytic properties, such as high substrate specificity and selectivity, high thermal stability, and high tolerance to nonaqueous solvents. 15 Therefore, BCL is commonly applied in organic media, particularly when hydrophobic compounds are part of the reaction media. 16,17 Nevertheless, most organic solvents applied display important disadvantageous, such as high vapor pressure, flammability, and toxicity.…”

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confidence: 99%

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Effects of phosphonium‐based ionic liquids on the lipase activity evaluated by experimental results and molecular docking

Barbosa

Freire

Souza

et al. 2019

Biotechnology Progress

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In this work, the effect of several phosphonium‐based ionic liquids (ILs) on the activity of lipase from Burkholderia cepacia (BCL) was evaluated by experimental assays and molecular docking. ILs comprising different cations ([P4444]+, [P444(14)]+, [P666(14)]+) and anions (Cl−, Br−, [Deca]−, [Phosp]−, [NTf2]−) were investigated to appraise the individual roles of IL ions on the BCL activity. From the activity assays, it was found that an increase in the cation alkyl chain length leads to a decrease on the BCL enzymatic activity. ILs with the anions [Phosp]− and [NTf2]− increase the BCL activity, while the remaining [P666(14)]‐based ILs with the Cl−, Br−, and [Deca]− anions display a negative effect on the BCL activity. The highest activity of BCL was identified with the IL [P666(14)][NTf2] (increase in the enzymatic activity of BCL by 61% at 0.055 mol·L−1). According to the interactions determined by molecular docking, IL cations preferentially interact with the Leu17 residue (amino acid present in the BCL oxyanion hole). The anion [Deca]− has a higher binding affinity compared to Cl− and Br−, and mainly interacts by hydrogen‐bonding with Ser87, an amino acid residue which constitutes the catalytic triad of BCL. The anions [Phosp]− and [NTf2]− have high binding energies (−6.2 and −5.6 kcal·mol−1, respectively) with BCL, and preferentially interact with the side chain amino acids of the enzyme and not with residues of the active site. Furthermore, FTIR analysis of the protein secondary structure show that ILs that lead to a decrease on the α‐helix content result in a higher BCL activity, which may be derived from an easier access of the substrate to the BCL active site.

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Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

Effects of phosphonium‐based ionic liquids on the lipase activity evaluated by experimental results and molecular docking

Barbosa

Freire

Souza

et al. 2019

Biotechnology Progress

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“…63 CRL is an isoenzyme showing a / hydrolase structure with a catalytic triad and a lid that covers the active site when the enzyme is in its inactive form. BCL is a widely used lipase due to its thermal resistance and tolerance to a large number of solvents and short-chain alcohols.…”

Section: Lipase Screeningmentioning

confidence: 99%

“…Hence adsorption of BCL on a hydrophobic polymeric support enhances its catalytic activity. 63 CRL is an isoenzyme showing a / hydrolase structure with a catalytic triad and a lid that covers the active site when the enzyme is in its inactive form. Its catalytic triad consists of Ser209-Glu341-His449, which is stabilized by a hydrogen bonding network.…”

Section: Lipase Screeningmentioning

confidence: 99%

Immobilized lipase catalyzed synthesis of n‐amyl acetate: parameter optimization, heterogeneous kinetics, continuous flow operation and reactor modeling

Mathpati

Kalghatgi

Mathpati

et al. 2018

J of Chemical Tech & Biotech

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BACKGROUND The work describes the synthesis of n‐amyl acetate from n‐amyl alcohol, a byproduct of the sugar industry. The synthesis was carried out using Burkholderia cepacia lipase immobilized on a hydrophobic polymer support containing hydroxypropyl methyl cellulose and polyvinyl alcohol. The reaction conditions were optimized and intrinsic kinetics were evaluated. An immobilized lipase‐coated film reactor was designed and evaluated for continuous flow synthesis. An attempt has been made to model the coated film reactor based on axial dispersion method. RESULTS The reaction conditions were optimized using a central composite design‐based response surface method. The optimum conditions for a maximum conversion of 99.5% were an acyl donor : alcohol ratio of 2:1, temperature 50 °C and catalyst loading 40 mg in n‐hexane. The intrinsic kinetics of reaction were fitted using an order bi–bi model with alcohol inhibition. The continuous flow synthesis was carried out in a coated film reactor with residence times ranging from 12 min to 60 min with per pass conversions of 5.6% and 22%, respectively. The catalyst was successfully recycled for five cycles. CONCLUSION The activation energy of the reaction was found to be 15.48 kJ mol−1. The productivity from batch and continuous flow reactor were found to be 8.16 and 6.54 mmol g−1 h−1. © 2018 Society of Chemical Industry

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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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Burkholderia cepacia lipase: A versatile catalyst in synthesis reactions

Cited by 98 publications

References 197 publications

Effects of phosphonium‐based ionic liquids on the lipase activity evaluated by experimental results and molecular docking

Effects of phosphonium‐based ionic liquids on the lipase activity evaluated by experimental results and molecular docking

Immobilized lipase catalyzed synthesis of n‐amyl acetate: parameter optimization, heterogeneous kinetics, continuous flow operation and reactor modeling

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

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