Lipases: An Overview

Casas-Godoy, Leticia; Gasteazoro, Francisco; Duquesne, Sophie; Bordes, Florence; Marty, Alain; Sandoval, Georgina

doi:10.1007/978-1-4939-8672-9_1

Cited by 98 publications

(104 citation statements)

References 151 publications

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“…Leu17 is one of the two hydrogen‐bond donor amino acid residues that constitute the BCL oxyanion hole and stabilize the tetrahedral intermediate during catalysis. As described before, the two constituent's amino acids (Leu17 and Gln88) of the BCL oxyanion hole are responsible for stabilizing the tetrahedral intermediate, which donate their backbone amide protons to the substrate in the transition state during ester hydrolysis . It was also demonstrated that interactions with the Leu17 residue contributes to the oxyanion hole narrowing, promoting different behaviors on the BCL enantioselectivity and substrate accessibility to the enzyme catalytic site .…”

Section: Resultsmentioning

confidence: 76%

“…Furthermore, two amino acids (Leu17 and Gln88) close to the active site form the BCL oxyanion hole. These amino acids are responsible for stabilizing the tetrahedral intermediate, which through donate their backbone amide protons to the substrate in the transition state during ester hydrolysis . A detailed analysis through molecular dynamics simulations in different media (water, octane, and water/octane interface) was performed by Barbe et al The researchers investigate the movement of the BCL Lid Domain, showing that the Leu17 residue contributes to the oxyanion hole narrowing.…”

Section: Resultsmentioning

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: Resultsmentioning

confidence: 76%

Section: Resultsmentioning

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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“…There are numerous features that make lipases useful biocatalysts for industry such as (i) broad substrate spectrum, (ii) excellent chemo-, regio-and stereoselectivity, (iii) high stability towards harsh reaction conditions, (iv) independence of cofactors and, furthermore, (v) a wide variety of lipases is commercially available [26]. Due to all these advantages lipases are used in industry for the removal of fats and oils or for the production of NEFA, monoacylglycerols (MAG), and diacylglycerols (DAG) as raw material [27].…”

Section: Lipasesmentioning

confidence: 99%

Engineering and application of enzymes for lipid modification, an update

Zorn

Oroz‐Guinea

Brundiek³

et al. 2016

Progress in Lipid Research

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This review first provides a brief introduction into the most important tools and strategies for protein engineering (i.e. directed evolution and rational protein design combined with high-throughput screening methods) followed by examples from literature, in which enzymes have been optimized for biocatalytic applications. This covers engineered lipases with altered fatty acid chain length selectivity, fatty acid specificity and improved performance in esterification reactions. Furthermore, recent achievements reported for phospholipases, lipoxygenases, P450 monooxygenases, decarboxylating enzymes, fatty acid hydratases and the use of enzymes in cascade reactions are treated.

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“…Lipases (EC 3.1.1.3, triacylclycerol acylhydrolases) are interfacial enzymes while catalysing the hydrolysis of lipids, and can also catalyse the esterification and transesterification under some favourable environments (Casas‐Godoy et al . ). Lipases have been widely used in food industry, oleochemical industry, detergent industry and pharmaceutical industry and some other fields (Goswami et al .…”

Section: Introductionmentioning

confidence: 97%

“…), due to their substrate specificities, substrate varieties and catalytic activities in both conventional and nonconventional media (Casas‐Godoy et al . ). Unfortunately, there are very limited lipases available for industrial application, mostly ascribed to their high production cost.…”

Section: Introductionmentioning

confidence: 97%

Co-expression of lipase isozymes for enhanced expression in Pichia pastoris

Cai

Zhang

Zhao

et al. 2017

Lett Appl Microbiol

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The low production level is one of the limitation factors for decreasing the prices of enzymes and expanding their application in industry as the biocatalysts. This research focuses on developing lipase isozyme co-expression strategies in Pichia pastoris to enhance the expression level of overall lipase isozymes which catalyse the same reaction. The Kex2-mediated co-expression strategy of lipase isozymes could potentially enhance the overall isozyme expression, and isozyme co-expression might provide a new direction for improving the recombinant isozyme expression, and decreasing the production and application prices of these mixed enzymes as biocatalysts.

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Lipases: An Overview

Cited by 98 publications

References 151 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

Engineering and application of enzymes for lipid modification, an update

Co-expression of lipase isozymes for enhanced expression in Pichia pastoris

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