Lipase catalysis in organic solvents: advantages and applications

Kumar, Ashok; Dhar, Kartik; Kanwar, Shamsher S.; Arora, Pankaj

doi:10.1186/s12575-016-0033-2

Cited by 379 publications

(220 citation statements)

References 118 publications

(103 reference statements)

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“…It is known that lipase formulation modulate enzyme properties [10][11][12][13]. The results presented herein show that the lyophilization process has inhibited the lipase functionality, and the presence of Aquasorb hydrogel plays a moderate lyoprotective effect.…”

Section: Insights In Enzyme Researchmentioning

confidence: 78%

Water-Retaining Polymers in Organic Solvent Increase Lipase Activity for Biodiesel Synthesis

Ghisleri¹,

Fu²,

Secundo³

2018

Insights Enzyme Res

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Section: Insights In Enzyme Researchmentioning

confidence: 78%

Water-Retaining Polymers in Organic Solvent Increase Lipase Activity for Biodiesel Synthesis

Ghisleri¹,

Fu²,

Secundo³

2018

Insights Enzyme Res

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“…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 . Nevertheless, most organic solvents applied display important disadvantageous, such as high vapor pressure, flammability, and toxicity.…”

Section: Introductionmentioning

confidence: 99%

“…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.…”

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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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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“…By doing the enzymatic reactions in organic solvent media, there would not be any possibility of microbial contamination or unwanted water-related reactions. Furthermore, by using organic solvents, the solubility of water-insoluble substrates would be increased and the substrate specificity of a particular enzyme could be altered to a desirable substrate [181].…”

Section: Halophilic Enzymes -Potential Industrial Applicationsmentioning

confidence: 99%

Systematics of haloarchaea and biotechnological potential of their hydrolytic enzymes

et al. 2017

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Halophilic archaea, also referred to as haloarchaea, dominate hypersaline environments. To survive under such extreme conditions, haloarchaea and their enzymes have evolved to function optimally in environments with high salt concentrations and, sometimes, with extreme pH and temperatures. These features make haloarchaea attractive sources of a wide variety of biotechnological products, such as hydrolytic enzymes, with numerous potential applications in biotechnology. The unique trait of haloarchaeal enzymes, haloenzymes, to sustain activity under hypersaline conditions has extended the range of already-available biocatalysts and industrial processes in which high salt concentrations inhibit the activity of regular enzymes. In addition to their halostable properties, haloenzymes can also withstand other conditions such as extreme pH and temperature. In spite of these benefits, the industrial potential of these natural catalysts remains largely unexplored, with only a few characterized extracellular hydrolases. Because of the applied impact of haloarchaea and their specific ability to live in the presence of high salt concentrations, studies on their systematics have intensified in recent years, identifying many new genera and species. This review summarizes the current status of the haloarchaeal genera and species, and discusses the properties of haloenzymes and their potential industrial applications. SYSTEMATICS OF HALOPHILIC ARCHAEAHalophilic micro-organisms are found in the three domains of life, and are extremophiles living in hypersaline environments in the presence of salt (generally NaCl) as a specific requisite for their growth [1]. Hypersaline environments contain higher salt concentrations than seawater (3.5 % total dissolved salts) [2]. According to the optimum NaCl concentration for growth, micro-organisms fall into one of the following categories: extreme halophiles with optimum growth at 15-30 % (2.5-5.2 M) NaCl; moderate halophiles with optimum growth at 3-15 % (0.5-2.5 M) NaCl; slight halophiles with optimum growth at 1-3 % (0.2-0.5 M) NaCl; non-halophiles with optimum growth at less than 1 % (0.2 M) NaCl; and halotolerant micro-organisms which are non-halophiles showing the ability to tolerate high NaCl concentrations [3]. Halophiles can live in hypersaline environments because they are able to sustain osmotic balance. They use two main strategies to withstand the adverse consequences of water loss when exposed to high salt concentrations. The first strategy used by extremely halophilic archaea (haloarchaea) and halophilic anaerobic bacteria such as members of Halanaerobiales is known as the 'salt-in-cytoplasm' strategy, during which salts such as NaCl or KCl accumulate in the cytoplasm at concentrations similar to the extracellular ones [4,5]. Another mechanism to cope with high salt concentrations is the accumulation of organic molecules such as amino acids, sugars and polyols, known as compatible solutes or osmolytes. Compatible solutes are small and highly soluble molecules that can...

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Lipase catalysis in organic solvents: advantages and applications

Cited by 379 publications

References 118 publications

Water-Retaining Polymers in Organic Solvent Increase Lipase Activity for Biodiesel Synthesis

Water-Retaining Polymers in Organic Solvent Increase Lipase Activity for Biodiesel Synthesis

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

Systematics of haloarchaea and biotechnological potential of their hydrolytic enzymes

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