Dancing with oils – the interaction of lipases with different oil/water interfaces

Filipe, Hugo A. L.; Almeida, Maëva C F; Teixeira, Rafaela R; Esteves, Margarida I M; Henriques, César A.; Antunes, Filipe E.

doi:10.1039/d1sm00590a

Cited by 9 publications

(14 citation statements)

References 70 publications

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“…Vodopivec et al employed CGMD simulations to study nanostructures of oil droplets in seawater stabilized by the two fungal hydrophobins EAS and HFBII. Filipe et al . conducted CGMD simulations to characterize the orientation of CALB at the triglyceride–water interface, confirming that CALB favorably interacts with the oil–water interface in a manner that protein binding sites are more available for triglyceride molecules.…”

Section: Introductionmentioning

confidence: 92%

“…Vodopivec et al 34 employed CGMD simulations to study nanostructures of oil droplets in seawater stabilized by the two fungal hydrophobins EAS and HFBII. Filipe et al 35 conducted CGMD simulations to characterize the orientation of CALB at the triglyceride− water interface, confirming that CALB favorably interacts with the oil−water interface in a manner that protein binding sites are more available for triglyceride molecules. The specific interaction pattern between CALB and triglyceride is a mandatory requirement for the interfacial activity of CALB, driving the development of protein engineering, by which better enzymatic performance can be envisioned.…”

Section: Introductionmentioning

confidence: 94%

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Effect of Oil Polarity on the Protein Adsorption at Oil–Water Interfaces

Qin

Jian

2023

Langmuir

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Protein adsorption at oil–water interfaces has received much attention in applications of food emulsion and biocatalysis. The protein activity is influenced by the protein orientation and conformation. The oil polarity is expected to influence the orientation and conformation of adsorbed proteins by modulating intermolecular interactions. Hence, it is possible to tune the protein emulsion stability and activity by varying the oil polarity. Martini v3.0-based coarse-grained molecular dynamics (CGMD) simulations were employed to investigate the effect of oil polarity on the orientation and conformation of hydrophobin (HFBI) and Candida antarctica lipase B (CALB) adsorbed at triolein–water, hexadecane–water, and octanol–water interfaces for the first time. The protein adsorption orientation was predicted through the hydrophobic dipole, indicating that protein adsorption exists in preferred orientations at hydrophobic oil interfaces. The conformation of the adsorbed HFBI is well conserved, whereas relatively larger conformational changes occur during the CALB adsorption as the oil hydrophobicity increases. Comparisons on the adsorption interaction energy of proteins with oils confirm the relationship between the oil polarity and the interaction strength of proteins with oils. In addition, CGMD simulations allow longer time scale simulations of the behaviors of protein adsorption at oil–water interfaces.

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Section: Introductionmentioning

confidence: 92%

Section: Introductionmentioning

confidence: 94%

Effect of Oil Polarity on the Protein Adsorption at Oil–Water Interfaces

Qin

Jian

2023

Langmuir

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“…After the two-phase system was built, 2T was added and then a simulation was run. The simulated sunflower oil phase was composed of 30 triolein molecules, 65 trilinolein molecules, and 5 tripalmitin molecules, 51 and the water layer was composed of 10234 water molecules and 0.3 mol/L NaCl. The cell size was adjusted manually to make sure that the density of the system was between 0.9 and 1 g/ cm 3 .…”

Section: Adsorption Process Of 2t At the Oil And Water Interfacementioning

confidence: 99%

Two-Dimensional Triblock Peptide Assemblies for the Stabilization of Pickering Emulsions with pH Responsiveness

Calicchia

Jurewicz

Muñoz

et al. 2022

ACS Appl. Mater. Interfaces

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A variety of two-dimensional (2D) nanomaterials, including graphene oxide and clays, are known to stabilize Pickering emulsions to fabricate structures for functions in sensors, catalysts, and encapsulation. We introduce here a novel Pickering emulsion using self-assembled amphiphilic triblock oligoglycine as the emulsifier. Peptide amphiphiles are more responsive to environmental changes (e.g., pH, temperature, and ionic strength) than inorganic 2D materials, which have a chemically rigid, in-plane structure. Noncovalent forces between the peptide molecules change with the environment, thereby imparting responsiveness. We provide new evidence that the biantennary oligoglycine, Gly 4 − NH−C 10 H 20 −NH−Gly 4 , self-assembles into 2D platelet structures, denoted as tectomers, in solution at a neutral buffered pH using small-angle X-ray scattering and molecular dynamics simulations. The molecules are stacked in the platelets with a linear conformation, rather than in a U-shape. We discovered that the lamellar oligoglycine platelets adsorbed at an oil/water interface and stabilized oil-in-water emulsions. This is the first report of 2D oligoglycine platelets being used as a Pickering stabilizer. The emulsions showed a strong pH response in an acidic environment. Thus, upon reducing the pH, the protonation of the terminal amino groups of the oligoglycine induced disassembly of the lamellar structure due to repulsive electrostatic forces, leading to emulsion destabilization. To demonstrate the application of the material, we show that a model active ingredient, β-carotene, in the oil is released upon decreasing the pH. Interestingly, in pH 9 buffer, the morphology of the oil droplets evolved over time, as the oligoglycine stabilizer created progressively a thicker interfacial layer. This demonstration opens a new route to use self-assembled synthetic peptide amphiphiles to stabilize Pickering emulsions, which can be significant for biomedical and pharmaceutical applications.

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“…In industrial and biological processes such as pharmaceutical manufacturing and food formulations, these lipids are often in direct contact with an aqueous environment. While there have been significant advances in the understanding of the changes in the self-assembled, liquid crystalline phase structure during the lipolysis of emulsified lipid assemblies (Borné et al, 2002a;Borné et al, 2002b;Caboi et al, 2002;Salentinig et al, 2010;Salentinig et al, 2011;Warren et al, 2011;Khay Fong et al, 2014;Wadsäter et al, 2014;Salentinig et al, 2015a;Barauskas et al, 2016;Filipe et al, 2021), the structural nature of the oil/water interface, and how it changes during lipolysis has received relatively little attention. Consequently, studying model-thin lipid films upon exposure to an aqueous environment is of fundamental importance as it allows biological processes, such as the action of lipases, to be better understood.…”

Section: Introductionmentioning

confidence: 99%

“…Lipases including Thermomyces lanuginosus, Rhizopus delemar, Candida rugosa, Rhizomucur miehei, and Candida antarctica A and B have gained significant industrial interest as biocatalysts (Schmid and Verger, 1998;Fernandez-Lafuente, 2010;Filipe et al, 2021;Moses et al, 2021). Not only do lipases catalyze the hydrolysis of triglycerides, a process that is extremely useful in detergents, but the reaction products such as free fatty acids (or fatty acid salts), partial glycerides and glycerol are essential for the food and cosmetics industry (Intarakumhaeng et al, 2018).…”

Section: Introductionmentioning

confidence: 99%

The Influence of pH on the Lipase Digestion of Nanosized Triolein, Diolein and Monoolein Films

Humphreys

Campos‐Terán

Arnold

et al. 2022

Front. Soft. Matter

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Herein we studied the processes at the liquid aqueous interface at pH 7 and 8.5 during Thermomyces lanuginosus lipase-catalyzed hydrolysis of nanosized tri-, di- and mono-olein films deposited on a planar substrate. By employing a combination of ellipsometry, QCM-D and ATR-FTIR, we were able to reveal the physical properties of the thin films at high time resolution throughout the initial hydration and subsequent digestion, as well as the main chemical species present before and after lipolysis. The ATR-FTIR results showed that the degree of digestion and protonated state of the oleic acid produced in the reaction are highly dependent on the pH of the aqueous solvent. Furthermore, the ellipsometry and QCM-D results reveal that the duration of the lag phase observed before lipolysis was detected and the magnitude and type of changes to the physical properties of the thin films throughout digestion was influenced by whether the initial substrate consisted of tri-, di- or mono-olein.

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Dancing with oils – the interaction of lipases with different oil/water interfaces

Abstract: The use of enzymes as biocatalysts in industrial applications has received much attention during the last years. Lipases are widely employed in the food and cosmetic industry, for the synthesis...

Cited by 9 publications

References 70 publications

Effect of Oil Polarity on the Protein Adsorption at Oil–Water Interfaces

Effect of Oil Polarity on the Protein Adsorption at Oil–Water Interfaces

Two-Dimensional Triblock Peptide Assemblies for the Stabilization of Pickering Emulsions with pH Responsiveness

The Influence of pH on the Lipase Digestion of Nanosized Triolein, Diolein and Monoolein Films

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