Chapter 14. Adsorption Experiments from Mixed Protein + Surfactant Solutions

Alahverdjieva, V.S.; Grigoriev, D. O.; Ferri, James K.; Fainerman, V. B.; Aksenenko, E. V.; Leser, Martin E.; Michel, Martin; Miller, R.

doi:10.1039/9781847557698-00209

Cited by 8 publications

(27 citation statements)

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“…A possible solution to this problem is connected with the interfacial adsorption of HEWL while promoting important conformational changes 43 and ultimately protein denaturation. 41 Because of their larger interfacial area per unit of volume, smaller crystallization drops also have higher fractions of adsorbed macromolecules undergoing structural rearrangements that compromise, sometimes irreversibly, the native biological function. We propose that the loss of catalytic activity of soluble HEWL is accompanied by a gain of thermodynamic activity as manifested by the peculiar evolution of the dissolution rates.…”

Section: ■ Discussionmentioning

confidence: 99%

“…In such cases, a great amount of soluble protein is adsorbed at the liquid interface thus decreasing the bulk concentration in the equivalent amount. 16,40,41 In vapor diffusion experiments, drop evaporation additionally increases the concentration of protein at the interfaces, where high local supersaturation levels tend to originate new nucleation events. 42 Taken alone, the differences between interfacial and bulk conditions cannot explain why crystals positioned in a fixed point of the drop neither dissolve nor grow when subjected to temperatures between 37 and 10 °C.…”

Section: Discussionmentioning

confidence: 99%

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The Finding of Nondissolving Lysozyme Crystals and Its Significance for the Study of Hard-to-Crystallize Biological Macromolecules

Ferreira

Rocha

Damas

et al. 2016

Crystal Growth & Design

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Major discoveries in structural biology depend on obtaining well-diffracting macromolecular crystals. This necessity has motivated many fundamental studies on protein crystallization using lysozyme as a model system. In the present contribution, we report the unprecedented observation of lysozyme crystals that stop dissolving under undersaturated conditions imposed to sub-microliter crystallization drops at mild temperatures. Subsequent growth of the same crystals is apparently undisturbed after the drops are cooled below the saturation temperature. The succession of heating/cooling cycles only partially recovers crystal dissolution while crystal growth becomes gradually slower. Ultimately, increasing and decreasing the temperature between 10 and 37 °C has no visible effect on the size of the crystals. We ascribe this phenomenon to the partial denaturation of the soluble protein in the drop as evidenced by the decreasing glycoside hydrolase activity of lysozyme over the incubation time. The disturbances in the phase transition processes are explained as the result of the changed chemical potential due to different folding states. In a time when the high-hanging fruits in structural biology have to be picked, the present findings call attention to interfacial phenomena as an important, though often imperceptible, aspect that affects protein stability and justifies further optimization of current crystallization methods.

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Section: ■ Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

The Finding of Nondissolving Lysozyme Crystals and Its Significance for the Study of Hard-to-Crystallize Biological Macromolecules

Ferreira

Rocha

Damas

et al. 2016

Crystal Growth & Design

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“…[50] Enzyme activity can be affected by such conformational flexibility to induce changes in their secondary protein structure or even, partial unfolding, if not complete denaturation. [51] Another reason for reduced accessibility of substrate to printed lysozyme could be high proteinprotein interaction after immobilization on fiber surface. [52] In case of the second route, higher activity could be expected, as it is less prone to immobilization effects.…”

Section: Activity Of Printed Enzymementioning

confidence: 99%

“…As discussed earlier, such high reduction of activity might have been caused by various immobilization phenomena subjected on the enzyme, for example, change of protein structure, shape and conformation, along with possible partial unfolding. [49][50][51] To recover the active state, enzymes would need to rearrange their structure upon desorption, [59] thus, activity of desorption-based system would be difficult to improve further. Conversely, less compromised activity can be expected from a surface retaining most enzymes even after desorption or washing process due to improved protein adsorption stability achieved through an appropriate physical and/or chemical surface modification.…”

Section: Adsorption Stabilitymentioning

confidence: 99%

Effective Pretreatment Routes of Polyethylene Terephthalate Fabric for Digital Inkjet Printing of Enzyme

Biswas

Nierstrasz

2021

Adv Materials Inter

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A major number of studies used enzymes during pre-processing in the form of beads, pellets, otherwise during post-processing, for example, surface cleaning and effluent treatment. [2,3] A few studies used flat film and paper like supports, however, use of non-flat textile like surfaces for immobilization is very limited. [4] Textile fabrics can be a more suitable support for enzyme immobilization due to their inherent advantages of being strong, flexible, and lightweight, along with providing low pressure drop in chemical processes. Thus, they show potential to be used in a range of advanced applications, for example, controlled release, drug delivery, bacterial inhibition, and biosensing. [5] Such advanced application often requires highly controlled, precise, contactless, and customizable production method such as digital inkjet printing. [6] Compared to conventional production methods, for example, coating, finishing and screen printing, resource efficient inkjet technology minimizes use of water, energy, chemical and wastes of valuable functional materials, for example, enzymes. [7] Drop-on-demand (DOD) inkjet technology has been successfully used for printing of enzymes on textiles for various applications, compared to the continuous system. [8] Among two ejection mechanisms of DOD printheads, that is, thermal and piezoelectric, the latter one is preferred due to less possible influence on the protein structure of enzymes and resulting activity. [9,10] Along with printhead mechanics, inkjet printing of enzyme on textiles comes with challenges on ink recipe optimization for a specific enzyme-printhead combination and ensuring proper fabric-enzyme interaction. [11] Optimization strategy of ink-containing enzyme for rheological, ionic, and printhead parameters has been demonstrated in our previous work. [12] In this work, fabric surface characteristics necessary for efficient inkjet printing and retention of active enzymes are studied. Polyethylene terephthalate (PET) fiber based synthetic products are being used in applications ranging from apparel and home furnishing to medical textiles with rising market trend for more advanced applications. [13] This inert fiber offers superior physiochemical and mechanical properties. Nevertheless, such fibers retain challenges for printing because of their hydrophobic surface caused by lack of polar groups. Additionally, synthetic fiber surfaces may induce greater hydrophobic interaction with enzymes, for example, lysozyme to cause confirmation changes and denaturation. [14] Due to this fact, studies regarding immobilization of this enzyme on synthetic fiber Enzymes immobilized on synthetic polyethylene terephthalate (PET) textile surface by resource-efficient inkjet printing technology can promote developments for various novel applications. Synthetic fabrics often require adequate pretreatments to facilitate such printing process. This work discusses PETwoven fabric pretreatment routes to improve wettability by alkaline, enzymatic, and plasma processes for effective pri...

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“…This model assumes that protein molecules can exist in a number of states of different molar areas, varying from a maximum value (ω max ) at a very low surface coverage (low surface pressure) to a minimum value (ω min ) at a very high surface coverage. 16,[27][28][29][30] The molar areas of two "neighboring" conformations differ from each other by the molar area increment ω 0 , chosen to be equal to the molar area of the solvent.…”

Section: ' Introductionmentioning

confidence: 99%

Liquid Scintillation Spectrometry of Tritium in Studying Lysozyme Behavior in Aqueous/Organic Liquid Systems. The Influence of the Organic Phase

Chernysheva

Badun

2011

Langmuir

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Liquid scintillation spectrometry of tritium in the application of the scintillation phase method was used for studying the adsorption of lysozyme at the liquid/liquid interface and its distribution in the bulk of the system. The goal of this research was to reveal the influence of the nature of the organic phase on the distribution and adsorption ability of the protein when it is placed in a system containing two immiscible liquids. Based on the radiochemical assay distribution coefficients and adsorption isotherms obtained for aqueous/octane, aqueous/p-xylene and aqueous/octanol systems, it was concluded that the interaction of the protein with the interface plays a dominant role in protein behavior in aqueous/organic liquid systems.

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Chapter 14. Adsorption Experiments from Mixed Protein + Surfactant Solutions

Cited by 8 publications

References 0 publications

The Finding of Nondissolving Lysozyme Crystals and Its Significance for the Study of Hard-to-Crystallize Biological Macromolecules

The Finding of Nondissolving Lysozyme Crystals and Its Significance for the Study of Hard-to-Crystallize Biological Macromolecules

Effective Pretreatment Routes of Polyethylene Terephthalate Fabric for Digital Inkjet Printing of Enzyme

Liquid Scintillation Spectrometry of Tritium in Studying Lysozyme Behavior in Aqueous/Organic Liquid Systems. The Influence of the Organic Phase

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