Zeta potential measurement as a diagnostic tool in enzyme immobilisation

Schultz, Nadja; Metreveli, George; Franzreb, Matthias; Frimmel, Fritz H.; Syldatk, Christoph

doi:10.1016/j.colsurfb.2008.05.004

Cited by 77 publications

(39 citation statements)

References 18 publications

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“…When the potential is low, attraction exceeds repulsion and the particles tend to aggregate. So, particles with high zeta potential (negative or positive) are electrically stabilized while particles with low zeta potentials tend to coagulate or flocculate as outlined in Table 1 [8,9].…”

Section: Introductionmentioning

confidence: 99%

Bioactive glass nanoparticles with negative zeta potential

Doostmohammadi

Monshi

Salehi

et al. 2011

Ceramics International

159

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Section: Introductionmentioning

confidence: 99%

Bioactive glass nanoparticles with negative zeta potential

Doostmohammadi

Monshi

Salehi

et al. 2011

Ceramics International

159

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“…as well as the type of method or buffer used (Michen and Graule 2010) and the temperature of determination. For example, Schultz et al (2008) measured IEPs of 4 and 7.5 for Candida antarctica A-type lipase using, respectively, electrophoretic mobility and isoelectric focusing techniques. Righetti and Caravaggio reported in 1976 that the IEP of a protein might differ by up to 0.5 pH unit when determined at 25 and 4°C, the value increasing as the temperature decreases.…”

Section: Isoelectric Point and Zeta Potentialmentioning

confidence: 99%

Zeta Potential and Aggregation of Virus-Like Particle of Human Norovirus and Feline Calicivirus Under Different Physicochemical Conditions

2015

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Although the spread of human norovirus reportedly depends on its ability to bind to food materials, the mechanism of the phenomenon remains unknown. Since protein size and electrical charge are reportedly important parameters in their adsorption, the current work is focused on determining human noroviruses isoelectric point (IEP), electrical charge and aggregate size at different pH, ionic strength (IS), and temperature. Using the baculovirus expression vector system, we produced and purified virus-like particles (VLPs) of GI.1 and GII.4 noroviruses and feline calicivirus, determined their IEP, and examined their size and electrical charge using a Zetasizer Nano ZS apparatus. Shape and size were also visualized using transmission electron microscopy. IEPs were found close to pH 4. Net charge increased as the pH deviated from the IEP. VLPs were negatively charged at all IS tested and showed a gradual decrease in charge with increasing IS. At low temperature, VLPs were 20-45 nm in diameter at pH far from their IEP and under almost all IS conditions, while aggregates appeared at or near the IEP. At increased temperatures, aggregates appeared at or near the IEP and at high IS. Aggregation at the IEP was also confirmed by microscopy. This suggests that electrostatic interactions would be the predominant factor in VLPs adhesion at pH far from 4 and at low ionic strength. In contrast, non-electrostatic interactions would prevail at around pH 4 and would be reinforced by aggregates, since size generally favors multiple bonding with sorbents.

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“…Previous studies demonstrated that these techniques were suitable for protein characterization [26,27]. In order to analyse the particle size in pectinase solution in the conditions in which membrane was fouled with pectinase (at 25 °C) and during cleaning treatment (at 50 °C in presence of NaCl), different analysis were carried out by DLS varying protein concentration (2, 7, 15 g/L).…”

Section: Characterization Of the Enzymatic Solutionsmentioning

confidence: 99%

Destabilization and removal of immobilized enzymes adsorbed onto polyethersulfone ultrafiltration membranes by salt solutions

Corbatón-Báguena

Gugliuzza

Cassano

et al. 2015

Journal of Membrane Science

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ElsevierCorbatón Báguena, MJ.; Cassano, A.; Giorno, L. (2015). Destabilization AbstractIn this work the effectiveness of two saline solutions (NaCl and Na 2 SO 4 ) to clean a permanently hydrophilic polyethersulfone (PESH) ultrafiltration (UF) membrane with a molecular weight cut-off (MWCO) of 30 kDa previously fouled with enzymatic solutions 2 was investigated. The influence of protein concentration in the enzymatic solution during the fouling step and the effect of salt type during the cleaning procedure were studied.The protein aggregation was analysed in solution and onto the membrane surface by using several techniques including Dynamic Light Scattering (DLS), Atomic Force Microscopy (AFM) and Infrared Spectroscopy with Attenuated Total Reflectance (ATR-FTIR). In addition, mechanisms that dominate membrane fouling were studied by fitting some mathematical models (Hermia's models adapted to crossflow filtration, a combined model based on the complete blocking and cake formation equations and a resistance-in-series model) to the experimental data.Fouling results showed that the complete blocking/adsorption on membrane surface was the predominant fouling mechanism. Regarding the cleaning results, higher cleaning efficiency and low residual protein concentration was obtained with NaCl solutions for all the feed solutions tested due to the favourable interaction between Cl -and proteins.

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Zeta potential measurement as a diagnostic tool in enzyme immobilisation

Cited by 77 publications

References 18 publications

Bioactive glass nanoparticles with negative zeta potential

Bioactive glass nanoparticles with negative zeta potential

Zeta Potential and Aggregation of Virus-Like Particle of Human Norovirus and Feline Calicivirus Under Different Physicochemical Conditions

Destabilization and removal of immobilized enzymes adsorbed onto polyethersulfone ultrafiltration membranes by salt solutions

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