Ellipsometric Study of Bovine Serum Albumin Adsorbed onto Ti/TiO2 Electrodes

Giacomelli, Carla E.; Esplandiu, M.J.; Ortiz, Patrícia I.; Avena, Marcelo Javier; Pauli, Carlos P. De

doi:10.1006/jcis.1999.6434

Cited by 77 publications

(63 citation statements)

References 50 publications

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“…43,44 Figure 10 illustrates the variation of BSA flux and rejection with pH for a feed concentration of 0.5 g L −1 at 207 kPa. It is observed from Fig.…”

Section: Effect Of Ph On Bsa Separationmentioning

confidence: 99%

“…The BSA molecule binds parallel to the membrane by a flat configuration similar to side-on orientation and the rejection depends on the sieving mechanism as well as the electrostatic attraction between BSA and membrane. 43,48 Effect of pressure on BSA separation Figure 11 shows the flux and retention behavior of BSA with applied pressure. The flux and rejection of BSA increase when the applied pressure increases.…”

Section: Effect Of Ph On Bsa Separationmentioning

confidence: 99%

“…In particular, the repulsive interactions could obstruct the transmission of protein through the pores, and consequently higher rejection is observed at pH 3. 16,43 At pH 3, BSA is in the expanded form, due to the conformational changes of the BSA molecule attached perpendicular to the γ -Al 2 O 3 membrane surface by weak end-on orientation, which reduces the transmission of BSA and leads to higher rejection. The uncharged BSA showed a 47% rejection at pH 4.9 indicating that sieving is expected to outweigh electrostatic interaction.…”

Section: Effect Of Ph On Bsa Separationmentioning

confidence: 99%

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Separation of bovine serum albumin (BSA) using γ‐Al₂O₃–clay composite ultrafiltration membrane

Monash

Majhi

Pugazhenthi

2009

J of Chemical Tech & Biotech

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BACKGROUND: Ceramic membranes have received more attention than polymeric membranes for the separation and purification of bio-products owing to their superior chemical, mechanical and thermal properties. Commercially available ceramic membranes are too expensive. This could be overcome by fabricating membranes using low-cost raw materials. The aim of this work is to fabricate a low-cost γ -Al 2 O 3 -clay composite membrane and evaluate its potential for the separation of bovine serum albumin (BSA) as a function of pH, feed concentration and applied pressure. To achieve this, the membrane support is prepared using low-cost clay mixtures instead of very expensive alumina, zirconia and titania materials. The cost of the membrane can be further reduced by preparing a γ -alumina surface layer on the clay support using boehmite sol synthesized from inexpensive aluminium chloride instead of expensive aluminium alkoxide using a dip-coating technique.

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“…43,44 Figure 10 illustrates the variation of BSA flux and rejection with pH for a feed concentration of 0.5 g L −1 at 207 kPa. It is observed from Fig.…”

Section: Effect Of Ph On Bsa Separationmentioning

confidence: 99%

Section: Effect Of Ph On Bsa Separationmentioning

confidence: 99%

Section: Effect Of Ph On Bsa Separationmentioning

confidence: 99%

See 1 more Smart Citation

Separation of bovine serum albumin (BSA) using γ‐Al₂O₃–clay composite ultrafiltration membrane

Monash

Majhi

Pugazhenthi

2009

J of Chemical Tech & Biotech

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“…These interactions are often mediated via weak associations, including ionic forces and hydrogen bonds, resulting in unstable, highly reversible protein adsorption to TiO 2 (e.g., albumin: do Serro et al, 1999;Oliva et al, 2003). In some cases, stronger hydrophobic interactions are involved (Giacomelli et al, 1999;MacDonald et al, 2002). Often, the interaction of certain proteins leads to undesirable effects (www.interscience.wiley.com) DOI:10.1002/jmr.919 Research Article such as inflammatory (Hu et al, 2001;Keselowsky et al, 2007) or thrombogenic (Thor et al, 2007) phenomena which should be reduced.…”

Section: Introductionmentioning

confidence: 99%

The titanium binding protein of Rhodococcus ruber GIN1 (NCIMB 40340) is a cell‐surface homolog of the cytosolic enzyme dihydrolipoamide dehydrogenase

Siegmann

Komarska

Betzalel

et al. 2008

J of Molecular Recognition

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Rhodococcus ruber GIN1 (formally Rh. strain GIN1) was previously isolated on the basis of its strong adherence to coal fly ash (CFA) and titanium dioxide particles from CFA sedimentation ponds of an electrical power plant in Israel. The interaction of the bacterium with oxides has been shown to be mediated by a cell surface protein designated TiBP (titanium binding protein) involving primarily strong, non-electrostatic forces. In this work, we set forward to identify this unique exocellular protein. Sequence analysis of the purified protein by mass spectrometry (LC/MS/MS) following trypsinization revealed 11 peptides. All of them showed >90% amino acid residues identity with sequences of one of the orthologs (dldh1) of the cytosolic enzyme dihydrolipoamide dehydrogenase (DLDH), based on the genome sequence of Rhodococcus strain RHA1. This genome was selected as a reference since currently it is the only sequenced Rhodococcal genome. Altogether, these peptides covered over 25% of the 52 kDa protein molecule. N- and C-termini primers were prepared and used to sequence the paralog gene from Rh. ruber GIN1 after polymerase chain reaction (PCR) amplification. All 11 peptides showed 100% identity with the sequence of this gene. The homology of TiBP with the supposedly cytosolic DLDH raised the question of whether the exocellular TiBP possesses DLDH activity. Indeed, intact late logarithmic phase Rh. ruber GIN1 cells, previously shown to express TiBP, were found to possess such activity, while very low activity was associated with stationary phase cells which possess diminished TiBP expression on their surface. Further evidence for the exocellular location of TiBP/DLDH was achieved using specific anti-TiBP polyclonal antibodies by whole cell and protein enzyme-linked immunosorbent assay (ELISA), showing high reactivity of the logarithmic phase cell surface and substantially lower reactivity with the stationary phase cells. As expected, logarithmic phase spheroplasts were not recognized by these antibodies. Similar results were obtained by fluorescence and scanning electron microscopy. Our postulation that DLDH is located on the surface of Rh. ruber GIN1, serving as a TiO2 binding protein, is in accordance with literary evidence on DLDH in other organisms, Bacteria, Archea, and Eukaryots that suggests it is associated with the outer membranes or cell surfaces. As an exocellular protein DLDH assumes various tasks which are not related to its classical role as a 2-oxoacid dehydrogenase, including serving as an adhesion/binding protein in certain bacteria.

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“…Proteins behavior is influ-(AFM) [6,12,16] have been developed to monitor conformational changes, adsorption amounts, thickness, and surface morphology of adsorbed protein, respectively. The measurement of adsorption kinetics and equilibrium adsorption isotherms of proteins can be accomplished by these techniques, and possible adsorption orientations may be thereby inferred; however, the results of these techniques provide neither direct confirmation of the preferred orientation of adsorbed protein nor molecular-level details of protein adsorption.…”

Section: Introductionmentioning

confidence: 99%

Preferred orientation of albumin adsorption on a hydrophilic surface from molecular simulation

Hsu¹,

Sheu²,

Tsay³

2008

Colloids and Surfaces B: Biointerfaces

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Ellipsometric Study of Bovine Serum Albumin Adsorbed onto Ti/TiO2 Electrodes

Cited by 77 publications

References 50 publications

Separation of bovine serum albumin (BSA) using γ‐Al₂O₃–clay composite ultrafiltration membrane

Separation of bovine serum albumin (BSA) using γ‐Al₂O₃–clay composite ultrafiltration membrane

The titanium binding protein of Rhodococcus ruber GIN1 (NCIMB 40340) is a cell‐surface homolog of the cytosolic enzyme dihydrolipoamide dehydrogenase

Preferred orientation of albumin adsorption on a hydrophilic surface from molecular simulation

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Ellipsometric Study of Bovine Serum Albumin Adsorbed onto Ti/TiO2 Electrodes

Cited by 77 publications

References 50 publications

Separation of bovine serum albumin (BSA) using γ‐Al2O3–clay composite ultrafiltration membrane

Separation of bovine serum albumin (BSA) using γ‐Al2O3–clay composite ultrafiltration membrane

The titanium binding protein of Rhodococcus ruber GIN1 (NCIMB 40340) is a cell‐surface homolog of the cytosolic enzyme dihydrolipoamide dehydrogenase

Preferred orientation of albumin adsorption on a hydrophilic surface from molecular simulation

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Product

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About

Separation of bovine serum albumin (BSA) using γ‐Al₂O₃–clay composite ultrafiltration membrane

Separation of bovine serum albumin (BSA) using γ‐Al₂O₃–clay composite ultrafiltration membrane