The effect of pH and NaCl concentration on adsorption of β-lactoglobulin at hydrophilic and hydrophobic silicon surfaces

Luey, J.; McGuire, Joseph; Sproull, Robert D.

doi:10.1016/0021-9797(91)90282-d

Cited by 62 publications

(36 citation statements)

References 25 publications

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“…This is consistent with the effects of pH on bLG adsorption on hydrophilic and hydrophobic silicon surfaces as studied by Luey et al (1991). They found that electrostatic forces play a major role in the adsorption of bLG on hydrophilic surfaces while nonelectrostatic interactions dominate on hydrophobic surfaces.…”

Section: Forces Responsible For Deposition and Permeationsupporting

confidence: 85%

Quantitative analysis of membrane fouling by protein mixtures using MALDI‐MS

Chan¹,

Chen²,

Bucknall³

2003

Biotech & Bioengineering

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Binary aqueous solutions of bovine serum albumin (BSA) and beta-lactoglobulin (bLG) were subject to flux-stepping and constant flux ultrafiltration to identify the apparent critical flux and to study the mechanisms and factors affecting fouling when the membrane is permeable to one protein component. Membranes from these filtration experiments were analyzed using matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS) to locate and quantify levels of fouling below and above the apparent critical flux. Hydrophilic (PLTK) regenerated cellulose and hydrophobic (PBTK) polysulfone asymmetric membranes were used, both of 30 kDa nominal molecular weight cut-off. For the hydrophilic PLTK membrane, protein deposition was shown to depend on electrostatic forces, exhibiting little or no fouling when the proteins had the same charge sign as that of the membrane. This was found to apply for both dilute equal mass-per-unit-volume and equimolar binary mixtures. For the PBTK membrane, hydrophobic protein-membrane attractive forces were sufficiently strong to cause deposition of bLG even in the presence of repulsive electrostatic forces. For the PBTK membrane deposition exceeded monolayer coverage below and above apparent critical flux conditions but for the PLTK membrane this generally occurred when the apparent critical flux was exceeded. MALDI-MS was shown to be a facile direct analytical technique for individually quantifying adsorbed proteins on membrane surfaces at levels as low as 50 fmol/mm(2). The high levels of compound specificity inherent to mass spectrometry make this approach especially suited to the quantification of individual components in mixed deposits. In this study, MALDI-MS was found to be successful in identifying and quantifying the protein species responsible for fouling.

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Section: Forces Responsible For Deposition and Permeationsupporting

confidence: 85%

Quantitative analysis of membrane fouling by protein mixtures using MALDI‐MS

Chan¹,

Chen²,

Bucknall³

2003

Biotech & Bioengineering

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“…Reduced electrostatic interactions can alter protein adsorption levels. For example, Luey et al (1991) reported that the adsorption of β-lactoglobulin (β-Lg) onto a hydrophilic silicon surface at pH 8.9…”

Section: Introductionmentioning

confidence: 99%

Effect of Sodium Chloride on the Adsorption of Proteins from Pink Shrimp (<i>Pandalus eous</i>) onto Stainless Steel Surfaces

Ratanasumawong

Hagiwara

Sakiyama

2015

FSTR

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Cross-contamination of protein deposits to other food products can cause serious issues in food plants, where several products might be processed using the same equipment. The key to preventing cross-contamination of foods is the thorough cleaning of work surfaces. To establish an optimum cleaning process for such equipment, understanding of the adhesion behavior of proteins on food-contact surfaces is important. This work aims to examine the effect of sodium chloride (NaCl) on the adsorption of shrimp proteins onto stainless steel surfaces.The presence of NaCl during extraction slightly increased the ratio of adsorbed total protein, while that of the protein tropomyosin, a major shrimp allergen, decreased. The addition of NaCl to the shrimp protein extract postextraction had no effect on the ratios of adsorbed total protein and tropomyosin. The addition of NaCl during extraction affected both the protein composition of the extract and the major type of protein adsorbed onto stainless steel surfaces.

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“…The ability of proteins to induce film formation depends on a number of parameters of molecular nature which have been studied into detail in the past and is collectively governed by a net energy gain from absorbing at an interface. Milk proteins have been identified as good foaming agents as a result of their aggregation state, molecular stability and flexibility, electrostatics, and (surface) exposed hydrophobicity (Hunter et al, 1991;Luey et al, 1991;Shirahama et al, 1990;Suttiprasit et al, 1992;Waniska & Kinsella, 1985). Chemical modifications have been employed in the past to improve surface activity of less performing proteins.…”

Section: Surface Properties: Emulsions and Foamsmentioning

confidence: 99%