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Biomedical subjects

W Norde

Publications and source records attributed to W Norde.

31 records · Page 2Linked to original sources
PubMed1995

Inactivation of a subtilisin in colloidal systems.

The aim of the present study is to establish the relation between the inactivation of the proteolytic enzyme Savinase and its adsorption at different types of solid-liquid interfaces. The loss of activity has been determined both in solution and in the presence of colloidal particles, which provide a surface area for adsorption of 25% of the enzyme population. Analysis of the remaining solution at different periods of incubation of the various systems shows that the intact protein is converted into autolytic degradation products at the expense of biological activity. The different particles, however, deactivate the enzymes to a different extent. Under the experimental conditions the half-life of the enzymatic activity in solution is 3.5 hours. In the presence of particles that have hydrophobic surface properties (teflon- or polystyrene latex) the half-life is reduced to 0.7 hours. On the contrary, hydrophilic silica particles stabilize the enzyme against autolysis as compared to the inactivation in solution. Polystyrene latex particles which are chemically grafted with short poly(ethylene oxide) chains ([EO]8) are, for steric reasons, also mild with respect to the reduction of enzymatic stability. It is thus concluded that the type of surface determines the mode in which the enzyme is adsorbed on a particle which, in turn, affects the autocatalytic rate.

Adsorption↗
PubMed1995

Influence of fluoride applications on some physicochemical surface properties of synthetic hydroxyapatite and human dental enamel and its consequences for protein adsorption.

Synthetic hydroxyapatite and human dental enamel (polished and non-polished) were subjected to various fluoride applications, i.e., using solutions of sodium fluoride (NaF), acidulated phosphate fluoride (APF), and stannous fluoride (SnF2). Treatment with APF has a strong influence on the morphology of the apatite. All fluorides, in particular SnF2, make the enamel surfaces more hydrophobic. NaF and APF applications slightly alter the electrokinetic potentials of the surfaces, but SnF2 renders them much more negatively charged. The adsorption of the proteins lysozyme and alpha-lactalbumin on these surfaces can be explained in terms of electrostatic and hydrophobic interactions between the proteins and the sorbent surfaces.

Acidulated Phosphate Fluoride↗
PubMed1991

Interfacial thermodynamics of protein adsorption and ion co-adsorption. III. Electrochemistry of bovine serum albumin adsorption on silver iodide.

An experimental analysis of charge regulation in protein adsorption is presented. The model system consists of colloidal particles of the slightly water soluble salt silver iodide as the adsorbent and the protein bovine serum albumin as the adsorbate. Protein adsorption experiments corroborate earlier findings that albumin adsorbs maximally close to the isoelectric point of the protein. The adsorption is reversible with respect to protein-protein exchange. The charge regulation is studied by novel potentiometric titrations. The Galvani potential of the adsorbent, partially covered with protein, is varied by the addition of AgNO3/KI while the pH is kept constant by means of a pH-stat. It is shown that the ion co-adsorption is a linear decreasing function of the blank surface charge density. The results are consistent with thermodynamics: for the first time a few phenomenological linkage relations between the ion co-adsorptions and chemical potentials are verified experimentally. The charge regulation is interpreted in terms of a contact layer model, which explains the ion co-adsorption by compounded ion exchange equilibria in the small layer of atomic contact between adsorbed protein and surface.

Adsorption↗
PubMed1990

Influence of interfaces on microbial activity.

Bacterial adhesion in natural and artificial systems has been critically reviewed to investigate the influences exerted by the presence of interfaces. Numerous investigations have demonstrated that, in the presence of a solid phase, the activity of bacterial cultures is changed. Reviewing relevant literature, two problems were encountered. One is of an experimental nature. Due to lack of similarity in experimental conditions, disparate experiments often cannot be compared; their results may even appear conflicting. The other problem is of an interpretational nature: several hypothetical theories exist which try to explain the effect of surfaces on microbial activity. These theories often confuse changes in the medium and limitations in mass transfer which are due to the presence of solid surfaces (indirect influences) with changes in cell properties (direct influences). Whenever a surface is reported to influence the metabolism of bacteria, the action is found almost exclusively to be due to changes in the medium or environment and is therefore indirect. Based on data reported in the literature, and by using thermodynamic and kinetic considerations, it is concluded that so far neither experimental nor theoretical evidence exists for a direct influence of interfaces on microbial activity.

Bacteria↗
PubMed1990

Physical chemical description of bacterial adhesion.

For the description of general bacterial adhesion phenomena two different physicochemical approaches are available. The first one, based on a surface Gibbs energy balance, assumes intimate contact between the interacting surfaces. According to this approach adhesion is solely related to the Gibbs energies of the surfaces involved. The second approach, based on colloid chemical theories (DLVO theory), allows for two types of adhesion: 1. secondary minimum adhesion, which is often weak and reversible, and 2. irreversible primary minimum adhesion. In the first case a thin water film is present between the interacting surfaces. In the DLVO approach adhesion is determined by long range interactions, i.e., Van der Waals and electrostatic interactions. Van der Waals interactions may be related to the hydrophobicity of the cell wall. For the measurement of bacterial hydrophobicity and electrokinetic potential several macroscopic methods are available. Based on a literature review of the influence of both surface characteristics on adhesion, it is concluded that the surface Gibbs energy balance approach is not adequate to describe the majority of adhesion phenomena. On the other hand the DLVO-theory describes the observations fairly well, especially in the case of reversible (secondary minimum) adhesion. The influence of adsorbing (in)organic compounds, extracellular polymers and cell surface appendages on adhesion can also be predicted by a DLVO-type approach.

Bacterial Adhesion↗
PubMed1987

The role of bacterial cell wall hydrophobicity in adhesion.

In this study, the adhesion of bacteria differing in surface hydrophobicity was investigated. Cell wall hydrophobicity was measured as the contact angle of water on a bacterial layer collected on a microfilter. The contact angles ranged from 15 to 70 degrees. This method was compared with procedures based upon adhesion to hexadecane and with the partition of cells in a polyethylene glycol-dextran two-phase system. The results obtained with these three methods agreed reasonably well. The adhesion of 16 bacterial strains was measured on sulfated polystyrene as the solid phase. These experiments showed that hydrophobic cells adhered to a greater extent than hydrophilic cells. The extent of adhesion correlated well with the measured contact angles (linear regression coefficient, 0.8).

Alkanes↗
PubMed1987

Electrophoretic mobility and hydrophobicity as a measured to predict the initial steps of bacterial adhesion.

The relationship between physiochemical surface parameters and adhesion of bacterial cells to negatively charged polystyrene was studied. Cell surface hydrophobicity and electrokinetic potential were determined by contact angle measurement and electrophoresis, respectively. Both parameters influence cell adhesion. The effect of the electrokinetic potential increases with decreasing hydrophobicity. Cell surface characteristics determining adhesion are influenced by growth conditions. At high growth rates, bacterial cells tend to become more hydrophobic. This fact can be of ecological significance for controlling the spread of bacteria throughout the environment.

Bacteria↗
PubMed1986

Adsorption of proteins from solution at the solid-liquid interface.

The purpose of this article is to present some general principles and rules for the adsorption of proteins from aqueous solution on solid surfaces, emphasizing conformational and reversibility aspects. Special attention is paid to the relation between structural properties of the protein molecule and its adsorption behavior and to the role of small ions in the overall adsorption process. Thermodynamic analysis reveals that, under many conditions, the adsorption is driven by an entropy increase that is (partly) related to changes in the structure of the protein molecules.

Adsorption↗
PubMed1985

The interaction between alkyl derivatives and elastin.

Elastin from bovine ligamentum nuchae is exposed to aqueous solutions of different alkyl sulfates and carboxylates (fatty acids). The substrates of alkyl chain lengths varying between C8 and C17 bind to the elastin, the more so the longer the alkyl chain. However, the presence of two (or more) double bonds in the chain obstructs the penetration into the elastin network. As a result of absorption the elastin swells. The rate of binding is determined from the swelling of an elastin strip, that is monitored using a cathetometer. The diffusion of the substrate in the elastin is slower the longer the alkyl chain. The binding is reversible so that the Gibbs energy involved can be derived from the absorption isotherm. The values for the Gibbs energy of binding may amount to some tens of kJ per mol of substrate, with an increment of -4 kJ mol-1 per CH2 group. From the influence of temperature it is concluded that the binding is entropically driven. This, as well as the observation that the glass transition temperature of elastin is not affected by the presence of the alkyl derivatives, suggests that the substrates are bound to the amino acid residues of the elastin, rather than to the polypeptide backbone. Stress-strain experiments reveal that the elasticity decreases markedly on swelling of the sample, irrespective of the type of substrate that is absorbed. The phenomena described in this paper may be similar to those that occur between fatty acids in blood and arterial elastin, which could be at the origin of the development of atherosclerosis.

Absorption↗
PubMedDate not supplied

Measurements of the wettability of protein-covered hydroxyapatite surfaces.

We developed a new method (dropping time method, DTM) to investigate the wettability of a surface of a protein layer adsorbed on glass plates in aqueous solution. However, the previous setup of DTM can only be utilized for optically transparent materials. In this study, we have extended the method to optically nontransparent materials such as hydroxyapatite plates. DTM is based on measuring the dropping time of a liquid film along a protein-covered surface when this surface is instantaneously vertically removed from the protein solution. The intensity of the reflected light beam depends on the presence of a liquid film on the surface. This allows to estimate the movement of the liquid film along the sorbent surface. Thus, the extended DTM can be used for determining the wettability of optically nontransparent solid plates. The adsorption behavior of four proteins (albumin, lysozyme, beta-lactoglobulin, ovalbumin) on a hydrophobic hydroxyapatite plate in water was studied by this method. When adsorbed from a protein solution of high concentration, the surfaces of adsorbed proteins, except ovalbumin, were fairly hydrophilic; this hydrophilicity was already attained at the initial stage of the adsorption process. The surface of ovalbumin on hydroxyapatite was more hydrophobic than those of the other proteins, and the hydrophilicity increased with the protein adsorption process. At low protein concentration, the hydrophilicity increased in the course of the adsorption process. The change in hydrophilicity with time depends on the kind of protein. Hen's egg lysozyme is more hydrophilic and the time to reach saturation is shorter than for the other proteins. The processes of increasing hydrophilicity of the surface of human serum albumin, beta-lactoglobulin and ovalbumin are similar. However, for beta-lactoglobulin hydrophobicity at adsorption saturation is stronger than for human serum albumin and ovalbumin. Thus, using DTM it is shown that the hydrophilicity of the surface of adsorbed protein on hydroxyapatite depends strongly on the kind of protein.

Adsorption↗