Lysozyme adsorption at the air/water interface

Hunter, James R.; Kilpatrick, Peter K.; Carbonell, Ruben G.

doi:10.1016/0021-9797(90)90421-j

Cited by 89 publications

(86 citation statements)

References 40 publications

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“…The experimental setup for foam separation is almost the same as that used in the previous study [6,21,24]. A schematic diagram of the experimental setup is shown in Fig.…”

Section: Methodsmentioning

confidence: 99%

“…The procedure for measuring the flow rate of the liquid in foam was the same as it described in the previous study [6,21,24]. The OA solution prepared at a desired concentration or pH was stored in a storage tank.…”

Section: Methodsmentioning

confidence: 99%

“…interface by using radiolabeling technique [24]. They reported that the adsorption kinetics and the adsorption equilibrium followed Lamgmuir adsorption model.…”

Section: Determination Of Adsorption Parametersmentioning

confidence: 99%

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Variation of saturated surface density of ovalbumin on bubble surface in continuous foam separation

Maruyama

Seki

Suzuki

et al. 2006

Journal of Colloid and Interface Science

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“…The experimental setup for foam separation is almost the same as that used in the previous study [6,21,24]. A schematic diagram of the experimental setup is shown in Fig.…”

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Variation of saturated surface density of ovalbumin on bubble surface in continuous foam separation

Maruyama

Seki

Suzuki

et al. 2006

Journal of Colloid and Interface Science

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“…Radiometry results confirmed constant adsorbed protein mass with time t over the range 5 ≤ t ≤ 90 min., but the total amount of radio-labeled HAS was about 15-20% lower than that obtained with unlabeled protein (using the electrophoresis method at 2.4 mg/ mL, see Table 2). We attribute this difference to the influence of the radiolabel on protein amphilicity [33][34][35][36][37]. Table 2 compiles experimental results obtained for the proteins listed in Table 1.…”

Section: Protein Adsorption Kinetics Measured Using the Solution Deplmentioning

confidence: 99%

“…It is important to stress that this assumption is particular only to proteins at the relatively-high solution concentrations studied herein. It is known that mass-adsorption kinetics can be observed for proteins at low concentrations (≤ 1 mg/mL) by sensitive techniques with good time resolution [34,38].…”

mentioning

confidence: 99%

Volumetric interpretation of protein adsorption: Kinetic consequences of a slowly-concentrating interphase

Barnthip¹,

Noh²,

Leibner³

et al. 2008

Biomaterials

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Time-dependent energetics of blood-protein adsorption are interpreted in terms of a slowlyconcentrating three-dimensional interphase volume initially formed by rapid diffusion of protein molecules into an interfacial region spontaneously formed by bringing a protein solution into contact with a physical surface. This modification of standard adsorption theory is motivated by the experimental observation that interfacial tensions of protein-containing solutions decrease slowly over the first hour to a steady-state value while, over this same period, the total adsorbed-protein mass is constant (for lysozyme, 15 kDa; albumin, 66 kDa; prothrombin, 72 kDa; IgG, 160 kDa; fibrinogen, 341 kDa studied in this work). These seemingly divergent observations are rationalized by the fact that interfacial energetics (tensions) are explicit functions of solute chemical potential (concentration), not adsorbed mass. Hence, rates-of-interfacial-tension-change parallel a slow interphase concentration effect whereas solution depletion detects a constant interphase composition within the time frame of experiment. A straightforward mathematical model approximating the perceived physical situation leads to an analytic formulation that is used to compute time-varying interphase volume and protein concentration from experimentally-measured interfacial tensions. Derivation from the fundamental thermodynamic adsorption equation verifies that protein adsorption from dilute solution is controlled by a partition coefficient at equilibrium, as is observed experimentally at steady state. Implications of the alternative interpretation of adsorption kinetics on biomaterials and biocompatibility are discussed. KeywordsProtein adsorption; kinetics; interfacial energetics; interphase; surface; radiometry IntroductionProtein-adsorption kinetics are of practical importance in biomaterials because adsorption rates have been implicated as a cause of selective protein adsorption. For example, the so-called Vroman Effect is commonly thought to occur because low-molecular-weight proteins *Author to whom correspondence should be addressed EAV3@PSU.EDU. Publisher's Disclaimer: This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. NIH Public Access Author ManuscriptBiomaterials. Author manuscript; available in PMC 2009 July 1. Published in final edited form as:Biomaterials. presumably arriving first at a surface immersed in a multi-component solution are displaced by higher-molecular-weight proteins arriving later (see refs. and citations therein). The final adsorbed-protein composition is thus purported to be achieved through a complex se...

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Hydroxynitrile lyase at the diisopropyl ether/water interface: Evidence for interfacial enzyme activity

Hickel¹,

Radke²,

Blanch³

1999

Biotechnol. Bioeng.

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Lysozyme adsorption at the air/water interface

Cited by 89 publications

References 40 publications

Variation of saturated surface density of ovalbumin on bubble surface in continuous foam separation

Variation of saturated surface density of ovalbumin on bubble surface in continuous foam separation

Volumetric interpretation of protein adsorption: Kinetic consequences of a slowly-concentrating interphase

Hydroxynitrile lyase at the diisopropyl ether/water interface: Evidence for interfacial enzyme activity

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