Journal
ADVANCES IN COLLOID AND INTERFACE SCIENCE
Volume 107, Issue 1, Pages 27-49Publisher
ELSEVIER
DOI: 10.1016/j.cis.2003.08.003
Keywords
proteins; surfactants; competitive adsorption; emulsion and foam stability; atomic force microscopy; Brownian dynamics simulation; phase separation
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Proteins and low-molecular-weight (LMW) surfactants are used in the food industry as emulsifying (and foaming) ingredients and as stabilizers. These attributes are related to their ability to adsorb at fluid-fluid (and gas-fluid) interfaces lowering the interfacial (and surface) tension of liquids. Hence, the study of the properties of adsorbed layers of these molecules can be expected to lead to a better understanding of their effect on food products. Direct proof of the validity of mesoscopic models of systems of proteins and LMW surfactants can only be achieved by quantitative theoretical predictions being tested against both macroscopic and mesoscopic experiments. Computer simulation constitutes one of the few available tools to predict mathematically the behaviour of models of realistic complexity. Furthermore, experimental techniques such as atomic force microscopy (AFM) now allow high resolution imaging of these systems, providing the mesoscopic scale measurements to compare with the simulations. In this review, we bring together a number of related findings that have been generated at this mesoscopic level over the past few years. A useful simple model consisting of spherical particles interacting via bonded and unbonded forces is described, and the derived computer simulation results are compared against those from the imaging experiments. Special attention is paid to the adsorption of binary mixtures of proteins, mixtures of LMW surfactants, and also protein + surfactant mixed systems. We believe that further development of these mathematically well-defined physical models is necessary in order to achieve a proper understanding of the key physico-chemical processes involved. (C) 2003 Elsevier B.V. All rights reserved.
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