Eric Dickinson
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Previous Organizations / Institutes
The organizations / institutes from the scholar's other articles in the past ten years
Research Interests
Eric Dickinson has a total of 365 co-authors. Here are the top co-authors by number of shared publications:
Brent S. Murray
39 shared publications- Jianshe Chen
Laboratory of Food Oral Processing, School of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, China
18 shared publications Rammile Ettelaie
16 shared publications- Stephen Robert Euston
Institute of Biological Chemistry, Biophysics and Bioengineering, School of Engineering and Physical Sciences, Heriot-Watt University, Edinburgh, United Kingdom
14 shared publications George Stainsby
12 shared publications- Luis Ariel Pugnaloni
Universidad Nacional de La Pampa
12 shared publications
Latest Publications
- 1 August 2021
- Published by Elsevier in Food Hydrocolloids
- Vol. 117
The perfect hydrocolloid stabilizer: Imagination versus reality
- 1 August 2021
- Published by Elsevier in Food Hydrocolloids
- Vol. 117
The perfect hydrocolloid stabilizer: Imagination versus reality
- Top Cited Papers
- 23 March 2017
- Published by Wiley in Comprehensive Reviews in Food Science and Food Safety
- Vol. 16 (3) , 532-555
Double Emulsions Relevant to Food Systems: Preparation, Stability, and Applications
This review describes advances in the preparation of food‐relevant double emulsions (DEs) of the water‐in‐oil‐in‐water (W/O/W) and oil‐in‐water‐in‐oil (O/W/O) types with emphasis on research published within the last decade. The information is assembled and critically evaluated according to the following aspects: the food application area, the range of encapsulated components and emulsion composition, the emulsification preparation methods, the balancing of the osmotic pressure, the stabilization by increased viscosity or gelation, the role of protein–polysaccharide interactions, and the techniques used to estimate DE yield and emulsification efficiency. Particular focus is directed toward the control of encapsulation and release behavior, including strategies that have been employed to improve the retention ability of the inner phase droplets by modifying the outer oil–water interface through mixed ingredient interactions, Pickering stabilization by particles, and biopolymer gelation. We also briefly consider the incorporation of DEs into dried microcapsules and the stability of W/O/W emulsions during eating and digestion. It would appear that 2 outstanding issues are currently preventing full realization of the potential of DEs in food applications: (i) the lack of availability of large‐scale production equipment to ensure efficient nondestructive 2nd‐stage emulsification, and (ii) the limited range of food‐grade ingredients available to successfully replace polyglycerol polyricinoleate as the primary emulsifier in W/O/W formulations.
- 23 March 2017
- Published by Wiley in Comprehensive Reviews in Food Science and Food Safety
- Vol. 16 (3) , 532-555
Top Cited PapersDouble Emulsions Relevant to Food Systems: Preparation, Stability, and Applications
This review describes advances in the preparation of food‐relevant double emulsions (DEs) of the water‐in‐oil‐in‐water (W/O/W) and oil‐in‐water‐in‐oil (O/W/O) types with emphasis on research published within the last decade. The information is assembled and critically evaluated according to the following aspects: the food application area, the range of encapsulated components and emulsion composition, the emulsification preparation methods, the balancing of the osmotic pressure, the stabilization by increased viscosity or gelation, the role of protein–polysaccharide interactions, and the techniques used to estimate DE yield and emulsification efficiency. Particular focus is directed toward the control of encapsulation and release behavior, including strategies that have been employed to improve the retention ability of the inner phase droplets by modifying the outer oil–water interface through mixed ingredient interactions, Pickering stabilization by particles, and biopolymer gelation. We also briefly consider the incorporation of DEs into dried microcapsules and the stability of W/O/W emulsions during eating and digestion. It would appear that 2 outstanding issues are currently preventing full realization of the potential of DEs in food applications: (i) the lack of availability of large‐scale production equipment to ensure efficient nondestructive 2nd‐stage emulsification, and (ii) the limited range of food‐grade ingredients available to successfully replace polyglycerol polyricinoleate as the primary emulsifier in W/O/W formulations.
- 1 January 2016
- Published by Elsevier in Food Hydrocolloids
- Vol. 52, 497-509
Exploring the frontiers of colloidal behaviour where polymers and particles meet
- 1 January 2016
- Published by Elsevier in Food Hydrocolloids
- Vol. 52, 497-509
Exploring the frontiers of colloidal behaviour where polymers and particles meet
- 1 July 2015
- Published by Elsevier in Journal of Colloid and Interface Science
- Vol. 449, 38-45
Structuring of colloidal particles at interfaces and the relationship to food emulsion and foam stability
- 1 July 2015
- Published by Elsevier in Journal of Colloid and Interface Science
- Vol. 449, 38-45
Structuring of colloidal particles at interfaces and the relationship to food emulsion and foam stability
- 1 June 2015
- Published by Elsevier in Trends in Food Science & Technology
- Vol. 43 (2) , 178-188
Microgels — An alternative colloidal ingredient for stabilization of food emulsions
- 1 June 2015
- Published by Elsevier in Trends in Food Science & Technology
- Vol. 43 (2) , 178-188
Microgels — An alternative colloidal ingredient for stabilization of food emulsions
- 10 April 2015
- Published by Annual Reviews in Annual Review of Food Science and Technology
- Vol. 6 (1) , 211-233
Colloids in Food: Ingredients, Structure, and Stability
This article reviews progress in the field of food colloids with particular emphasis on advances in novel functional ingredients and nanoscale structuring. Specific aspects of ingredient development described here are the stabilization of bubbles and foams by the protein hydrophobin, the emulsifying characteristics of Maillard-type protein–polysaccharide conjugates, the structural and functional properties of protein fibrils, and the Pickering stabilization of dispersed droplets by food-grade nanoparticles and microparticles. Building on advances in the nanoscience of biological materials, the application of structural design principles to the fabrication of edible colloids is leading to progress in the fabrication of functional dispersed systems—multilayer interfaces, multiple emulsions, and gel-like emulsions. The associated physicochemical insight is contributing to our mechanistic understanding of oral processing and textural perception of food systems and to the development of colloid-based strategies to control delivery of nutrients during food digestion within the human gastrointestinal tract.
- 10 April 2015
- Published by Annual Reviews in Annual Review of Food Science and Technology
- Vol. 6 (1) , 211-233
Colloids in Food: Ingredients, Structure, and Stability
This article reviews progress in the field of food colloids with particular emphasis on advances in novel functional ingredients and nanoscale structuring. Specific aspects of ingredient development described here are the stabilization of bubbles and foams by the protein hydrophobin, the emulsifying characteristics of Maillard-type protein–polysaccharide conjugates, the structural and functional properties of protein fibrils, and the Pickering stabilization of dispersed droplets by food-grade nanoparticles and microparticles. Building on advances in the nanoscience of biological materials, the application of structural design principles to the fabrication of edible colloids is leading to progress in the fabrication of functional dispersed systems—multilayer interfaces, multiple emulsions, and gel-like emulsions. The associated physicochemical insight is contributing to our mechanistic understanding of oral processing and textural perception of food systems and to the development of colloid-based strategies to control delivery of nutrients during food digestion within the human gastrointestinal tract.
- 27 October 2014
- Published by IOP Publishing in Journal of Physics: Condensed Matter
- Vol. 26 (46) , 464109
First-order phase transition during displacement of amphiphilic biomacromolecules from interfaces by surfactant molecules
The adsorption of surfactants onto a hydrophobic interface, already laden with a fixed number of amphiphilic macromolecules, is studied using the self consistent field calculation method of Scheutjens and Fleer. For biopolymers having unfavourable interactions with the surfactant molecules, the adsorption isotherms show an abrupt jump at a certain value of surfactant bulk concentration. Alternatively, the same behaviour is exhibited when the number of amphiphilic chains on the interface is decreased. We show that this sudden jump is associated with a first-order phase transition, by calculating the free energy values for the stable and the metastable states at both sides of the transition point. We also observe that the transition can occur for two approaching surfaces, from a high surfactant coverage phase to a low surfactant coverage one, at sufficiently close separation distances. The consequence of this finding for the steric colloidal interactions, induced by the overlap of two biopolymer + surfactant films, is explored. In particular, a significantly different interaction, in terms of its magnitude and range, is predicted for these two phases. We also consider the relevance of the current study to problems involving the competitive displacement of proteins by surfactants in food colloid systems.
- 27 October 2014
- Published by IOP Publishing in Journal of Physics: Condensed Matter
- Vol. 26 (46) , 464109
First-order phase transition during displacement of amphiphilic biomacromolecules from interfaces by surfactant molecules
The adsorption of surfactants onto a hydrophobic interface, already laden with a fixed number of amphiphilic macromolecules, is studied using the self consistent field calculation method of Scheutjens and Fleer. For biopolymers having unfavourable interactions with the surfactant molecules, the adsorption isotherms show an abrupt jump at a certain value of surfactant bulk concentration. Alternatively, the same behaviour is exhibited when the number of amphiphilic chains on the interface is decreased. We show that this sudden jump is associated with a first-order phase transition, by calculating the free energy values for the stable and the metastable states at both sides of the transition point. We also observe that the transition can occur for two approaching surfaces, from a high surfactant coverage phase to a low surfactant coverage one, at sufficiently close separation distances. The consequence of this finding for the steric colloidal interactions, induced by the overlap of two biopolymer + surfactant films, is explored. In particular, a significantly different interaction, in terms of its magnitude and range, is predicted for these two phases. We also consider the relevance of the current study to problems involving the competitive displacement of proteins by surfactants in food colloid systems.
- 1 November 2013
- Published by Elsevier in Advances in Colloid and Interface Science
- Vol. 199-200, 114-127
Structure and rheology of colloidal particle gels: Insight from computer simulation
- 1 November 2013
- Published by Elsevier in Advances in Colloid and Interface Science
- Vol. 199-200, 114-127
Structure and rheology of colloidal particle gels: Insight from computer simulation
- 6 February 2013
- Published by American Chemical Society (ACS) in Journal of Agricultural and Food Chemistry
- Vol. 61 (7) , 1554-1562
Interfacial Study of Class II Hydrophobin and Its Mixtures with Milk Proteins: Relationship to Bubble Stability
Class II hydrophobin (HFBII) is a very promising ingredient for improving food foam stability. Pure HFBII-stabilized bubbles exhibited exceptional stability to disproportionation (dissolution) but were not stable to bubble coalescence induced by a pressure drop. Bubbles stabilized by mixtures of HFBII + sodium caseinate (SC) or β-lactoglobulin (BL) showed decreased shrinkage rates compared to pure SC or BL and improved the stability to pressure-drop-induced coalescence. Higher bubble stability was more closely correlated with higher surface shear viscosity than the surface dilatational elasticity of the mixed protein systems. Brewster angle microscopy observations and the high shear strength of adsorbed films, including HFBII, even in the presence of hydrophobic and hydrogen-bond-breaking agents, confirm that intermolecular attractive cross-links are unlikely to be the origin of the high strength of HFBII films. Possibly the HFBII molecules form a tightly interlocking monolayer of Janus-like particles at the air–water interface.
- 6 February 2013
- Published by American Chemical Society (ACS) in Journal of Agricultural and Food Chemistry
- Vol. 61 (7) , 1554-1562
Interfacial Study of Class II Hydrophobin and Its Mixtures with Milk Proteins: Relationship to Bubble Stability
Class II hydrophobin (HFBII) is a very promising ingredient for improving food foam stability. Pure HFBII-stabilized bubbles exhibited exceptional stability to disproportionation (dissolution) but were not stable to bubble coalescence induced by a pressure drop. Bubbles stabilized by mixtures of HFBII + sodium caseinate (SC) or β-lactoglobulin (BL) showed decreased shrinkage rates compared to pure SC or BL and improved the stability to pressure-drop-induced coalescence. Higher bubble stability was more closely correlated with higher surface shear viscosity than the surface dilatational elasticity of the mixed protein systems. Brewster angle microscopy observations and the high shear strength of adsorbed films, including HFBII, even in the presence of hydrophobic and hydrogen-bond-breaking agents, confirm that intermolecular attractive cross-links are unlikely to be the origin of the high strength of HFBII films. Possibly the HFBII molecules form a tightly interlocking monolayer of Janus-like particles at the air–water interface.