Structure-fracture measurements of particulate gels
Images on a micron scale and the stress-strain behaviour of gel structures during tension were simultaneously recorded in real time using a mini fracture cell under the confocal laser scanning microscope (CLSM). β-lactoglobulin gels tailor-made to vary in density, connectivity, thickness of strands...
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Veröffentlicht in: | Journal of materials science 2004-11, Vol.39 (21), p.6473-6482 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Images on a micron scale and the stress-strain behaviour of gel structures during tension were simultaneously recorded in real time using a mini fracture cell under the confocal laser scanning microscope (CLSM). β-lactoglobulin gels tailor-made to vary in density, connectivity, thickness of strands and size of aggregates and clusters were used as a food model system. Amylopectin and gelatin were used to generate different types of β-lactoglobulin network microstructures and also as a second continuous phase.Both rheological and structural differences in fragility between β-lactoglobulin gels were verified according to the density of their aggregated network structure. A dense gel has a more brittle behaviour where the clusters are rigid and the crack propagates smoothly compared to a gel with an open network structure, which has a discontinuous crack growth, via a winding pathway around clusters, and also break-up of the pores far from the crack tip. Differences in the stretchability of the aggregated β-lactoglobulin structure, induced by addition of amylopectin solution, were proved and related to differences in stress-strain behaviour and crack propagation.Gelatin gels in the pores between the β-lactoglobulin clusters do not affect the structure of the β-lactoglobulin network but make the fracture fragile giving a smooth fracture surface, cause continuous crack growth and fracture propagation through β-lactoglobulin clusters. This is a consequence of that the mixed gel follows the behaviour of the gelatin gel when the gelatin phase is stronger than the β-lactoglobulin network. |
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ISSN: | 0022-2461 1573-4803 1573-4803 |
DOI: | 10.1023/B:JMSC.0000044885.01345.a5 |