2010
DOI: 10.1016/j.tifs.2009.10.009
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New directions towards structure formation and stability of protein-rich foods from globular proteins

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Cited by 56 publications
(30 citation statements)
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“…The formation and control of micro-and macro-structures in concentrated food systems is still poorly understood (Purwanti, Van der Goot, Boom, & Vereijken, 2010) and scientific appreciation of the length scale differences involved in solid food materials remains a considerable challenge (Ubbink, Burbridge, & Mezzenga, 2008). All soft matter, is in principle, thermodynamically unstable (Van der Sman & Van der Goot, 2009), which leads invariably to age-related, structural and textural change, one manifestation of which is hardening.…”
Section: Introductionmentioning
confidence: 99%
“…The formation and control of micro-and macro-structures in concentrated food systems is still poorly understood (Purwanti, Van der Goot, Boom, & Vereijken, 2010) and scientific appreciation of the length scale differences involved in solid food materials remains a considerable challenge (Ubbink, Burbridge, & Mezzenga, 2008). All soft matter, is in principle, thermodynamically unstable (Van der Sman & Van der Goot, 2009), which leads invariably to age-related, structural and textural change, one manifestation of which is hardening.…”
Section: Introductionmentioning
confidence: 99%
“…It is important to know to what extent this new component modifies the product, affecting its sensory properties. In the case of macromolecules such as polysaccharides or proteins, changes in composition can affect product structure in particular, modifying both rheological behaviour and perceived texture (Dickinson, 2007;Purwanti, van der Goot, Boom, & Vereijken, 2010).…”
Section: Introductionmentioning
confidence: 99%
“…The size of the protein particles produced using the PIT-templating method developed in this 376 study (around 1 to 10 µm) were appreciably larger than those that can be produced from globular 377 proteins using antisolvent precipitation (around 0.1 to 10 µm) (Joye & McClements, 2013) or 378 controlled thermal denaturation (around 0.1 to 10 µm) (Jones & McClements, 2010), but were 379 fairly similar in size to those that can be produced by extrusion methods (around 1 to 100 µm) 380 (Purwanti, et al, 2010;Saglam, et al, 2014). In principle, it should be possible to tailor the size 381 of the protein particles produced using the PIT-templating method by controlling the 382 temperature.…”
mentioning
confidence: 73%