2016
DOI: 10.1016/j.ijbiomac.2016.04.012
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High pressure effects on the structural functionality of condensed globular-protein matrices

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Cited by 14 publications
(12 citation statements)
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References 103 publications
(109 reference statements)
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“…Both protein byproducts come from animal sources, but the morphologies of the protein systems are quite different. While proteins from crayfish are mainly myofibrillar proteins, albumen is a mixture of globular proteins …”
Section: Introductionmentioning
confidence: 99%
“…Both protein byproducts come from animal sources, but the morphologies of the protein systems are quite different. While proteins from crayfish are mainly myofibrillar proteins, albumen is a mixture of globular proteins …”
Section: Introductionmentioning
confidence: 99%
“…As shown in Figure 1, this source of plant protein remained largely in the native state (about 20% denaturation) in condensed preparations of 70-80% (w/w) solids that parallels the behaviour of the atmospheric (nonthermally treated) counterparts. The denaturation behaviour of soy glycinin is in between that of whey proteins undergoing almost complete denaturation up to 70% (w/w) solids and BSA that retains native conformation due to the presence of seventeen disulphide bridges in the molecule [10]. Despite the preservation of native conformation, soy glycinin at 80% (w/w) solids is able to form coherent networks exhibiting comparable mechanical strength and glass transition temperature to that of the thermally denatured counterparts, arguing that pressurisation provides both structural functionality and bioactivity in formulation engineering [12].…”
Section: Effect Of High Pressurementioning
confidence: 99%
“…The results indicate that the bio-and techno-functional properties of plant proteins can be improved through processing, including by heating, crosslinking with natural materials (e.g., genipin) [6] and binding with other biomaterials, like phenolic compounds. Specific treatments have been employed, including ultra-high temperature (UHT), high pressure and ultrasonication, to manipulate the structural behaviour and interactions with bioactive compounds/drugs leading to comparable functionality with corresponding dairy protein and Bovine Serum Albumin (BSA) systems [7][8][9][10].…”
Section: Introductionmentioning
confidence: 99%
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“…The common cause of these changes is the activation or inactivation of biological enzymes (22). An enzyme is a type of protein, and the impact of high-pressure processing on its structure is shown by several aspects, for example, an unchanged primary structure with unfolding and disassociation of the secondary, tertiary, and quaternary structures (23), the exposure of interior hydrophobic and sulfhydryl groups (24), and the denaturation, aggregation, and gelation of protein molecules, as well as changes to their interfacial properties (25). On the other hand, a change in chemical composition will be reflected in an increase/decrease of flavor or color substances.…”
Section: Zusammenfassungmentioning
confidence: 99%