Relationships Between Optical and Textural Properties of Cold-set Whey Protein Gels

Barbut, Shai

doi:10.1006/fstl.1996.0234

Cited by 9 publications

(10 citation statements)

References 12 publications

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“…Many globular food proteins have the ability to form a gel (1). The gel properties depend on protein concentration, ionic strength, pH, and heating procedure (2,3).…”

Section: Introductionmentioning

confidence: 99%

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A New Multistep Ca²⁺-Induced Cold Gelation Process for β-Lactoglobulin

Veerman

Baptist

Sagis

et al. 2003

J. Agric. Food Chem.

108

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The objective of this study was to obtain beta-lactoglobulin (beta-lg) gels at very low protein concentrations using a new multistep Ca(2+)-induced cold gelation process. In the conventional cold gelation process, salt free beta-lg solutions were heated at neutral pH, cooled, and cross-linked by adding salts. In our new process, first, long linear beta-lg fibrils were formed at pH 2. Solutions of these fibrils were cooled, and subsequently, the pH was adjusted to 7 or 8. Transmission electron microscopy studies showed that the long linear fibrils formed at pH 2 were stable when the pH was adjusted to 7 or 8. In the final step, the fibrils were cross-linked using CaCl(2). Using rheological measurements, the critical percolation concentration was determined. In the new multistep cold gelation process, the critical percolation concentration was an order of magnitude lower than in the conventional cold gelation method.

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“…Many globular food proteins have the ability to form a gel (1). The gel properties depend on protein concentration, ionic strength, pH, and heating procedure (2,3).…”

Section: Introductionmentioning

confidence: 99%

“…To obtain cold set gels, it is necessary to prepare a heatdenatured solution with a protein concentration below the critical gelation concentration at a temperature above the denaturation temperature. The gelation is induced at low temperatures by the addition of mono-or polyvalent cations (1,3,13,16,17).…”

Section: Introductionmentioning

confidence: 99%

A New Multistep Ca²⁺-Induced Cold Gelation Process for β-Lactoglobulin

Veerman

Baptist

Sagis

et al. 2003

J. Agric. Food Chem.

108

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“…The formation of disulfide bonds in heat-set gels is well established (Hoffmann and van Mil, 1997). A smaller number of papers have been published that relate the mechanical properties of coldset gels to specific preparation conditions (Ju and Kilara, 1998a,b) and properties of ingredients such as the presence of calcium (Barbut and Foegeding, 1993;Barbut, 1995Barbut, , 1997. Despite these studies there are still a number of unanswered questions regarding the cold gelation process.…”

Section: Introductionmentioning

confidence: 99%

Formation of Disulfide Bonds in Acid-Induced Gels of Preheated Whey Protein Isolate

Alting

Hamer

Kruif

et al. 2000

J. Agric. Food Chem.

214

165

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Cold gelation of whey proteins is a two-step process. First, protein aggregates are prepared by a heat treatment of a solution of native proteins in the absence of salt. Second, after cooling of the solution, gelation is induced by lowering the pH at ambient temperature. To demonstrate the additional formation of disulfide bonds during this second step, gelation of whey protein aggregates with and without a thiol-blocking treatment was studied. Modification of reactive thiols on the surface of the aggregates was carried out after the heat-treatment step. To exclude specific effects of the agent itself, different thiol-blocking agents were used. Dynamic light scattering and SDS-agarose gel electrophoresis were used to show that the size of the aggregates was not changed by this modification. The kinetics of gelation as determined by the development of pH and turbidity within the first 8 h of acidification were not affected by blocking thiol groups. During gelation, formation of large, covalently linked, aggregates occurred only in the case of unblocked WPI aggregates, which demonstrates that additional disulfide bonds were formed. Results of permeability and confocal scanning laser microscope measurements did not reveal any differences in the microstructure of networks prepared from treated or untreated whey protein aggregates. However, gel hardness was decreased 10-fold in gels prepared from blocked aggregates. Mixing different amounts of blocked and unblocked aggregates allowed gel hardness to be controlled. It is proposed that the initial microstructure of the gels is primarily determined by the acid-induced noncovalent interactions. The additional covalent disulfide bonds formed during gelation are involved in stabilizing the network and increase gel strength.

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“…1 Supramolecular structures obtained by a self-assembly process can exhibit novel features that can be used for various food and nonfood applications. Proteins are functional macromolecules and their functionalities are promoted by disturbing their native 3D structures via heat, 2,3 salts, 4,5 chemicals, 6 and enzymes. 7,8 Enzymatic hydrolysis denatures the highly ordered protein structure leading to the formation of various-sized peptide fragments, which, under the right conditions, can form molecular self-assemblies that promote novel supramolecules with the potential of improved features for various applications.…”

Section: Introductionmentioning

confidence: 99%

Structure and binding ability of self‐assembled α‐lactalbumin protein nanotubular gels

Tarhan

Hamaker

Campanella

2021

Biotechnology Progress

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Relationships Between Optical and Textural Properties of Cold-set Whey Protein Gels

Cited by 9 publications

References 12 publications

A New Multistep Ca²⁺-Induced Cold Gelation Process for β-Lactoglobulin

A New Multistep Ca²⁺-Induced Cold Gelation Process for β-Lactoglobulin

Formation of Disulfide Bonds in Acid-Induced Gels of Preheated Whey Protein Isolate

Structure and binding ability of self‐assembled α‐lactalbumin protein nanotubular gels

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Relationships Between Optical and Textural Properties of Cold-set Whey Protein Gels

Cited by 9 publications

References 12 publications

A New Multistep Ca2+-Induced Cold Gelation Process for β-Lactoglobulin

A New Multistep Ca2+-Induced Cold Gelation Process for β-Lactoglobulin

Formation of Disulfide Bonds in Acid-Induced Gels of Preheated Whey Protein Isolate

Structure and binding ability of self‐assembled α‐lactalbumin protein nanotubular gels

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A New Multistep Ca²⁺-Induced Cold Gelation Process for β-Lactoglobulin

A New Multistep Ca²⁺-Induced Cold Gelation Process for β-Lactoglobulin