Acid-induced cold gelation of globular proteins: effects of protein aggregate characteristics ans disulfide bonding on Rheological properties.

A.C. Alting, M. Weijers, E.H.A. de Hoog, A.M. Pijpekamp, M.A. Cohen Stuart, R.J. Hamer, C.G. de Kruif, R.W. Visschers

Research output: Contribution to journalArticleAcademicpeer-review

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Abstract

The process of cold gelation of ovalbumin and the properties of the resulting cold-set gels were compared to those of whey protein isolate. Under the chosen heating conditions, most protein was organized in aggregates. For both protein preparations, the aggregates consisted of covalently linked monomers. Both types of protein aggregates had comparable numbers of thiol groups exposed at their surfaces but had clearly different shapes. During acid-induced gelation, the characteristic ordering caused by the repulsive character disappeared and was replaced by a random distribution. This process did not depend on aggregate characteristics and probably applies to any type of protein aggregate. Covalent bonds are the main determinants of the gel hardness. The formation of additional disulfide bonds during gelation depended on the number and accessibility of thiol groups and disulfide bonds in the molecule and was found to clearly differ between the proteins studied. However, upon blocking of the thiol groups, long fibrillar structures of ovalbumin contribute significantly to gel hardness, demonstrating the importance of aggregate shape.
Original languageEnglish
Pages (from-to)623-631
JournalJournal of Agricultural and Food Chemistry
Volume52
Issue number3
DOIs
Publication statusPublished - 2004

Fingerprint

protein aggregates
Gelation
gelation
rheological properties
sulfides
Sulfhydryl Compounds
Disulfides
Gels
Ovalbumin
Hardness
Acids
acids
thiols
Proteins
proteins
disulfide bonds
ovalbumin
gels
Heating
Covalent bonds

Keywords

  • heat-induced gelation
  • denatured whey-protein
  • beta-lactoglobulin
  • alpha-lactalbumin
  • ca2+-induced gelation
  • interchange reactions
  • phase-separation
  • set gels
  • isolate
  • ovalbumin

Cite this

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title = "Acid-induced cold gelation of globular proteins: effects of protein aggregate characteristics ans disulfide bonding on Rheological properties.",
abstract = "The process of cold gelation of ovalbumin and the properties of the resulting cold-set gels were compared to those of whey protein isolate. Under the chosen heating conditions, most protein was organized in aggregates. For both protein preparations, the aggregates consisted of covalently linked monomers. Both types of protein aggregates had comparable numbers of thiol groups exposed at their surfaces but had clearly different shapes. During acid-induced gelation, the characteristic ordering caused by the repulsive character disappeared and was replaced by a random distribution. This process did not depend on aggregate characteristics and probably applies to any type of protein aggregate. Covalent bonds are the main determinants of the gel hardness. The formation of additional disulfide bonds during gelation depended on the number and accessibility of thiol groups and disulfide bonds in the molecule and was found to clearly differ between the proteins studied. However, upon blocking of the thiol groups, long fibrillar structures of ovalbumin contribute significantly to gel hardness, demonstrating the importance of aggregate shape.",
keywords = "heat-induced gelation, denatured whey-protein, beta-lactoglobulin, alpha-lactalbumin, ca2+-induced gelation, interchange reactions, phase-separation, set gels, isolate, ovalbumin",
author = "A.C. Alting and M. Weijers and {de Hoog}, E.H.A. and A.M. Pijpekamp and {Cohen Stuart}, M.A. and R.J. Hamer and {de Kruif}, C.G. and R.W. Visschers",
year = "2004",
doi = "10.1021/jf034753r",
language = "English",
volume = "52",
pages = "623--631",
journal = "Journal of Agricultural and Food Chemistry",
issn = "0021-8561",
publisher = "American Chemical Society",
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}

Acid-induced cold gelation of globular proteins: effects of protein aggregate characteristics ans disulfide bonding on Rheological properties. / Alting, A.C.; Weijers, M.; de Hoog, E.H.A.; Pijpekamp, A.M.; Cohen Stuart, M.A.; Hamer, R.J.; de Kruif, C.G.; Visschers, R.W.

In: Journal of Agricultural and Food Chemistry, Vol. 52, No. 3, 2004, p. 623-631.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Acid-induced cold gelation of globular proteins: effects of protein aggregate characteristics ans disulfide bonding on Rheological properties.

AU - Alting, A.C.

AU - Weijers, M.

AU - de Hoog, E.H.A.

AU - Pijpekamp, A.M.

AU - Cohen Stuart, M.A.

AU - Hamer, R.J.

AU - de Kruif, C.G.

AU - Visschers, R.W.

PY - 2004

Y1 - 2004

N2 - The process of cold gelation of ovalbumin and the properties of the resulting cold-set gels were compared to those of whey protein isolate. Under the chosen heating conditions, most protein was organized in aggregates. For both protein preparations, the aggregates consisted of covalently linked monomers. Both types of protein aggregates had comparable numbers of thiol groups exposed at their surfaces but had clearly different shapes. During acid-induced gelation, the characteristic ordering caused by the repulsive character disappeared and was replaced by a random distribution. This process did not depend on aggregate characteristics and probably applies to any type of protein aggregate. Covalent bonds are the main determinants of the gel hardness. The formation of additional disulfide bonds during gelation depended on the number and accessibility of thiol groups and disulfide bonds in the molecule and was found to clearly differ between the proteins studied. However, upon blocking of the thiol groups, long fibrillar structures of ovalbumin contribute significantly to gel hardness, demonstrating the importance of aggregate shape.

AB - The process of cold gelation of ovalbumin and the properties of the resulting cold-set gels were compared to those of whey protein isolate. Under the chosen heating conditions, most protein was organized in aggregates. For both protein preparations, the aggregates consisted of covalently linked monomers. Both types of protein aggregates had comparable numbers of thiol groups exposed at their surfaces but had clearly different shapes. During acid-induced gelation, the characteristic ordering caused by the repulsive character disappeared and was replaced by a random distribution. This process did not depend on aggregate characteristics and probably applies to any type of protein aggregate. Covalent bonds are the main determinants of the gel hardness. The formation of additional disulfide bonds during gelation depended on the number and accessibility of thiol groups and disulfide bonds in the molecule and was found to clearly differ between the proteins studied. However, upon blocking of the thiol groups, long fibrillar structures of ovalbumin contribute significantly to gel hardness, demonstrating the importance of aggregate shape.

KW - heat-induced gelation

KW - denatured whey-protein

KW - beta-lactoglobulin

KW - alpha-lactalbumin

KW - ca2+-induced gelation

KW - interchange reactions

KW - phase-separation

KW - set gels

KW - isolate

KW - ovalbumin

U2 - 10.1021/jf034753r

DO - 10.1021/jf034753r

M3 - Article

VL - 52

SP - 623

EP - 631

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

SN - 0021-8561

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