Influence of pH and Ionic Strength on Heat-Induced Formation and Rheological Properties of Soy Protein Gels in Relation to Denaturation and Their Protein Compositions

J.M.S. Renkema; H. Gruppen; T. van Vliet

doi:10.1021/jf020061b

Influence of pH and Ionic Strength on Heat-Induced Formation and Rheological Properties of Soy Protein Gels in Relation to Denaturation and Their Protein Compositions

J.M.S. Renkema, H. Gruppen, T. van Vliet

Research output: Contribution to journal › Article › Academic › peer-review

165 Citations (Scopus)

Abstract

The influence of pH and ionic strength on gel formation and gel properties of soy protein isolate (SPI) in relation to denaturation and protein aggregation/precipitation was studied. Denaturation proved to be a prerequisite for gel formation under all conditions of pH and ionic strength studied. Gels exhibited a low stiffness at pH >6 and a high stiffness at pH 5 less protein and especially fewer acidic polypeptides take part in the network, coinciding with less stiff gels. At pH 7.6, extensive rearrangements in the network structure took place during prolonged heating, whereas at pH 3.8 rearrangements did not occur.

Original language	English
Pages (from-to)	6064-6071
Journal	Journal of Agricultural and Food Chemistry
Volume	50
Issue number	21
DOIs	https://doi.org/10.1021/jf020061b
Publication status	Published - 2002

Keywords

soybean beta-conglycinin
molecular-structure
gelation
glycinin
subunits
solubility
isolate
7s
association
behavior

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10.1021/jf020061b

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title = "Influence of pH and Ionic Strength on Heat-Induced Formation and Rheological Properties of Soy Protein Gels in Relation to Denaturation and Their Protein Compositions",

abstract = "The influence of pH and ionic strength on gel formation and gel properties of soy protein isolate (SPI) in relation to denaturation and protein aggregation/precipitation was studied. Denaturation proved to be a prerequisite for gel formation under all conditions of pH and ionic strength studied. Gels exhibited a low stiffness at pH >6 and a high stiffness at pH 5 less protein and especially fewer acidic polypeptides take part in the network, coinciding with less stiff gels. At pH 7.6, extensive rearrangements in the network structure took place during prolonged heating, whereas at pH 3.8 rearrangements did not occur.",

keywords = "soybean beta-conglycinin, molecular-structure, gelation, glycinin, subunits, solubility, isolate, 7s, association, behavior",

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Influence of pH and Ionic Strength on Heat-Induced Formation and Rheological Properties of Soy Protein Gels in Relation to Denaturation and Their Protein Compositions. / Renkema, J.M.S.; Gruppen, H.; van Vliet, T.

In: Journal of Agricultural and Food Chemistry, Vol. 50, No. 21, 2002, p. 6064-6071.

Research output: Contribution to journal › Article › Academic › peer-review

TY - JOUR

T1 - Influence of pH and Ionic Strength on Heat-Induced Formation and Rheological Properties of Soy Protein Gels in Relation to Denaturation and Their Protein Compositions

AU - Renkema, J.M.S.

AU - Gruppen, H.

AU - van Vliet, T.

N1 - F698

PY - 2002

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N2 - The influence of pH and ionic strength on gel formation and gel properties of soy protein isolate (SPI) in relation to denaturation and protein aggregation/precipitation was studied. Denaturation proved to be a prerequisite for gel formation under all conditions of pH and ionic strength studied. Gels exhibited a low stiffness at pH >6 and a high stiffness at pH 5 less protein and especially fewer acidic polypeptides take part in the network, coinciding with less stiff gels. At pH 7.6, extensive rearrangements in the network structure took place during prolonged heating, whereas at pH 3.8 rearrangements did not occur.

AB - The influence of pH and ionic strength on gel formation and gel properties of soy protein isolate (SPI) in relation to denaturation and protein aggregation/precipitation was studied. Denaturation proved to be a prerequisite for gel formation under all conditions of pH and ionic strength studied. Gels exhibited a low stiffness at pH >6 and a high stiffness at pH 5 less protein and especially fewer acidic polypeptides take part in the network, coinciding with less stiff gels. At pH 7.6, extensive rearrangements in the network structure took place during prolonged heating, whereas at pH 3.8 rearrangements did not occur.

KW - soybean beta-conglycinin

KW - molecular-structure

KW - gelation

KW - glycinin

KW - subunits

KW - solubility

KW - isolate

KW - 7s

KW - association

KW - behavior

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JO - Journal of Agricultural and Food Chemistry

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SN - 0021-8561

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