The DOI matches its Crossref record.
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
Open accessAbstract
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 <6. This might be caused by variations in the association/dissociation behavior of the soy proteins on heating as a function of pH, as indicated by the different protein compositions of the dissolved protein after heating. At pH 3-5 all protein seems to participate in the network, whereas 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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
For soybean protein, gels formed at lower pH levels (pH < 6) exhibited greater stiffness and hardness compared to those formed at higher pH values (pH > 6).
“Renkema et al. (2002) investigated the effect of pH and ionic strength on the gelling properties of soybean protein, finding that gels formed at lower pH levels (pH < 6) exhibited greater stiffness and hardness compared to those formed at higher pH values (pH > 6).”
From A Review of Gelation of Plant Proteins and Their Influencing Factors (2025) · cites this paper as Renkema et al. (2002)
Citations
Cites
No references could be resolved yet.
Research works printed but not linked: 44
- Staswick P. E., 1984, J. Biol. Chem., 259, 13435
- Wolf W. J., 1958, J. Am. Chem. Soc., 80, 5735, 10.1021/ja01554a040 · DOI
- Lakemond C. M. M., 2000, J. Agric. Food Chem., 48, 1990
- Koshiyama I., 1983, Seed Proteins Biochemistry, Genetics, Nutritive Value, 450
- Thanh V. H., 1978, J. Agric. Food Chem., 26, 695, 10.1021/jf60217a027 · DOI
- Hermansson A.-M, 1986, J. Am. Oil Chem. Soc., 63, 666
- Damodaran S, 1988, J. Agric. Food Chem., 36, 269, 10.1021/jf00080a007 · DOI
- Danilenko A. N., 1987, Biophysics, 32, 439
- Lakemond C. M. M., 2000, J. Agric. Food Chem., 48, 1995
- Maruyama N., 1998, Eur. J. Biochem., 258, 862, 10.1046/j.1432-1327.1998.2580854.x · DOI
- Maruyama N., 1999, J. Agric. Food Chem., 47, 5284, 10.1021/jf990360+ · DOI
- Puppo M. C., 1999, J. Food Sci., 64, 56, 10.1111/j.1365-2621.1999.tb09859.x · DOI
- Renkema J. M. S., 2001, Food Hydrocolloids, 15, 414
- Catsimpoolas N., 1970, Cereal Chem., 47, 569
- Bau H. M., 1985, Can. Inst. Food Sci. Technol. J., 18, 279
- Utsumi S., 1985, J. Food Sci., 50, 1282, 10.1111/j.1365-2621.1985.tb10461.x · DOI
- van Kleef F. S. M, 1986, Biopolymers, 25, 59
- Nagano T., 1994, Biopolymers, 34, 1309
- Nagano T., 1994, J. Agric. Food Chem., 42, 1419, 10.1021/jf00043a005 · DOI
- Nagano T., 1994, Biopolymers, 34, 298
- Puppo M. C., 1995, J. Agric. Food Chem., 43, 2361, 10.1021/jf00057a008 · DOI
- Renkema J. M. S., 2000, J. Biotechnol., 79, 230
- Hermansson A. M., 1994, Protein structure−function relationships in foods, 42
- 1980, AOAC Official methods of analysis
- Hermansson A.-M., 1973, Functional properties of proteins for foods − Solubility. Bilaga till Halvarsskrift
- Shen J. L, 1976, J. Agric. Food Chem., 24, 788, 10.1021/jf60206a036 · DOI
- Hermansson A.-M, 1978, J. Texture Stud., 9, 58
- Wongprecha T., 2000, Hydrocolloids-Part 1. Physical Chemistry and Industrial Application of Gels, Polysaccharides, and Proteins, 377
- Privalov P. L, 1979, Adv. Protein Chem., 33, 241
- German B., 1982, J. Agric. Food Chem., 30, 811, 10.1021/jf00113a002 · DOI
- Utsumi S., 1987, Agric. Biol. Chem., 51, 2144
- van Vliet T., 1991, Colloid Polymer Sci., 269, 627, 10.1007/BF00659917 · DOI
- Verheul M., 1998, Langmuir, 14, 2268, 10.1021/la9708187 · DOI
- Renkema J. M. S., 2001, Relations between rheological properties and network structure of soy protein gels. Submitted for publication
- Doi E., 1989, Food Hydrocolloids, 3, 337
- Tanford C., 1961, Physical Chemistry of Macromolecules
- Yamagishi T., 1987, Cereal Chem., 64, 212
- Wolf W. J., 1969, Cereal Chem., 46, 344
- Hashizume K., 1975, Agric. Biol. Chem., 39, 1347
- Damodaran S., 1982, J. Agric. Food Chem., 30, 817, 10.1021/jf00113a003 · DOI
- Yamagishi T., 1983, Agric. Biol. Chem., 47, 1237
- Utsumi S., 1984, J. Agric. Food Chem., 32, 1412, 10.1021/jf00126a047 · DOI
- Mori T., 1981, J. Food Sci., 47, 30
- Yamauchi F., 1991, Food Rev. Int., 7, 322, 10.1080/87559129109540914 · DOI
Cited by
Sorted by citations
Soy protein isolates: A review of their composition, aggregation, and gelation.
Zheng, L., Regenstein, J. M., Zhou, L., & Wang, Z. (2022) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12925 · Cited by 266
Gelation of food protein-protein mixtures.
Nicolai, T. (2019) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2019.06.006 · Cited by 263
Sensitivity of oat protein solubility to changing ionic strength and pH
Li, R., & Xiong, Y. L. (2021) · Journal of Food Science · doi:10.1111/1750-3841.15544 · Cited by 91
A Review of Gelation of Plant Proteins and Their Influencing Factors
Hui, D., Liang, W., Wang, R., Feng, X., & Tang, X. (2025) · Sustainable Food Proteins · doi:10.1002/sfp2.70037 · Cited by 12
Metadata
- Authors
- Renkema, J. M. S., Gruppen, H., & van Vliet, T.
- Affiliations
- Wageningen University & Research (NL)
- Corresponding author
- van Vliet, Ton
- Venue
- Journal of Agricultural and Food Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2002-09-07
- Volume
- 50
- Issue
- 21
- Pages
- 6064-6071
- ISSN
- 0021-8561 (ISSN-L)
- 1520-5118
- OpenAlex
- W1996048374
- Cited by
- 262
- References
- 0
- Citations by year
- 2026: 18 · 2025: 15 · 2024: 23 · 2023: 17 · 2022: 6 · 2021: 20 · 2020: 16 · 2019: 17 · 2018: 12 · 2017: 9 · 2016: 13 · 2015: 12 · 2014: 8 · 2013: 6 · 2012: 11
- FWCI
- 6.84
- Type
- journal article
- Language
- en
- Open access
- green
- research.wur.nl
- Locations
- Journal of Agricultural and Food Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Socio-Environmental Systems Modeling (acceptedVersion)
- TNO Repository (submittedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Agricultural and Biological Sciences › Food Science › Polysaccharides Composition and Applications
- Health Sciences › Nursing › Nutrition and Dietetics › Food composition and properties
- Keywords
- soy protein isolate, heat-induced gelation, protein denaturation, pH effect, ionic strength, gel rheology, gel stiffness, protein aggregation, protein precipitation, protein network structure, acidic polypeptides, protein composition
- MeSH terms
- Calorimetry, Differential Scanning, Electrophoresis, Polyacrylamide Gel, Gels, Hot Temperature, Hydrogen-Ion Concentration, Osmolar Concentration, Chemical Precipitation, Protein Denaturation, Rheology, Solubility, Soybean Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review