The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Relationships of Hydrophobicity and Net Charge to the Solubility of Milk and Soy Proteins
Abstract
Protein hydrophobicity of 42 native and partially denatured milk and soy protein samples was determined fluorometrically by using three probes, 1‐anilino‐8‐naphthalenesulfonate (ANS), cis‐parinarate (CPA) and 1,6‐diphenyl hexatriene (DPH), and chromatographically by using Phenyl Sepharose CL‐4B (PSC). PSC and ANS hydro‐ phobicities correlated well to the protein insolubility determined at zero zeta potential, whereas no significant correlation was observed between CPA. hydrophobicity and protein insolubility. When backwards stepwise regression analysis was applied to 189 data of protein insolubility, a significant correlation (P < 0.001) was obtained between PSC hydrophobicity, zeta potential and protein insolubility. It is suggested that the aromatic hydrophobicity, in conjunction with zeta potential, may play a more important role in protein solublity than the aliphatic hydrophobicity.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Soybean proteins. Their functional, chemical, and physical properties
Wolf, W. J. (1970) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf60172a025 · Cited by 394
Research works printed but not linked: 42
- 10.1111/j.1365-2621.1980.tb04095.x · DOI
- 10.1016/0022-5193(67)90004-5 · DOI · Paper page
- Burley R.W., 1983, Hydrophobic chromatography of proteins in urea solutions. The separation of apoproteins from a lipoprotein of avian egg yolk, Biochem. J., 209, 143, 10.1042/bj2090143 · DOI
- 10.1002/bit.260240817 · DOI
- Chen J‐L., 1981, Affinity electronhoresis in zels containing hydrophobic substituents, J. Bibl. Chem:, 256, 9221, 10.1016/S0021-9258(19)52532-7 · DOI
- 10.1016/S0021-9673(01)88415-6 · DOI
- 10.1016/S0021-9673(01)85223-7 · DOI
- 10.1021/ja00460a031 · DOI
- 10.1016/0005-2795(80)90220-2 · DOI · Paper page
- 10.1271/bbb1961.47.33 · DOI
- 10.1021/jf00122a027 · DOI
- 10.1080/10408397609527208 · DOI · Paper page
- Kruyt H.R., 1952, “Coiloid Science
- 10.1042/bj0510168 · DOI
- 10.1111/j.1365-2621.1984.tb12418.x · DOI
- 10.1016/S0021-9258(19)52451-6 · DOI · Paper page
- Mahoney W.C., 1980, Separation of large denatured peptides by reverse phase high performance liquid chromatography. Trifluoroacetic acid as a peptide solvent, J. Biol. Chem., 255, 11199, 10.1016/S0021-9258(19)70275-0 · DOI · Paper page
- 10.1021/jf00119a013 · DOI
- McGowen J.C., 1979, Relationships between the solubiiity of amino acids, J. Appl. Biochem., 1, 423
- 10.1111/j.1365-2621.1979.tb08497.x · DOI
- 10.1016/0003-9861(77)90434-9 · DOI · Paper page
- 10.1016/S0315-5463(80)73297-2 · DOI
- Nozaki T., 1971, The solubihty of amino acids and two giycine peptides rn aqueous ethanol and dioxane solutions, J. Biol. Chem., 246, 2211, 10.1016/S0021-9258(19)77210-X · DOI · Paper page
- 10.1016/0006-3002(60)90153-0 · DOI
- Rekker R.F., 1977, “The Hydrophobic Fragmental Constant,”
- 10.1021/bi00855a038 · DOI · Paper page
- 10.1021/bi00844a016 · DOI
- 10.1021/ja01157a138 · DOI · Paper page
- 10.1111/j.1432-1033.1975.tb20970.x · DOI
- 10.1007/BF02660208 · DOI
- 10.1093/chromsci/16.6.223 · DOI
- Tanford C., 1973, “The Hydrophobic Effect: Formaton of Miceiles and Biological Membranes,”
- 10.1021/jf60208a030 · DOI · Paper page
- 10.3168/jds.S0022-0302(66)87947-X · DOI
- 10.1111/j.1365-2621.1983.tb10796.x · DOI
- 10.1111/j.1365-2621.1983.tb14781.x · DOI
- 10.1016/S0315-5463(83)72205-4 · DOI
- 10.1021/jf00115a015 · DOI
- 10.1016/S0021-9258(18)91331-1 · DOI · Paper page
- 10.1042/bj1990031 · DOI
- Wishnia A., 1966, Hydrophobic‐interactions in proteins, The alkane bhding site of plactoglobulins A and B. Biochemistry, 5, 1534
- 10.3168/jds.S0022-0302(63)89242-5 · DOI · Paper page
Cited by
Plant protein solubility: A challenge or insurmountable obstacle.
Gao, K., Rao, J., & Chen, B. (2024) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2023.103074 · Cited by 150
Functional Properties of Improved Glycinin and β-nglycinin Fractions
Rickert, D. A., Johnson, L. A., & Murphy, P. A. (2004) · Journal of Food Science · doi:10.1111/j.1365-2621.2004.tb06332.x · Cited by 116
Liu, M., Shan, S., Gao, X., Shi, Y., & Lu, W. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.124344 · Cited by 115
Ultrasound-induced structural modification and thermal properties of oat protein
Li, R., & Xiong, Y. L. (2021) · LWT · doi:10.1016/j.lwt.2021.111861 · Cited by 112
Gulzar, S., Martín-Belloso, O., & Soliva-Fortuny, R. (2024) · Foods · doi:10.3390/foods13030376 · Cited by 60
Metadata
- Authors
- HAYAKAWA, S., & NAKAI, S.
- Venue
- Journal of Food Science
- Publisher
- Wiley
- Published
- 1985-03
- Volume
- 50
- Issue
- 2
- Pages
- 486-491
- ISSN
- 0022-1147 (ISSN-L)
- 1750-3841
- OpenAlex
- W1973087371
- Cited by
- 506
- References
- 1
- FWCI
- 12.53
- Type
- journal article
- Language
- en
- Open access
- closed
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
