The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Comparison of Physicochemical Properties of 7S and 11S Globulins from Pea, Fava Bean, Cowpea, and French Bean with Those of Soybean—French Bean 7S Globulin Exhibits Excellent Properties
Abstract
Legume seeds contain 7S and/or 11S globulins as major storage proteins. The amino acid sequences of them from many legumes are similar to each other in the species but different from each other, meaning that some of these proteins from some crops exhibit excellent functional properties. To demonstrate this, we compared protein chemical and functional properties (thermal stability, surface hydrophobicity, solubility as a function of pH, and emulsifying properties) of these proteins from pea, fava bean, cowpea, and French bean with those of soybean as a control at the same conditions. The comparison clearly indicated that the 7S globulin of French bean exhibited excellent solubility (100%) at pH 4.2-7.0 even at a low ionic strength condition (mu = 0.08) and excellent emulsion stability (a little phase separation after 3 days) at pH 7.6 and mu = 0.08, although the emulsions from most of the other proteins separated in 1 h. These results indicate that our assumption is correct.
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Cites
Nakai, S. (1983) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf00118a001 · Cited by 421
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Aguilar-Padilla, J., Centeno-Leija, S., Bojórquez-Velázquez, E., Elizalde-Contreras, J. M., Ruiz-May, E., Serrano-Posada, H., & Osuna-Castro, J. A. (2023) · Foods · doi:10.3390/foods12030461 · Cited by 9
Metadata
- Authors
- Kimura, A., Fukuda, T., Zhang, M., Motoyama, S., Maruyama, N., & Utsumi, S.
- Venue
- Journal of Agricultural and Food Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2008-10-02
- Volume
- 56
- Issue
- 21
- Pages
- 10273-10279
- ISSN
- 0021-8561 (ISSN-L)
- 1520-5118
- OpenAlex
- W2078406808
- Cited by
- 262
- References
- 1
- FWCI
- 8.14
- Type
- journal article
- Language
- en
- Open access
- closed
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