The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Relationship between Secondary Structure and Surface Hydrophobicity of Soybean Protein Isolate Subjected to Heat Treatment
Open accessAbstract
This study investigated relationship between secondary structure and surface hydrophobicity of soy protein isolate (SPI) subjected to a thermal treatment at 70~90°C. Heat denaturation increased the surface hydrophobicity and surface hydrophobicity decreased as aggregate formed. Heat caused an increase in the relative amount of α-helix structures and an overall decrease in the amount of β-sheet structures when compared with nontreated SPI. The relative amounts of secondary structures varied with time, temperature, and intensity of heat treatment applied. The β-sheet structure was most important for its significant role in denaturation of 7S globulin and following formed aggregates and even in denaturation of 11S globulin. The amount of β-sheet structure in SPI had an inverse correlation with the surface hydrophobicity when the temperature was kept below 90°C. Besides,β-turn structure increased as β-7S/B-11S aggregate formated.
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Metadata
- Authors
- Wang, Z., Li, Y., Jiang, L., Qi, B., & Zhou, L.
- Venue
- Journal of Chemistry
- Publisher
- Wiley
- Published
- 2014
- Volume
- 2014
- Pages
- 1-10
- ISSN
- 2090-9063 (ISSN-L)
- 2090-9071
- OpenAlex
- W2011483199
- Cited by
- 342
- References
- 35
- FWCI
- 9.56
- Type
- journal article
- Language
- en
- Open access
- gold
- Funders
- National Natural Science Foundation of China (31071493, nycytx-004)
- Ministry of Agriculture of Modern Technology System Projects the Soybean Industry (31071493, nycytx-004)
- The National Research Center of Soybean Engineering and Technology (31071493, nycytx-004)
- Northeast Agricultural University (31071493, nycytx-004)
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