Sirison, Jiraporn

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Sirison, Jiraporn
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jiraporn.si@kmitl.ac.th

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    Item type:Publication,
    Solubility of soy lipophilic proteins: Comparison with other soy protein fractions
    (2017-01-01)
    Sirison, Jiraporn
    ;
    Matsumiya, Kentaro
    ;
    Samoto, Masahiko
    ;
    Hidaka, Hiroshi
    ;
    Kouno, Mitsutaka
    Solubility of soy lipophilic proteins (LP) was studied as compared with that of other soy protein fractions. LP, ß-conglycinin, glycinin, and soy protein isolate (N-SPI) were prepared under the condition to avoid heat denaturation. Solubility of LP was lower than that of other soy protein fractions under all the tested conditions varying in pH values and ionic strength. The solubility of LP was increased constantly by elevating temperature until 90 °C, whereas that of ß-conglycinin and glycinin dropped at high temperature. Temperature-dependent change in solubility of N-SPI might reflect the balance among that of glycinin, ß-conglycinin and LP. Based on the results of SDS-PAGE, determination of phospholipid content and Fourier Transform Infrared spectroscopy, we discussed the solubilization behavior of LP relating to its origin and composition.
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    Item type:Publication,
    Soybean lipophilic proteins — Origin and functional properties as affected by interaction with storage proteins
    (2017-03-01)
    Matsumura, Yasuki
    ;
    Sirison, Jiraporn
    ;
    Ishi, Toya
    ;
    Matsumiya, Kentaro
    Soy protein isolate (SPI) is a typical commercial product of soybean, widely used as a food ingredient. SPI has long been thought to consist of two major storage proteins, namely, glycinin and β-conglycinin. However, the finding of new protein fractions, lipophilic proteins (LP), which occupy about 30% of SPI, requires us to reconsider the composition and functional properties of SPI. In this review, we consider the origin of LP and its interaction with the two storage proteins referring to recent results on the solubility of LP, glycinin, β-conglycinin, and SPI. The importance of the interaction between LP and the storage proteins is also highlighted by comparing our results with those previously published on the emulsifying properties of LP. The major component of LP is a complex of oleosin-phospholipids, and this complex forms a strong membrane surrounding the oil body in soybean seeds. The possibility of using the oil body as an emulsifying agent is also discussed, and the importance of the interaction between LP and storage proteins is highlighted.