Sirison, Jiraporn

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

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    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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    Comparison of surface and foaming properties of soy lipophilic protein with those of glycinin and β-conglycinin
    (2021-03-01)
    Sirison, Jiraporn
    ;
    Ishii, Toya
    ;
    Matsumiya, Kentaro
    ;
    Samoto, Masahiko
    ;
    Kohno, Mitsutaka
    Soy lipophilic protein (LP) is considered to form a major fraction of soy protein isolate, in addition to β-conglycinin (7 S) and glycinin (11 S). LP consists of phospholipid-protein complex and phospholipid-free protein molecules. Surface and foaming properties of LP were compared to those of 7 S and 11 S. These soy protein samples were prepared under mild conditions in order to avoid thermal denaturation, which enabled us to study the effects of heat treatment on surface and foaming properties of the proteins. Without heat treatment, the surface and foaming properties of LP were superior to those of other soy protein fractions, suggesting the phospholipid-protein complex in LP can produce fine bubbles with high drainage stability. Despite low surface and foaming properties of non-heated 7 S and 11 S, heat treatment improved the surface and foaming properties of 7 S and 11 S dramatically, which could be relevant to heat-induced changes in particle size, zeta-potential and surface hydrophobicity of 7 S and 11 S molecules. On the other hand, the foaming ability of LP was declined, but the foam stability was increased to maintain the foam volume up to the final stage of observation, by heating. In the foam stabilized by heated LP, medium sized bubbles as well as fine bubbles were produced. The improved foam stability may be attributed to the combination effect of the delayed drainage from the lamellar phase of fine bubbles and the increased resistance to the bursting of medium sized bubble.
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    Tuning of rheological behavior of soybean lipophilic protein-stabilized emulsions
    (2023-08-01)
    Sirison, Jiraporn
    ;
    Ishii, Toya
    ;
    Matsumiya, Kentaro
    ;
    Higashino, Yuki
    ;
    Nambu, Yuko
    Soy lipophilic protein (LP) is a protein fraction mainly composed of a phospholipid-protein complex isolated from defatted soy meal. This work investigated effects of seasoning materials, i.e., NaCl, sucrose, and acetic acid, on rheological properties of LP-stabilized O/W emulsions. LP dispersions in water were homogenized with soybean oil to create LP-stabilized emulsions of which added oil was 50 wt%. LP emulsions immediately flocculated but resisted coalescence at least for 8 weeks. An addition of NaCl and sucrose separately decreased emulsion viscosity probably due to salting-in and hydration effects, respectively. LP emulsions initially in a liquid form at pH 7.2 became semisolid at pH 5.7 by stepwise acidification, and thereafter returned to liquid by further acidification below pH 4.2. The drastic change was attributed to insufficient inter-droplet electrostatic repulsion within the pH range (pH 5.7–4.2) according to the zeta-potential analysis. The storage modulus (G′) of the solidified emulsions was higher than the loss modulus (G″) and not strongly dependent on frequency, indicating internal network structure. Cryo-SEM clarified that acidification neither caused more inhomogeneous distribution nor promoted coalescence of oil droplets, revealing that the acid-induced solidification resulted from enhanced non-covalent interactions between contacted and packed oil droplets. The solidified emulsion was stable against coalescence for at least 8 weeks under a commercial shelf-life condition. These findings show that LP can create stable emulsions highly tunable regarding rheological behavior, thereby emphasizing potential of LP for application to various food emulsion products varying in texture from liquid to semisolid.
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    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.