Sirison, Jiraporn
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Item type:Publication, Salad cream formulated with tofu and coconut oil(2017-01-01); ;Rirermwong, Awika ;Tanwisuit, NattawadeeMeaksan, TaviyapornPurpose: The purpose of this paper is to develop a new salad cream formulation from a mixture of tofu and coconut oil for replacement of egg yolk and soy oil, respectively. Design/methodology/approach: A salad cream formulation mainly composing of edible oil, egg and vinegar was formulated. Ratios of egg yolk and soy oil were replaced by tofu and coconut oil, respectively. The formulated salad creams were determined for pH, color, viscosity, protein and fat. Sensory acceptances of formulated products was evaluated by using a seven-point hedonic scale test and untrained panelists (n=30). The formulated salad creams were stored in a refrigerator for 14 days and determined for pH, color and viscosity. Findings: The results showed that the formulated salad creams using the mixture of 50 percent tofu and 50 percent egg yolk (RE) by weight of egg yolk ratio in control presented 4.25+0.01 of pH which was comparable to control. The highest scores in the sensory test were obtained in the formula using 37 percent coconut oil by weight of salad cream. The formulated salad creams using tofu and coconut oil (REC) presented 4.42+0.03 of pH, 4.25+0.05 cm. of viscosity, and 87.36+0.44 (L), −1.13+0.04 (a), 16.32+0.22 (b) of color values. Protein and fat contents were 4.79 and 27.59 percent (w/w) in the REC, respectively. After storage under refrigerated, pH, color and viscosity of the modified product were less changed. Originality/value: Replacement of egg yolk and soy oil with tofu and coconut oil in salad creams was feasible. The REC was less changed in its quality both fresh and after storage. It was accepted in sensory evaluation. The REC could prepare at home and being a food choice for consumers. - Some of the metrics are blocked by yourconsent settings
Item type:Publication, Solubility of soy lipophilic proteins: Comparison with other soy protein fractions(2017-01-01); ;Matsumiya, Kentaro ;Samoto, Masahiko ;Hidaka, HiroshiKouno, MitsutakaSolubility 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. - Some of the metrics are blocked by yourconsent settings
Item type:Publication, Soybean lipophilic proteins — Origin and functional properties as affected by interaction with storage proteins(2017-03-01) ;Matsumura, Yasuki; ;Ishi, ToyaMatsumiya, KentaroSoy 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.
