title: Solubility of soy lipophilic proteins: comparison with other soy protein fractions.
abstract: Solubility of soy lipophilic proteins (LP) was studied as compared with that of other soy protein fractions. LP, β-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 β-conglycinin and glycinin dropped at high temperature. Temperature-dependent change in solubility of N-SPI might reflect the balance among that of glycinin, β-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.
authors.affiliation: c Faculty of Agro-Industry , King Mongkut's Institute of Technology Ladkrabang , Bangkok , Thailand.
authors.forename: Jiraporn
authors.initials: J
authors.lastname: Sirison
authors.affiliation: a Laboratory of Quality Analysis and Assessment, Division of Agronomy and Horticultural Science, Graduate School of Agriculture , Kyoto University , Kyoto , Japan.
authors.forename: Kentaro
authors.initials: K
authors.lastname: Matsumiya
authors.affiliation: b R&D Division for Future Creation , Fuji Oil Holdings INC , Tsukubamirai-shi , Japan.
authors.forename: Masahiko
authors.initials: M
authors.lastname: Samoto
authors.affiliation: b R&D Division for Future Creation , Fuji Oil Holdings INC , Tsukubamirai-shi , Japan.
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Hidaka
authors.affiliation: b R&D Division for Future Creation , Fuji Oil Holdings INC , Tsukubamirai-shi , Japan.
authors.forename: Mitsutaka
authors.initials: M
authors.lastname: Kouno
authors.affiliation: a Laboratory of Quality Analysis and Assessment, Division of Agronomy and Horticultural Science, Graduate School of Agriculture , Kyoto University , Kyoto , Japan.
authors.forename: Yasuki
authors.initials: Y
authors.lastname: Matsumura
mesh_terms: D052179:Antigens, Plant / Q000737:chemistry*; D005916:Globulins / Q000737:chemistry*; D006358:Hot Temperature; D011489:Protein Denaturation; D055314:Seed Storage Proteins / Q000737:chemistry*; D012995:Solubility; D030262:Soybean Proteins / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D052179:Antigens, Plant; D005916:Globulins; D055314:Seed Storage Proteins; D030262:Soybean Proteins; C013894:beta-conglycinin protein, Glycine max; C011474:glycinin
keywords: glycinin; membrane-associated proteins; solubility; soy lipophilic proteins; β-congycinin