Solubility of soy lipophilic proteins: comparison with other soy protein fractions

被引:36
|
作者
Sirison, Jiraporn [3 ]
Matsumiya, Kentaro [1 ]
Samoto, Masahiko [2 ]
Hidaka, Hiroshi [2 ]
Kouno, Mitsutaka [2 ]
Matsumura, Yasuki [1 ]
机构
[1] Kyoto Univ, Grad Sch Agr, Div Agron & Hort Sci, Lab Qual Anal & Assessment, Kyoto, Japan
[2] Fuji Oil Holdings INC, R&D Div Future Creat, Tsukubamirai, Japan
[3] King Mongkuts Inst Technol Ladkrabang, Fac Agroind, Bangkok, Thailand
关键词
soy lipophilic proteins; solubility; glycinin; -congycinin; membrane-associated proteins; TRANSFORM INFRARED-SPECTROSCOPY; SOYBEAN BETA-CONGLYCININ; OIL BODIES; FUNCTIONAL-PROPERTIES; SECONDARY STRUCTURE; EMULSIFYING PROPERTIES; THERMAL-DENATURATION; SELF-DECONVOLUTION; MEMBRANE-PROTEINS; GELATION PROCESS;
D O I
10.1080/09168451.2017.1282808
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Solubility of soy lipophilic proteins (LP) was studied as compared with that of other soy protein fractions. LP, -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 degrees C, whereas that of -conglycinin and glycinin dropped at high temperature. Temperature-dependent change in solubility of N-SPI might reflect the balance among that of glycinin, -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.
引用
收藏
页码:790 / 802
页数:13
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