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Microbial transglutaminase-induced polymerization of 尾-conglycinin and glycinin in soymilk: A proteomics approach
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文摘
This study investigated the microbial transglutaminase (MTGase)-induced polymerization of 尾-conglycinin (7S) and glycinin (11S) in soymilk at 30聽掳C. SDS-PAGE analysis showed that the 7S acidic proteins, 11S acidic proteins and a portion of the 11S basic proteins were polymerized by MTGase (2.0 units mL鈭?) during 2聽h of incubation. The intensities of the protein bands corresponding to the 7S 伪鈥? 7S 伪, 7S 尾, and 11S A3 acidic subunits and the 11S basic proteins decreased from 34.4聽卤聽3.6, 86.8聽卤聽15.6, 68.4聽卤聽6.3, 27.3聽卤聽3.7, 224.9聽卤聽27.2, and 239.8聽卤聽26.8 arbitrary units (A.U.) to 7.7聽卤聽1.5, 3.5聽卤聽2.7, 13.1聽卤聽0.9, 3.8聽卤聽0.7, 15.2聽卤聽3.5, and 110.0聽卤聽18.9 A.U., respectively, during that period. Components with higher molecular weights were observed after 2聽h of incubation, indicating that inter- or intramolecular crosslinking occurred among the 7S and 11S proteins in the MTGase-treated soymilk. SDS-PAGE and two-dimensional electrophoretic analysis indicated that a portion of the 7S (伪鈥? 伪, and 尾), 11S acidic (A1a, A1b, A2, A3, and A4), and 11S basic (B1a, B1b, and B3) proteins in the soymilk were polymerized during incubation with MTGase (1.0 units mL鈭?). The MTGase-induced polymerization occurred more rapidly for the 7S (伪鈥? 伪, and 尾) and 11S acidic (A1a, A1b, A2, A3, and A4) proteins than for the 11S basic (B1a, B1b, and B3) proteins.

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