作者: Jian-Hua Ren , Shun-Tang Guo
DOI: 10.1016/J.CCLET.2013.04.025
关键词: Pepsin 、 Trypsin 、 Digestion 、 β conglycinin 、 Enzyme 、 In vitro 、 Hydrolysate 、 Chromatography 、 Chemistry 、 In vitro digestion
摘要: Abstract The in vitro digestibility of alcalase enzymatic hydrolysates β -conglycinin was studied. results showed that the zeta potentials decreased and their electronegativity increased when digested with pepsin trypsin. Furthermore, content peptides molecular weight from 10 kDa to 20 kDa remained stable, while those higher (>20 kDa) decreased, lower ( digestion, but no significant change surface hydrophobicity indices digestion products observed P were degraded through degree degradation relatively low. Peptides resisted by trypsin they stable during processes.