作者: Qiuyue Pan , Bing Zhou , Lei Liu , Lei Wang , Fang Yuan
DOI: 10.1016/J.FOODRES.2014.06.036
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摘要: Abstract In this study the interaction between soy protein isolate (SPI) and Bifidobacterium was investigated to reveal protecting mechanism of SPI on Bifidobacterium. The results indicated that average particle size aggregate longum (B. longum, better surface hydrophobicity four Bifidobacterium) exhibited more considerable expansion than alone, from 295.9 nm 404.8 nm (the aggregate). It confirmed B. localized in microparticle core, while acted as a wall-coating material, determined by zeta potential laser scanning confocal microscopy (LSCM). Surface hydrophobicity, which described fluorescence intensity, decreased 72% SPI. main binding force originated hydrophobic verified isothermal titration calorimetry (ITC). enthalpy (ΔH) ITC be − 3.24 kJ mol− 1 for adsorption at 25 °C pH 7.0. Furthermore, aggregation testified an endothermic process, process spontaneous irreversible. forces interpreted has useful food ingredient probiotics.