摘要
以牛血清白蛋白(BSA)和鸡蛋白蛋白(albumin)为模型蛋白，研究了热变性对蛋白质起泡性能和分子结构的影响. 结果表明，热变性后的BSA起泡能力下降，泡沫稳定性有增强的趋势. 热变性使BSA分子表面巯基含量下降，分子之间发生缔合，表面疏水性下降. 而albumin在热变性后的起泡能力及泡沫稳定性都大大提高，热变性使albumin分子展开，表面巯基含量增加. 实验证明，蛋白质分子的表面疏水性是决定其起泡能力的重要因素之一，蛋白质分子之间的相互作用对泡沫的稳定性有很大的影响.
The effect of heat-denature on the foaming properties and molecular structure was studied by using BSA and albumin as model proteins. The results showed that the foaming capability of BSA was decreased and foam stability was increased by heat-denature. The content of hydrosulfide group was reduced with lower surface hydrophobicity of BSA molecules, which suggested that bisulfide bond occurred between different BSA protein molecules. However, both foaming capability and foam stability of albumin were improved and albumin molecules unfolded showing more hydrosulfate exposed to solvent after heat-denature. Hence, surface hydrophobicity may be one of the most important factors determining the foaming capability of proteins, and protein-protein interactions play key roles as the foam stability is concerned.
出处
《化工冶金》
EI
CSCD
北大核心
2000年第4期379-383,共5页
基金
国家自然科学重点基金资助项目!(编号:29836130)
